Any feedback?
Information on EC 2.6.1.52 - phosphoserine transaminase and Organism(s) Niallia circulans and UniProt Accession Q59196
for references in articles please use BRENDA:EC2.6.1.52Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.6.1.52 phosphoserine transaminaseIUBMB 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
The taxonomic range for the selected organisms is: Niallia circulans
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
psat, phosphoserine aminotransferase, phosphoserine aminotransferase 1, ehpsat, 3-phosphoserine aminotransferase, psat2, l-phosphoserine aminotransferase, psat beta, bmpsat, psat alpha, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-phosphoserine aminotransferase
-
-
-
-
hydroxypyruvic phosphate-glutamic transaminase
-
-
-
-
L-phosphoserine aminotransferase
-
-
-
-
phosphohydroxypyruvate transaminase
-
-
-
-
phosphohydroxypyruvic-glutamic transaminase
-
-
-
-
phosphoserine aminotransferase
-
-
-
-
PSAT
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -
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
9030-90-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
additional information
?
-
-
high aspartate aminotransferase side activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
enzyme kinetics, overview
-
0.0017
3-phosphooxypyruvate
pH 8.2, 25°C, recombinant enzyme mutant K2G
0.0173
3-phosphooxypyruvate
pH 9.5, 25°C, recombinant enzyme mutant K2G
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9.5
pH 8.0: about 50% of maximal activity, pH 9: about 60% of maximal activity, phosphoserine synthesis
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
release of pyridoxal-5'-phosphate and protein thermal denaturation occur simultaneously at pH 6.0 in contrast to pH 8.5 where denaturation preceds release of cofactors by approximately 3°C
additional information
-
release of pyridoxal-5'-phosphate and protein thermal denaturation occur simultaneously at pH 6.0 in contrast to pH 8.5 where denaturation preceds release of cofactors by approximately 3°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
the alkaliphilic microbe grows optimally at pH 9.5-10.5
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
enzyme PSAT catalyses the second step of phosphorylated pathway of serine biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
2 * 38000-39800, recombinant enzyme mutant K2G, SDS-PAGE, 2 * 39793, sequence calculation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method at 22°C crystal. Structure of phosphoserine aminotransferase is determined at 1.2 and 1.5 A resolution at pH 8.5 and 4.6, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme mutant K2G 5.5fold from Escherichia coli strain XL-1 Blue by anion exchange chromatography, ultrafiltration, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene serC, recombinant overexpression of enzyme mutant K2G in Escherichia coli strain XL-1 Blue
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Battchikova, N.; Himanen, J.P.; Ahjolahti, M.; Korpela, T.
Phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus: purification, gene cloning and sequencing
Biochim. Biophys. Acta
1295
187-194
1996
Niallia circulans
Kapetaniou, E.G.; Thanassoulas, A.; Dubnovitsky, A.P.; Nounesis, G.; Papageorgiou, A.C.
Effect of pH on the structure and stability of Bacillus circulans ssp. alkalophilus phosphoserine aminotransferase: thermodynamic and crystallographic studies
Proteins
63
742-753
2006
Niallia circulans (Q59196), Niallia circulans
Koivulehto, M.; Battchikova, N.; Korpela, S.; Khalikova, E.; Zavialov, A.; Korpela, T.
Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria
Open Chem.
18
149-164
2020
Alkalihalobacillus alcalophilus (Q9RME2), Bos taurus (A0A3S5ZPF7), Escherichia coli (E2QJB8), Escherichia coli (P23721), Glycine max (I1JCA9), Niallia circulans (Q59196), Ovis aries (W5PS11), Tetradesmus obliquus (Q9S8N7)
-
EXTERNAL LINKS (specific for EC-Number 2.6.1.52)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
