Information on EC 2.6.1.51 - serine-pyruvate transaminase

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

EC NUMBER
COMMENTARY hide
2.6.1.51
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RECOMMENDED NAME
GeneOntology No.
serine-pyruvate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-serine + pyruvate = 3-hydroxypyruvate + L-alanine
show the reaction diagram
A pyridoxal-phosphate protein; A pyridoxal-phosphate protein.; a pyridoxal-phosphate protein. The liver enzyme may be identical with EC 2.6.1.44 alanine-glyoxylate transaminase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycine, serine and threonine metabolism
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Metabolic pathways
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serine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-serine:pyruvate aminotransferase
A pyridoxal-phosphate protein. The liver enzyme may be identical with EC 2.6.1.44 alanine-glyoxylate transaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-88-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
human
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
rainbow trout
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Manually annotated by BRENDA team
kidney bean, L. cv. Red Kidney
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Manually annotated by BRENDA team
var. Alaska
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Manually annotated by BRENDA team
Donryu strain
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Manually annotated by BRENDA team
strain Wistar
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-
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
2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
show the reaction diagram
-
-
-
?
5-hydroxytryptophan + pyruvate
3-(5-hydroxyindole)-2-oxopropanoate + alanine
show the reaction diagram
arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
show the reaction diagram
-
-
-
?
asparagine + pyruvate
2-oxosuccinamate + L-alanine
show the reaction diagram
cysteine + pyruvate
3-mercapto-2-oxo-propanoate + L-alanine
show the reaction diagram
-
-
-
?
glutamic acid + 3-hydroxypyruvate
2-oxo-1,5-pentandioate + serine
show the reaction diagram
-
-
-
-
r
glutamine + phenylpyruvate
4-carbamoyl-2-oxobutanoate + L-phenylalanine
show the reaction diagram
-
-
-
?
glutamine + pyruvate
4-carbamoyl-2-oxobutanoate + L-alanine
show the reaction diagram
glycine + 3-hydroxypyruvate
glyoxylate + L-serine
show the reaction diagram
glycine + 3-hydroxypyruvate
L-serine + glyoxylate
show the reaction diagram
glycine + pyruvate
glyoxylate + L-alanine
show the reaction diagram
-
-
-
?
histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
show the reaction diagram
-
-
-
?
histidine + pyruvate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-alanine
show the reaction diagram
isoleucine + pyruvate
3-methyl-2-oxopentanoate + alanine
show the reaction diagram
-
-
-
?
L-alanine + 3-hydroxypyruvate
pyruvate + L-serine
show the reaction diagram
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
show the reaction diagram
-
-
-
?
L-asparagine + phenylpyruvate
2-oxosuccinamate + L-phenylalanine
show the reaction diagram
-
-
-
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L-leucine + phenylpyruvate
4-methyl-2-oxopentanoate + L-phenylalanine
show the reaction diagram
L-leucine + pyruvate
4-methyl-2-oxopentanoate + L-alanine
show the reaction diagram
-
-
-
?
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
show the reaction diagram
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-
-
?
L-methionine + phenylpyruvate
4-methylsulfanyl-2-oxobutanoate + L-phenylalanine
show the reaction diagram
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
show the reaction diagram
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
show the reaction diagram
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-
-
?
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
show the reaction diagram
L-serine + glyoxylate
glycine + 3-hydroxypyruvate
show the reaction diagram
L-serine + oxaloacetate
3-hydroxypyruvate + L-aspartate
show the reaction diagram
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-
-
?
L-serine + phenylpyruvate
3-hydroxypyruvate + L-phenylalanine
show the reaction diagram
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
show the reaction diagram
L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
show the reaction diagram
-
-
-
?
L-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
show the reaction diagram
-
-
-
-
?
L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
show the reaction diagram
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-
-
?
L-tyrosine + pyruvate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-alanine
show the reaction diagram
lysine + pyruvate
6-amino-2-oxohexanoate + alanine
show the reaction diagram
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-
-
-
?
ornithine + phenylpyruvate
5-amino-2-oxopentanoate + L-phenylalanine
show the reaction diagram
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-
-
?
ornithine + pyruvate
5-amino-2-oxopentanoate + L-alanine
show the reaction diagram
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-
-
?
threonine + phenylpyruvate
3-hydroxy-2-oxobutanoate + L-phenylalanine
show the reaction diagram
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-
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?
valine + pyruvate
3-methyl-2-oxobutanoate + alanine
show the reaction diagram
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?
additional information
?
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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
L-alanine + 3-hydroxypyruvate
pyruvate + L-serine
show the reaction diagram
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r
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
show the reaction diagram
additional information
?
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enzyme converts L-hydroxyproline-derived glyoxylate into glycine in situ, preventing undesirable overflow into the production of oxalate
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
histidine
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competitive inhibitor of serine transamination
hydroxylamine
Isonicotinic acid hydrazide
N-ethylmaleimide
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Semicarbazide
serine
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competitive inhibitor of histidine transamination
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glucagon
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mitochondrial enzyme is markedly induced by
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
149
alanine
pH 7.0, 50C, recombinant enzyme
0.01 - 64
glyoxylate
4
Hydroxypyruvate
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pH 8.4-9.2, 15C
2.2
L-alanine
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pH 8.4-9.2, 15C
8.1
L-serine
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pH 8.4-9.2, 15C, Km increases with rising temperature, remains constant over the range 5-30C
0.21 - 51
pyruvate
0.39 - 256
serine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
131
alanine
Drosophila melanogaster
Q9W3Z3
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113
glyoxylate
Drosophila melanogaster
Q9W3Z3
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.02
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alanine-hydroxypyruvate transamination
2.23
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alanine-hydroxypyruvate transamination
3.47
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serine-pyruvate aminotransferase activity
3.58
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serine-pyruvate transamination
4.08
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serine-pyruvate transamination
4.62
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recombinant enzyme
5.41
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recombinant enzyme
8.2
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source leaf, age 10 days
8.3
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source apical meristem, age 16 days
8.5
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source apical meristem, age 15 days; source leaf, age 11 days
8.6
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source apical meristem, age 13 days
8.8
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source leaf, age 13 days
9.4
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source apical meristem, age 10 days
9.5
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source apical meristem, age 11 days
11.1
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source leaf, age 16 days
13
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serine-pyruvate transamination
13.1
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source leaf, age 15 days
14
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serine-pyruvate transamination
16.63
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alanine-hydroxypyruvate transamination
25.7
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histidine-pyruvate aminotransferase activity
31.38
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alanine-hydroxypyruvate transamination
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.4 - 9.2
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8.5 - 9
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73000 - 79000
73000
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gel filtration
75000 - 80000
75000
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sucrose density gradient centrifugation
80000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.8 A resolution. The structure of the Sulfolobus solfataricus enzyme is determined with an amino form of the cofactor pyridoxamine 5'-phosphate bound in the active site and in complex with gabaculine, an aminotransferase inhibitor. These structures show the changes in the enzyme active site during the course of the catalytic reaction
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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heating of the purified enzyme for different lengths of time produces equivalent losses of both activities
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme recovered in the supernatant is resistant to proteinase K in presence or absence of Triton X-100, enzyme recovered in the precipitate is sensitive to the protease
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precursor of mitochondrial enzyme is highly sensitive to proteinase K digestion, peroxisomal enzyme is fairly resistant to the protease
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM potassium phosphate buffer, pH 7.5 may be stored for at least 6 weeks without loss of either activity
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-20C, 50 mM potassium phosphate buffer, pH 7.5, containing 0.1 M pyridoxal 5'-phosphate, may be stored for at least 4 weeks without loss of activity
0-5C, little or none of either activity is lost when the enzyme is stored for 2 weeks
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0-6C, 50 mM potassium phosphate buffer, pH 7.5, containing 0.1 M pyridoxal 5'-phosphate, little loss with storage for at least 2 weeks
5C, acetone powder of fresh liver stored in a vacuum desiccator over aluminia retains its enzymatic activity for months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-purification of serine:glyoxylate aminotransferase
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isoenzyme 1 of histidine-pyruvate aminotransferase
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mitochondrial and peroxisomal isoforms
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native and recombinant enzyme
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recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
binding sites identified by using a luciferase reporter assay with HepG2 cells, DNase I footprinting analysis and gel shift experiments
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C-terminal SPT mutants constructed and examined in transfected COS-1 cells
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cDNA cloned and expressed in Escherichia coli DH1
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cloned and expressed in Escherichia coli DH5 and Escherichia coli ER1458
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expressed in SF9 cells, using a insect/baculovirus expression system
plasmid containing cDNA of human SPT cloned
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SPT/AGT gene is linked to the CAT gene and transiently expressed in human hepatoma-derived HepG2 cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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absence of human SPT/AGT or mistargeting of this enzyme causes primary hyperoxaluria type 1, an inborn error of glyoxylate metabolism characterized by increased oxalate production
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