Information on EC 2.6.1.23 - 4-hydroxyglutamate transaminase

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The expected taxonomic range for this enzyme is: Rattus norvegicus

EC NUMBER
COMMENTARY hide
2.6.1.23
-
RECOMMENDED NAME
GeneOntology No.
4-hydroxyglutamate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-hydroxy-L-glutamate + 2-oxoglutarate = 4-hydroxy-2-oxoglutarate + L-glutamate
show the reaction diagram
oxaloacetate can replace 2-oxoglutarate
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-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
trans-4-hydroxy-L-proline degradation I
-
-
Arginine and proline metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-L-glutamate:2-oxoglutarate aminotransferase
Oxaloacetate can replace 2-oxoglutarate. This enzyme may be identical with EC 2.6.1.1 aspartate transaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
37277-86-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxy-L-glutamate + 2-oxoglutarate
4-hydroxy-2-oxoglutarate + L-glutamate
show the reaction diagram
4-hydroxy-L-glutamate + oxaloacetate
4-hydroxy-2-oxoglutarate + L-aspartate
show the reaction diagram
-
-
-
-
r
4-hydroxy-L-glutamate + oxo acid
4-hydroxy-2-oxoglutarate + L-glutamate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxy-L-glutamate + oxo acid
4-hydroxy-2-oxoglutarate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydroxylamine
-
70% inhibition at 1 mM
L-glutarate
-
63% inhibition at 0.5 mM
Maleate
-
65% inhibition at 5 mM
N-ethylmaleimide
-
50% inhibition at 5 mM
p-chloromercuribenzoate
-
77% inhibition at 0.5 mM
phenylhydrazine
-
84% inhibition at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41
2-oxoglutarate
-
pH 8.1, 37C
5.7
4-hydroxyglutamate
-
pH 8.0, 37C
240
erythro-L-hydroxyglutamic acid
-
pH 8.1, 37C
-
33
L-glutamate
-
pH 8.1, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.49
-
partially purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
-
with erythro-L-hydroxyglutamic acid
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 9.5
-
pH 6.7: about 45% of activity maximum, pH 9.5: about 55% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
15fold; partial
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