Information on EC 2.6.1.4 - glycine transaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.6.1.4
-
RECOMMENDED NAME
GeneOntology No.
glycine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glycine + 2-oxoglutarate = glyoxylate + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
photorespiration
-
-
glycine metabolism
-
-
Glycine, serine and threonine metabolism
-
-
Glyoxylate and dicarboxylate metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
glycine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-99-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
var. Longstanding Bloomsdale
-
-
Manually annotated by BRENDA team
5 isoforms with varying substrate specificities; var. Duet
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glyoxylate + L-alanine
glycine + pyruvate
show the reaction diagram
glyoxylate + L-glutamate
glycine + 2-oxoglutarate
show the reaction diagram
glyoxylate + L-glutamine
glycine + 2-oxoglutaramate
show the reaction diagram
-
-
-
-
ir
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
show the reaction diagram
-
-
-
?
L-glutamate + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
L-homocysteate + glyoxylate
? + glycine
show the reaction diagram
-
-
-
?
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
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
glyoxylate + L-glutamate
glycine + 2-oxoglutarate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-chloro-L-alanine
-
-
Aminooxyacetate
-
-
ammonium chloride
-
50% inhibition at 15 mM
Cd2+
-
85% inhibition at 1 mM
Cu2+
-
strong
glycine
-
weak, 30% inhibition at 15 mM
hydroxylamine
Isonicotinic acid hydrazide
L-alanine
-
competitive
L-serine
-
weak, 20% inhibition at 15 mM
Maleic acid
phenylhydrazine
-
pyridoxal phosphate restores activity
Zn2+
-
weak, 25% inhibition at 1 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 4.6
glutamate
0.75 - 8.3
glyoxylate
1.2 - 6.2
L-glutamate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48.2
glyoxylate
Rhodopseudomonas palustris
-
pH 7.5, 30C
46.8
L-glutamate
Rhodopseudomonas palustris
-
pH 7.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.13
-
partially purified enzyme
0.185
-
purified enzyme
1.5
pH 7.4, 25C, L-glutamate (1 mM) + glyoxylate
2.1
pH 7.4, 25C, L-alanine (10 mM) + glyoxylate
2.4
-
peroxisomes
2.5
pH 7.4, 25C, L-glutamate (10 mM) + glyoxylate
3.25
-
purified enzyme
87
pH 7.5, 25C, L-alanine + 2-oxoglutarate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at; assay at
7.5
-
assay at
8
-
phosphate or veronal buffers
additional information
-
pI: 5.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.5
-
80% activity at pH 5.0 and pH 7.5
6.2 - 8.2
-
about half-maximal activity at pH 6.2 and pH 8.2
6.3 - 8.5
-
about half-maximal activity at pH 6.3 and about 60% of maximal activity at pH 8.5
6.9 - 7.9
highest activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
limited activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
subcellular distribution
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
gel filtration
45500
-
gel filtration
50000
-
5 isoforms, gel filtration
57000
recombinant enzyme
62000
gel filtration, 1.5fold larger than single peptide mass, indicating that enzyme is a monomer or homodimer
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
inactivation
639991
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
5 min, stable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, fairly stable for 8 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
191fold to homogeneity
-
290fold
-
partial, 5 isoforms
-
partial, about 30fold
-
using a DE52 column, butyl-Toyopearl column, DEAE-Toyopearl column, CHT ceramic hydroxyapatite column and MonoQ column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed as His6-tagged protein in Escherichia coli cells; overexpressed as His6-tagged protein in Escherichia coli cells