Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.6.1.52 - phosphoserine transaminase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WQ73

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: ?
This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WQ73
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
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
3-phosphoserine aminotransferase
-
-
-
-
hydroxypyruvic phosphate-glutamic transaminase
-
-
-
-
L-phosphoserine aminotransferase
-
-
-
-
phosphohydroxypyruvate transaminase
-
-
-
-
phosphohydroxypyruvic-glutamic transaminase
-
-
-
-
phosphoserine aminotransferase
-
-
-
-
PSAT
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
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
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with cofactor pyridoxal 5'-phosphate, to 1.5 A resolution. The enzyme has a fold typical of the aspartate aminotransferase family of pyridoxal phosphate-dependent enzymes. The protein forms a stable symmetrical homodimer which is maintained by extensive interactions, mostly between the large domains of the two subunits. Each active site contains a bound cofactor molecule. The aromatic ring rests above the C-terminal end of the central strand 7 of the seven-stranded beta-sheet in a pocket in which its pyridine N-atom points in towards the interior of the large domain, hydrogen-bonded to the invariant residue Asp176, and its 5'-phosphate and C4 substituent point out into the dimer interface. The phosphate group is adjacent to the N-terminus of helix 3, hydrogen-bonded to the main-chain amide N-atoms of Ala84 and Thr85 and the side chain of Gln199 from one monomer, as well as to Asn251 and Thr252 of the opposing monomer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Coulibaly, F.; Lassalle, E.; Baker, H.M.; Baker, E.N.
Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis
Acta Crystallogr. Sect. D
68
553-563
2012
Mycobacterium tuberculosis (P9WQ73), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WQ73)
Manually annotated by BRENDA team