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Information on EC 2.6.1.52 - phosphoserine transaminase and Organism(s) Methanosarcina barkeri and UniProt Accession P52878

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.52 phosphoserine transaminase
IUBMB Comments
A pyridoxal 5'-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis [1,3] and the third step in pyridoxal 5'-phosphate biosynthesis in the bacterium Escherichia coli . Pyridoxal 5'-phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis . Non-phosphorylated forms of serine and threonine are not substrates . The archaeal enzyme has a relaxed specificity and can act on L-cysteate and L-alanine as alternative substrates to O-phospho-L-serine .
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Methanosarcina barkeri
UNIPROT: P52878
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The taxonomic range for the selected organisms is: Methanosarcina barkeri
The enzyme appears in selected viruses and cellular organisms
Synonyms
psat, phosphoserine aminotransferase, phosphoserine aminotransferase 1, ehpsat, 3-phosphoserine aminotransferase, psat2, l-phosphoserine aminotransferase, psat beta, bmpsat, psat alpha, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoserine aminotransferase
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3-phosphoserine aminotransferase
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hydroxypyruvic phosphate-glutamic transaminase
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-
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L-phosphoserine aminotransferase
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-
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phosphohydroxypyruvate transaminase
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phosphohydroxypyruvic-glutamic transaminase
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phosphoserine aminotransferase
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PSAT
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
O-phospho-L-serine:2-oxoglutarate aminotransferase
A pyridoxal 5'-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis [1,3] and the third step in pyridoxal 5'-phosphate biosynthesis in the bacterium Escherichia coli [3]. Pyridoxal 5'-phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis [4]. Non-phosphorylated forms of serine and threonine are not substrates [4]. The archaeal enzyme has a relaxed specificity and can act on L-cysteate and L-alanine as alternative substrates to O-phospho-L-serine [7].
CAS REGISTRY NUMBER
COMMENTARY hide
9030-90-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
show the reaction diagram
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-
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Metcalf, W.W.; Zhang, J.K.; Shi, X.; Wolfe, R.S.
Molecular, genetic, and biochemical characterization of the serC gene of Methanosarcina barkeri Fusaro
J. Bacteriol.
178
5797-5802
1996
Methanosarcina barkeri (P52878), Methanosarcina barkeri, Methanosarcina barkeri DSM 804 (P52878)
Manually annotated by BRENDA team