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IUBMB Comments The enzyme participates in a degradation pathway of trans -4-hydroxy-L -proline, a compound that contributes to the stability of the collagen triple helix. Oxaloacetate can replace 2-oxoglutarate. This enzyme may be identical with EC 2.6.1.1 aspartate transaminase.
Synonyms
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4-hydroxyglutamate aminotransferase
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aminotransferase, 4-hydroxyglutamate
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additional information
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may be identical with EC 2.6.1.1 aspartate transaminase
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erythro-4-hydroxy-L-glutamate + 2-oxoglutarate = (4R)-4-hydroxy-2-oxoglutarate + L-glutamate
oxaloacetate can replace 2-oxoglutarate
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amino group transfer
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MetaCyc
trans-4-hydroxy-L-proline degradation I
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erythro-4-hydroxy-L-glutamate:2-oxoglutarate aminotransferase
The enzyme participates in a degradation pathway of trans-4-hydroxy-L-proline, a compound that contributes to the stability of the collagen triple helix. Oxaloacetate can replace 2-oxoglutarate. This enzyme may be identical with EC 2.6.1.1 aspartate transaminase.
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4-hydroxy-L-glutamate + 2-oxoglutarate
4-hydroxy-2-oxoglutarate + L-glutamate
4-hydroxy-L-glutamate + oxaloacetate
4-hydroxy-2-oxoglutarate + L-aspartate
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Substrates: -
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4-hydroxy-L-glutamate + oxo acid
4-hydroxy-2-oxoglutarate + L-glutamate
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Substrates: metabolism of 4-hydroxy-L-glutamate in rat liver
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L-erythro-4-hydroxyglutamate + 2-oxoglutarate
D-4-hydroxy-2-oxoglutarate + L-glutamate
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Substrates: -
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additional information
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4-hydroxy-L-glutamate + 2-oxoglutarate
4-hydroxy-2-oxoglutarate + L-glutamate
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Substrates: -
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4-hydroxy-L-glutamate + 2-oxoglutarate
4-hydroxy-2-oxoglutarate + L-glutamate
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Substrates: enzyme utilises erythro-L-4-hydroxyglutamate and threo-L-4-hydroxyglutamate to the same extent, but no D-isomers
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additional information
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Substrates: substrate stereospecificity
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additional information
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Substrates: no activity with pyruvate, glyoxylate
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additional information
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Substrates: pyruvate is a poor substrate
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4-hydroxy-L-glutamate + oxo acid
4-hydroxy-2-oxoglutarate + L-glutamate
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Substrates: metabolism of 4-hydroxy-L-glutamate in rat liver
r
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additional information
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no cofactor requirement
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hydroxylamine
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70% inhibition at 1 mM
L-glutarate
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63% inhibition at 0.5 mM
Maleate
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65% inhibition at 5 mM
N-ethylmaleimide
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50% inhibition at 5 mM
p-chloromercuribenzoate
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77% inhibition at 0.5 mM
phenylhydrazine
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84% inhibition at 1 mM
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0.41
2-oxoglutarate
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pH 8.1, 37°C
5.7
4-hydroxy-L-glutamate
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pH 8.0, 37°C
240
L-erythro-4-hydroxyglutamate
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pH 8.1, 37°C
33
L-glutamate
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pH 8.1, 37°C
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0.49
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partially purified enzyme
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8.2
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with erythro-L-hydroxyglutamic acid
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6.7 - 9.5
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pH 6.7: about 45% of activity maximum, pH 9.5: about 55% of activity maximum
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brenda
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brenda
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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C4IWV5_BRUAO
269
0
28527
TrEMBL
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C0RMT5_BRUMB
Brucella melitensis biotype 2 (strain ATCC 23457)
269
0
28527
TrEMBL
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C0G8S3_9HYPH
269
0
28527
TrEMBL
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Goldstone, A.; Adams, E.
Metabolism of gamma-hydroxyglutamic acid. I. Conversion to alpha-hydroxy-gamma-ketoglutarate by purified glutamic-aspartic transaminase of rat liver
J. Biol. Chem.
237
3476-3485
1962
Rattus norvegicus
brenda
Kuratomi, K.; Fukunaga, K.; Kobayashi, Y.
The metabolism of gamma hydroxyglutamate in rat liver. II. A transaminase concerned in gamma-hydroxyglutamate metabolism
Biochim. Biophys. Acta
78
629-636
1963
Rattus norvegicus
brenda
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