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
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Glycine, serine and threonine metabolism
-
-
Glyoxylate and dicarboxylate metabolism
-
-
Metabolic pathways
-
-
photorespiration
-
-
glycine metabolism
-
-
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
rice leaves usually show 3-4 times higher abundance of glutamate relative to serine, implicating that glutamate:glyoxylate aminotransferase GGAT may preferentially utilize glyoxylate to form glycine over serine:glyoxylate aminotransferase SGAT. When SGAT or GGAT activity is regulated by gene transformation or nitrogen deficiency, respectively, the glycine content is positively related to GGAT activities, while both serine and glycine contents are negatively related to SGAT activities, suggesting that GGAT preferentially catalyzes the conversion of glyoxylate into glycine while SGAT is mainly responsible for the transamination reaction of serine to hydroxypyruvate in the photorespiratory pathway of rice
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-glutamate + glyoxylate
2-oxoglutarate + glycine
show the reaction diagram
-
-
-
?
L-glutamate + pyruvate
2-oxoglutarate + L-alanine
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
0.55
2-oxoglutarate
cosubstrate L-alanine, pH 7.6, 30C
2 - 4.6
glutamate
0.21 - 8.3
glyoxylate
2.37 - 2.96
L-alanine
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
132.9 - 140.6
L-alanine
46.8 - 144.9
L-glutamate
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
tetramer
4 * 54000, SDS-PAGE
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
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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