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Information on EC 2.6.1.52 - phosphoserine transaminase and Organism(s) Pseudomonas aeruginosa

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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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Pseudomonas aeruginosa

The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms

Reaction Schemes

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4-phosphooxy-L-threonine

2-oxoglutarate

(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate

L-glutamate

Synonyms

3-O-phospho-L-serine:2-oxoglutarate aminotransferase, 3-phosphoserine aminotransferase, AspAT, AtPSAT, BCIR PSAT, EhPSAT, hydroxypyruvic phosphate-glutamic transaminase, L-phosphoserine aminotransferase, phosphohydroxypyruvate transaminase, phosphohydroxypyruvic-glutamic transaminase, show all synonyms

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3-phosphoserine aminotransferase

hydroxypyruvic phosphate-glutamic transaminase

L-phosphoserine aminotransferase

phosphohydroxypyruvate transaminase

phosphohydroxypyruvic-glutamic transaminase

phosphoserine aminotransferase

PSAT

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amino group transfer

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BRENDA

serine metabolism, vitamin B6 metabolism

KEGG

Biosynthesis of secondary metabolites, Cysteine and methionine metabolism, Glycine, serine and threonine metabolism, Methane metabolism, Microbial metabolism in diverse environments, Vitamin B6 metabolism

MetaCyc

L-cysteine biosynthesis IX (Trichomonas vaginalis), L-serine biosynthesis I, pyridoxal 5'-phosphate biosynthesis I

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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].

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9030-90-4