show all | hide all No of entries

Information on EC 2.6.1.52 - phosphoserine transaminase

for references in articles please use BRENDA:EC2.6.1.52
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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 .
Specify your search results
Select one or more organisms in this record: ?
The enzyme appears in 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
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-phosphooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
show the reaction diagram
(2)
-
-
-
O-phospho-L-serine + 2-oxoglutarate = 3-phosphooxypyruvate + L-glutamate
show the reaction diagram
Select items on the left to see more content.