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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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Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-phosphoserine aminotransferase
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hydroxypyruvic phosphate-glutamic transaminase
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L-phosphoserine aminotransferase
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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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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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A2R3ITI3_PSEAI
361
0
39990
TrEMBL
A0A485ENZ7_PSEAI
188
0
20856
TrEMBL
A0A2S5IJP8_PSEAI
361
0
39728
TrEMBL
A0A485FIA4_PSEAI
727
0
80584
TrEMBL
A0A0A8RFZ9_PSEAI
379
0
41828
TrEMBL
A0A367MI08_PSEAI
361
0
39949
TrEMBL
A0A0C7CSX6_PSEAI
361
0
39961
TrEMBL
A0A0F6UC55_PSEAI
361
0
39999
TrEMBL
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