asparaginyl-tRNA synthase (glutamine-hydrolysing)
Pathways
glutamate and glutamine metabolism (BRENDA)
:= BRENDA, := KEGG, := MetaCyc, := SABIO-RK
:= amino acid sequences := show the reaction diagram
EC Number
Reaction
Pathways
Reaction IDs
Stoichiometry Check
Missing Substrate
Missing Product
Commentary
Remark
ATP + L-glutamyl-tRNAGln + L-glutamine = ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
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natural substrates
glutaminyl-tRNA synthase (glutamine-hydrolysing)
ATP + L-glutamyl-tRNAGln + L-glutamine = ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
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natural substrates
succinate-semialdehyde dehydrogenase [NAD(P)+]
succinate semialdehyde + NADP+ + H2O = succinate + NADPH + H+
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: NADH (see R00713)
natural substrates
succinate-semialdehyde dehydrogenase (NAD+)
succinate semialdehyde + NADP+ + H2O = succinate + NADPH + H+
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: NADH (see R00713)
natural substrates
2,5-dioxovalerate dehydrogenase
succinate semialdehyde + NADP+ + H2O = succinate + NADPH + H+
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: NADH (see R00713)
natural substrates
succinate-semialdehyde dehydrogenase (NADP+)
succinate semialdehyde + NADP+ + H2O = succinate + NADPH + H+
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: NADH (see R00713)
natural substrates
aldose reductase
succinate semialdehyde + NADP+ + H2O = succinate + NADPH + H+
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: NADH (see R00713)
natural substrates
6-aminohexanoate aminotransferase
4-aminobutanoate + pyruvate = succinate semialdehyde + L-alanine
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natural substrates
beta-alanine-pyruvate transaminase
4-aminobutanoate + pyruvate = succinate semialdehyde + L-alanine
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natural substrates
4-aminobutyrate-2-oxoglutarate transaminase
4-aminobutanoate + pyruvate = succinate semialdehyde + L-alanine
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natural substrates
(R)-3-amino-2-methylpropionate-pyruvate transaminase
4-aminobutanoate + pyruvate = succinate semialdehyde + L-alanine
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natural substrates
4-aminobutyrate-pyruvate transaminase
4-aminobutanoate + pyruvate = succinate semialdehyde + L-alanine
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natural substrates
isocitrate lyase
(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
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: multi-step reaction (see R03153+R00237)
natural substrates, multi-step reaction
citramalate lyase
(2S)-2-hydroxy-2-methylbutanedioate = acetate + pyruvate
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: multi-step reaction (see R03153+R00237)
natural substrates, multi-step reaction
fumarate hydratase
(S)-2-Methylmalate = 2-methylfumarate + H2O
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natural substrates
(S)-2-methylmalate dehydratase
(S)-2-Methylmalate = 2-methylfumarate + H2O
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natural substrates
methylaspartate ammonia-lyase
L-threo-3-methylaspartate = mesaconate + NH3
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natural substrates
methylaspartate mutase
L-threo-3-methylaspartate = L-glutamate
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natural substrates
propionate CoA-transferase
butyryl-CoA + acetate = acetyl-CoA + butanoate
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natural substrates
5-hydroxypentanoate CoA-transferase
butyryl-CoA + acetate = acetyl-CoA + butanoate
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natural substrates
acetate CoA-transferase
butyryl-CoA + acetate = acetyl-CoA + butanoate
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natural substrates
butyrate-acetoacetate CoA-transferase
butyryl-CoA + acetate = acetyl-CoA + butanoate
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natural substrates
acyl-CoA dehydrogenase (NADP+)
crotonyl-CoA + reduced acceptor = butyryl-CoA + oxidized acceptor
: BS370908
generic compounds
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natural substrates, generic
short-chain acyl-CoA dehydrogenase
crotonyl-CoA + reduced acceptor = butyryl-CoA + oxidized acceptor
: BS370908
generic compounds
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natural substrates, generic
7.2.4.5
glutaconyl-CoA decarboxylase
(2E)-4-carboxybut-2-enoyl-CoA + Na+[side 1] = (2E)-but-2-enoyl-CoA + CO2 + Na+[side 2]
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natural substrates
(R)-2-hydroxyglutaryl-CoA = (E)-glutaconyl-CoA + H2O
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natural substrates
(R)-2-hydroxyglutaryl-CoA dehydratase
(R)-2-hydroxyglutaryl-CoA = (E)-glutaconyl-CoA + H2O
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natural substrates
aspartate ammonia-lyase
L-aspartate = fumarate + NH3
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natural substrates
methylaspartate ammonia-lyase
L-aspartate = fumarate + NH3
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natural substrates
2-oxoglutaramate amidase
2-oxoglutaramate + H2O = 2-oxoglutarate + NH3
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natural substrates
omega-amidase
2-oxoglutaramate + H2O = 2-oxoglutarate + NH3
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natural substrates
N-methyl-2-oxoglutaramate hydrolase
2-oxoglutaramate + H2O = 2-oxoglutarate + NH3
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natural substrates
glutamine-pyruvate transaminase
L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine
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natural substrates
serine-pyruvate transaminase
L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine
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natural substrates
amino-acid racemase
L-glutamate = D-glutamate
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natural substrates
glutamate racemase
L-glutamate = D-glutamate
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natural substrates
arginine racemase
L-glutamate = D-glutamate
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natural substrates
tryptophanyl aminopeptidase
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
asparaginase
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
glutaminase
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
glutamin-(asparagin-)ase
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
peptidyl-glutaminase
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
protein-glutamine glutaminase
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
imidazole glycerol phosphate synthase
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
imidazole glycerol-phosphate synthase
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
pyridoxal 5'-phosphate synthase (glutamine hydrolysing)
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
CTP synthase (glutamine hydrolysing)
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
lipid II isoglutaminyl synthase (glutamine-hydrolysing)
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
GMP synthase (glutamine-hydrolysing)
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
asparagine synthase (glutamine-hydrolysing)
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
carbamoyl-phosphate synthase (glutamine-hydrolysing)
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
asparaginyl-tRNA synthase (glutamine-hydrolysing)
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
glutaminyl-tRNA synthase (glutamine-hydrolysing)
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
gamma-glutamyltransferase
L-glutamine + H2O = L-glutamate + NH3
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: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
L-glutamine + H2O = L-glutamate + NH3
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-
-
: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
amidophosphoribosyltransferase
L-glutamine + H2O = L-glutamate + NH3
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-
-
: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
4-amino-4-deoxychorismate synthase (2-amino-4-deoxychorismate-forming)
L-glutamine + H2O = L-glutamate + NH3
-
-
-
: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
aminodeoxychorismate synthase
L-glutamine + H2O = L-glutamate + NH3
-
-
-
: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
glutamate synthase (NADPH)
L-glutamine + H2O = L-glutamate + NH3
-
-
-
: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
glutamate synthase (NADH)
L-glutamine + H2O = L-glutamate + NH3
-
-
-
: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
glutamate synthase (ferredoxin)
L-glutamine + H2O = L-glutamate + NH3
-
-
-
: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
L-glutamine + H2O = L-glutamate + NH3
-
-
-
: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)
: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.
natural substrates
glutamine synthetase
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
-
-
-
-
natural substrates
glutamate synthase (ferredoxin)
2 L-glutamate + oxidized ferredoxin = L-glutamine + 2-oxoglutarate + reduced ferredoxin + 2 H+
-
-
-
: two-step reaction (see R00256+R10086)
natural substrates, generic, protein
glutamate synthase (NADPH)
2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+
-
-
-
-
natural substrates
glutamate synthase (NADH)
2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+
-
-
-
-
natural substrates
glutamate synthase (NADPH)
2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+
-
-
-
: two-step reaction (see R00256+R00248)
natural substrates
glutamate synthase (NAD(P)H)
2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+
-
-
-
: two-step reaction (see R00256+R00248)
natural substrates
glutamate synthase (NADPH)
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
-
-
-
: NADH (ec 1.4.1.3, see R00243)
natural substrates
glutamate dehydrogenase
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
-
-
-
: NADH (ec 1.4.1.3, see R00243)
natural substrates
aspartate dehydrogenase
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
-
-
-
: NADH (ec 1.4.1.3, see R00243)
natural substrates
glutamate dehydrogenase [NAD(P)+]
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
-
-
-
: NADH (ec 1.4.1.3, see R00243)
natural substrates
glutamate dehydrogenase (NADP+)
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
-
-
-
: NADH (ec 1.4.1.3, see R00243)
natural substrates
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
-
-
-
: NADH (ec 1.4.1.3, see R00243)
natural substrates
alanine dehydrogenase
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
: L-ornithine biosynthesis II,
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
: BR36868
: R00243
: GLUTAMATE-DEHYDROGENASE-NADP+-RXN_WOPThis reaction also exists with phosphate., GLUTAMATE-DEHYDROGENASE-RXN
: 755
-
-
-
: NADPH (ec 1.4.1.3 and 1.4.1.4, see R00248)
natural substrates
glutamate synthase (NADH)
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
: L-ornithine biosynthesis II,
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
: BR36868
: R00243
: GLUTAMATE-DEHYDROGENASE-NADP+-RXN_WOPThis reaction also exists with phosphate., GLUTAMATE-DEHYDROGENASE-RXN
: 755
-
-
-
: NADPH (ec 1.4.1.3 and 1.4.1.4, see R00248)
natural substrates
glutamate dehydrogenase
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
: L-ornithine biosynthesis II,
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
: BR36868
: R00243
: GLUTAMATE-DEHYDROGENASE-NADP+-RXN_WOPThis reaction also exists with phosphate., GLUTAMATE-DEHYDROGENASE-RXN
: 755
-
-
-
: NADPH (ec 1.4.1.3 and 1.4.1.4, see R00248)
natural substrates
aspartate dehydrogenase
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
: L-ornithine biosynthesis II,
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
: BR36868
: R00243
: GLUTAMATE-DEHYDROGENASE-NADP+-RXN_WOPThis reaction also exists with phosphate., GLUTAMATE-DEHYDROGENASE-RXN
: 755
-
-
-
: NADPH (ec 1.4.1.3 and 1.4.1.4, see R00248)
natural substrates
secondary-alkyl amine dehydrogenase [NAD(P)+]
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
: L-ornithine biosynthesis II,
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
: BR36868
: R00243
: GLUTAMATE-DEHYDROGENASE-NADP+-RXN_WOPThis reaction also exists with phosphate., GLUTAMATE-DEHYDROGENASE-RXN
: 755
-
-
-
: NADPH (ec 1.4.1.3 and 1.4.1.4, see R00248)
natural substrates
glutamate dehydrogenase [NAD(P)+]
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
: L-ornithine biosynthesis II,
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
: BR36868
: R00243
: GLUTAMATE-DEHYDROGENASE-NADP+-RXN_WOPThis reaction also exists with phosphate., GLUTAMATE-DEHYDROGENASE-RXN
: 755
-
-
-
: NADPH (ec 1.4.1.3 and 1.4.1.4, see R00248)
natural substrates
glutamate dehydrogenase (NADP+)
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
: L-ornithine biosynthesis II,
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
: BR36868
: R00243
: GLUTAMATE-DEHYDROGENASE-NADP+-RXN_WOPThis reaction also exists with phosphate., GLUTAMATE-DEHYDROGENASE-RXN
: 755
-
-
-
: NADPH (ec 1.4.1.3 and 1.4.1.4, see R00248)
natural substrates
L-amino-acid dehydrogenase
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
Alanine, aspartate and glutamate metabolism,
Taurine and hypotaurine metabolism,
Nitrogen metabolism,
Metabolic pathways,
Microbial metabolism in diverse environments
: L-ornithine biosynthesis II,
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
GABA shunt I,
L-glutamate biosynthesis II,
L-glutamate degradation X,
L-glutamate degradation V (via hydroxyglutarate),
L-glutamate degradation XI (reductive Stickland reaction),
4-aminobutanoate degradation V,
methylaspartate cycle,
ethene biosynthesis IV (engineered),
L-alanine degradation II (to D-lactate),
L-glutamate degradation I
: BR36868
: R00243
: GLUTAMATE-DEHYDROGENASE-NADP+-RXN_WOPThis reaction also exists with phosphate., GLUTAMATE-DEHYDROGENASE-RXN
: 755
-
-
-
: NADPH (ec 1.4.1.3 and 1.4.1.4, see R00248)
natural substrates
aspartate transaminase
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
: TCA cycle VIII (Chlamydia),
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
-
-
-
-
natural substrates
4-aminobutyrate-2-oxoglutarate transaminase
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
: TCA cycle VIII (Chlamydia),
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
-
-
-
-
natural substrates
alanine transaminase
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
: TCA cycle VIII (Chlamydia),
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
-
-
-
-
natural substrates
2-aminoadipate transaminase
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
: TCA cycle VIII (Chlamydia),
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
-
-
-
-
natural substrates
branched-chain-amino-acid transaminase
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
: TCA cycle VIII (Chlamydia),
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
-
-
-
-
natural substrates
tyrosine transaminase
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
: TCA cycle VIII (Chlamydia),
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
-
-
-
-
natural substrates
aromatic-amino-acid transaminase
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
: TCA cycle VIII (Chlamydia),
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
-
-
-
-
natural substrates
cysteine-conjugate transaminase
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
: TCA cycle VIII (Chlamydia),
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
-
-
-
-
natural substrates
aspartate-prephenate aminotransferase
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
: TCA cycle VIII (Chlamydia),
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
-
-
-
-
natural substrates
glutamate-prephenate aminotransferase
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
Alanine, aspartate and glutamate metabolism,
Carbon fixation in photosynthetic organisms,
Metabolic pathways,
Biosynthesis of secondary metabolites,
Microbial metabolism in diverse environments,
Carbon metabolism,
2-Oxocarboxylic acid metabolism,
Biosynthesis of amino acids
: TCA cycle VIII (Chlamydia),
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
C4 photosynthetic carbon assimilation cycle, PEPCK type,
C4 photosynthetic carbon assimilation cycle, NAD-ME type,
L-aspartate degradation I,
L-asparagine degradation III (mammalian),
anaerobic energy metabolism (invertebrates, cytosol),
L-aspartate biosynthesis,
L-glutamate degradation II,
malate/L-aspartate shuttle pathway
-
-
-
-
natural substrates
glutamate decarboxylase
L-glutamate = 4-aminobutanoate + CO2
-
-
-
-
natural substrates
tyrosine decarboxylase
L-glutamate = 4-aminobutanoate + CO2
-
-
-
-
natural substrates
sulfinoalanine decarboxylase
L-glutamate = 4-aminobutanoate + CO2
-
-
-
-
natural substrates
acetylornithine transaminase
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
-
-
-
-
natural substrates
beta-alanine—2-oxoglutarate transaminase
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
-
-
-
-
natural substrates
4-aminobutyrate-2-oxoglutarate transaminase
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
-
-
-
-
natural substrates
alanine transaminase
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
-
-
-
-
natural substrates
(S)-3-amino-2-methylpropionate transaminase
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
-
-
-
-
natural substrates
diamine transaminase
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
-
-
-
-
natural substrates
5-aminovalerate transaminase
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
-
-
-
-
natural substrates
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
-
-
-
-
natural substrates
glucuronate reductase
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
-
-
-
-
natural substrates
alcohol dehydrogenase (NADP+)
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
-
-
-
-
natural substrates
glyoxylate reductase
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
-
-
-
-
natural substrates
4-hydroxybutyrate dehydrogenase
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
-
-
-
-
natural substrates
glyoxylate reductase (NADP+)
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
-
-
-
-
natural substrates
succinate semialdehyde reductase (NADPH)
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
-
-
-
-
natural substrates
1.1.1.co
4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH + H+
-
-
-
-
natural substrates
succinate-semialdehyde dehydrogenase [NAD(P)+]
succinate semialdehyde + NAD+ + H2O = succinate + NADH + H+
-
-
-
: NADP+ (ec 1.2.1.16, see R00714)
natural substrates
aminobutyraldehyde dehydrogenase
succinate semialdehyde + NAD+ + H2O = succinate + NADH + H+
-
-
-
: NADP+ (ec 1.2.1.16, see R00714)
natural substrates
glycolaldehyde dehydrogenase
succinate semialdehyde + NAD+ + H2O = succinate + NADH + H+
-
-
-
: NADP+ (ec 1.2.1.16, see R00714)
natural substrates
succinate-semialdehyde dehydrogenase (NAD+)
succinate semialdehyde + NAD+ + H2O = succinate + NADH + H+
-
-
-
: NADP+ (ec 1.2.1.16, see R00714)
natural substrates
2,5-dioxovalerate dehydrogenase
succinate semialdehyde + NAD+ + H2O = succinate + NADH + H+
-
-
-
: NADP+ (ec 1.2.1.16, see R00714)
natural substrates
aldehyde dehydrogenase (NAD+)
succinate semialdehyde + NAD+ + H2O = succinate + NADH + H+
-
-
-
: NADP+ (ec 1.2.1.16, see R00714)
natural substrates
succinate-semialdehyde dehydrogenase (NADP+)
succinate semialdehyde + NAD+ + H2O = succinate + NADH + H+
-
-
-
: NADP+ (ec 1.2.1.16, see R00714)
natural substrates
L-glutamate gamma-semialdehyde dehydrogenase
succinate semialdehyde + NAD+ + H2O = succinate + NADH + H+
-
-
-
: NADP+ (ec 1.2.1.16, see R00714)
natural substrates
2-oxoglutarate reductase
(R)-2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+
-
-
-
-
natural substrates
phosphoglycerate dehydrogenase
(R)-2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+
-
-
-
-
natural substrates
L-2-hydroxyglutarate dehydrogenase
(R)-2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+
-
-
-
-
natural substrates
glutaconate CoA-transferase
acetyl-CoA + (R)-2-hydroxyglutarate = acetate + (R)-2-hydroxyglutaryl-1-CoA
-
-
-
-
natural substrates
glutamate-tRNA ligase
ATP + L-glutamate + tRNAGlx = AMP + diphosphate + glutamyl-tRNAGlx
: BR44350
-
-
-
-
natural substrates, nucleotide
glutamine-tRNA ligase
ATP + L-glutamate + tRNAGlx = AMP + diphosphate + glutamyl-tRNAGlx
: BR44350
-
-
-
-
natural substrates, nucleotide
glutamate-tRNAGln ligase
ATP + L-glutamate + tRNAGlx = AMP + diphosphate + glutamyl-tRNAGlx
: BR44350
-
-
-
-
natural substrates, nucleotide
lysine-tRNA ligase
ATP + L-glutamate + tRNAGlx = AMP + diphosphate + glutamyl-tRNAGlx
: BR44350
-
-
-
-
natural substrates, nucleotide
glutamyl-Q-tRNA(Asp) ligase
ATP + L-glutamate + tRNAGlx = AMP + diphosphate + glutamyl-tRNAGlx
: BR44350
-
-
-
-
natural substrates, nucleotide