Pathways

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BRENDA KEGG MetaCyc

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
asparaginyl-tRNA synthase (glutamine-hydrolysing)
ATP + L-glutamyl-tRNAGln + L-glutamine = ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
-
natural substrates
glutaminyl-tRNA synthase (glutamine-hydrolysing)
ATP + L-glutamyl-tRNAGln + L-glutamine = ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
-
natural substrates
6-aminohexanoate aminotransferase
4-aminobutanoate + pyruvate = succinate semialdehyde + L-alanine
-
-
-
-
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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-
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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
-
-
-
: multi-step reaction (see R03153+R00237)
natural substrates, multi-step reaction
(S)-2-methylmalate dehydratase
(S)-2-Methylmalate = 2-methylfumarate + H2O
-
-
-
-
natural substrates
acyl-CoA dehydrogenase (NADP+)
crotonyl-CoA + reduced acceptor = butyryl-CoA + oxidized acceptor
generic compounds
-
-
-
natural substrates, generic
short-chain acyl-CoA dehydrogenase
crotonyl-CoA + reduced acceptor = butyryl-CoA + oxidized acceptor
generic compounds
-
-
-
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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-
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-
natural substrates
(R)-2-hydroxyglutaryl-CoA dehydratase
(R)-2-hydroxyglutaryl-CoA = (E)-glutaconyl-CoA + H2O
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-
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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
-
-
-
-
natural substrates
tryptophanyl aminopeptidase
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
asparaginase
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
glutaminase
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
glutamin-(asparagin-)ase
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
peptidyl-glutaminase
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
protein-glutamine glutaminase
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
imidazole glycerol phosphate 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
imidazole glycerol-phosphate 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
pyridoxal 5'-phosphate synthase (glutamine hydrolysing)
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
CTP synthase (glutamine hydrolysing)
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
lipid II isoglutaminyl synthase (glutamine-hydrolysing)
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
GMP synthase (glutamine-hydrolysing)
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
asparagine synthase (glutamine-hydrolysing)
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
carbamoyl-phosphate synthase (glutamine-hydrolysing)
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
asparaginyl-tRNA synthase (glutamine-hydrolysing)
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
glutaminyl-tRNA synthase (glutamine-hydrolysing)
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
gamma-glutamyltransferase
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
amidophosphoribosyltransferase
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
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
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
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
-
-
-
-
natural substrates, nucleotide
glutamine-tRNA ligase
ATP + L-glutamate + tRNAGlx = AMP + diphosphate + glutamyl-tRNAGlx
-
-
-
-
natural substrates, nucleotide
glutamate-tRNAGln ligase
ATP + L-glutamate + tRNAGlx = AMP + diphosphate + glutamyl-tRNAGlx
-
-
-
-
natural substrates, nucleotide
lysine-tRNA ligase
ATP + L-glutamate + tRNAGlx = AMP + diphosphate + glutamyl-tRNAGlx
-
-
-
-
natural substrates, nucleotide
glutamyl-Q-tRNA(Asp) ligase
ATP + L-glutamate + tRNAGlx = AMP + diphosphate + glutamyl-tRNAGlx
-
-
-
-
natural substrates, nucleotide