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EC 2.6.1.52 Details
show Brenda entryEC number
2.6.1.52
Accepted name
phosphoserine transaminase
Reaction
(1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphooxypyruvate + L-glutamate;;(2) 4-phosphooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
Other name(s)
PSAT,
phosphoserine aminotransferase,
3-phosphoserine aminotransferase,
hydroxypyruvic phosphate-glutamic transaminase,
L-phosphoserine aminotransferase,
phosphohydroxypyruvate transaminase,
phosphohydroxypyruvic-glutamic transaminase,
3-O-phospho-L-serine:2-oxoglutarate aminotransferase,
SerC,
PdxC,
3PHP transaminase
Systematic name
O-phospho-L-serine:2-oxoglutarate aminotransferase
CAS registry number
9030-90-4
Comment
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].
History
created 1972, modified 2006
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1 Oxidoreductases
2 Transferases
2.6.1.10 created 1961, deleted 1972 2.6.1.20 created 1965, deleted 1972 2.6.1.25 created 1972, deleted 1984 2.6.1.53 created 1972, deleted 1976 2.6.1.61 created 1982, deleted 2004 2.6.1.69 created 1989, deleted 2004
