Information on EC 2.6.1.52 - phosphoserine transaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.6.1.52
-
RECOMMENDED NAME
GeneOntology No.
phosphoserine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-serine biosynthesis
-
-
pyridoxal 5'-phosphate biosynthesis I
-
-
serine metabolism
-
-
vitamin B6 metabolism
-
-
Glycine, serine and threonine metabolism
-
-
Methane metabolism
-
-
Vitamin B6 metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
O-phospho-L-serine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli [2,3]. It also catalyses the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in Escherichia coli (using Reaction 2 above) [3]. In Escherichia coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). Pyridoxal 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].
CAS REGISTRY NUMBER
COMMENTARY hide
9030-90-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acutodesmus obliquus
mutant C-2 A'
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
enzyme forms a protein-protein complex with D-phosphoglycerate dehydrogenase, which has a 1:1 stoichiometry. Ionic interactions play a significant role in complex formation and stability. The nucleotide binding domain of D-phosphoglycerate dehydrogenase specifically interacts with the enzyme. The purified nucleotide binding domain of D-phosphoglycerate dehydrogenase interacts with phosphoserine transaminase. The reactions catalyzed by the complex suggest a possibility of substrate channelling in the protein complex
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-4-phosphonobutyrate + 2-oxoglutarate
2-oxophosphonobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
2-amino-5-phosphonovalerate + 2-oxoglutarate
5-phosphono-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
2-oxo-3-hydroxy-4-phosphobutanoate + L-glutamate
4-(phosphonooxy)-L-threonine + 2-oxoglutarate
show the reaction diagram
3-O-phospho-L-serine + 2-oxoglutarate
?
show the reaction diagram
3-phosphonooxypyruvate + 2-oxoglutarate
?
show the reaction diagram
3-phosphonooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
homocysteate + 2-oxoglutarate
4-mercapto-2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 3-phosphonooxypyruvate
O-phospho-L-serine + pyruvate
show the reaction diagram
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
show the reaction diagram
L-glutamate + 4,5-dioxopentanoate
5-aminolevulinate + 2-oxoglutarate
show the reaction diagram
Acutodesmus obliquus
-
-
-
-
?
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Amino-4-phosphonobutyrate
-
-
2-oxoglutarate
-
-
L-cysteine
L-glutamate
-
-
L-phosphoserine
-
product inhibition
O-acetylserine
10 mM, 50% inhibition
o-phospho-D-serine
10 mM, 70% inhibition
O-phospho-L-threonine
10 mM, 65% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043 - 0.8
2-oxoglutarate
0.017 - 0.037
3-O-phospho-L-serine
0.005 - 5
3-phosphohydroxypyruvate
0.01 - 0.1
3-phosphonooxypyruvate
0.84
4,5-Dioxopentanoate
Acutodesmus obliquus
-
pH 8.0, 35C
0.11
4-(phosphonooxy)-L-threonine
-
MalE/PdxC(SerC) fusion protein, pH 8.2, 37C; PdxC(SerC) protein, pH 8.2, 37C
0.07 - 5.05
L-glutamate
0.035 - 0.083
L-phosphoserine
0.0368 - 0.225
O-phospho-L-serine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.39 - 0.63
3-O-phospho-L-serine
1.33 - 1.75
3-phosphonooxypyruvate
0.08 - 0.15
4-(phosphonooxy)-L-threonine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24
2-Amino-4-phosphonobutyrate
-
-
2.55
2-oxoglutarate
-
pH 7.5, 30C
7.42
L-glutamate
-
pH 7.5, 30C
0.045
L-phosphoserine
-
pH 7.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.47
-
substrate: O-phospho-L-serine, pH 8.5, 25C
0.66
substrate: 2-oxoglutarate, pH 8.5, 25C
0.67
substrate: O-phospho-L-serine, pH 8.5, 25C
0.74
-
substrate: 2-oxoglutarate, pH 8.5, 25C
1.29
-
-
5.82
substrate: L-glutamate, pH 8.5, 25C
6.14
substrate: 3-phosphohydroxypyruvate, pH 8.5, 25C
9.65
-
substrate: 3-phosphohydroxypyruvate, pH 8.5, 25C
12
-
pH and temperature not specified in the publication
13.2
-
-
13.84
Acutodesmus obliquus
-
-
21.22
-
substrate: L-glutamate, pH 8.5, 25C
additional information
-
13 U/mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8.2
Acutodesmus obliquus
-
-
6.8 - 7.2
-
-
7
Acutodesmus obliquus
-
phosphoserine with 2-oxoglutarate as amino acceptor
7.4
-
assay at
8 - 8.5
formation of 3-phosphohydroxypyruvate
8 - 9
formation of O-phospho-L-serine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
Acutodesmus obliquus
-
-
5.5 - 11
about 75% of maximal activit at pH 5.5 and pH 11.0, formation of 3-phosphohydroxypyruvate
7 - 10
about 50% of maximal activity at pH 7.0 and at pH 10.0, formation of O-phospho-L-serine
7.8 - 8.8
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 hide
LITERATURE
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.43
His-tagged recombinant enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
PSAT1 is overexpressed in colon tumors
Manually annotated by BRENDA team
-
mRNA expressed in
Manually annotated by BRENDA team
-
mRNA expressed in
Manually annotated by BRENDA team
additional information
-
very weak mRNA expression in thymus,prostate, testis and colon
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35200
-
PSATalpha, predicted from cDNA
36000
-
PdxC(SerC) protein
39790
-
predicted from cDNA
40000
-
PSATbeta, predicted from cDNA
41680
-
deduced from amino acid sequence
70000
-
gel filtration
77000
-
calculated from Stokes radius
79000
-
MalE/PdxC(SerC) fusion protein, Coomassie blue stained SDS-PAGE
80000
Acutodesmus obliquus
-
gel filtration
90700
-
sedimentation equilibrium ultracentrifugation
96000
-
Trautman modification of the Archibald approach to equilibrium method
155000
-
gel filtration, protein-protein complex with D-phosphoglycerate dehydrogenase, which has a 1:1 stoichiometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme forms a protein-protein complex with D-phosphoglycerate dehydrogenase, which has a 1:1 stoichiometry. Ionic interactions play a significant role in complex formation and stability. The nucleotide binding domain of D-phosphoglycerate dehydrogenase specifically interacts with the enzyme. The purified nucleotide binding domain of D-phosphoglycerate dehydrogenase interacts with phosphoserine transaminase. The reactions catalyzed by the complex suggest a possibility of substrate channelling in the protein complex
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
comparison with enzyme structure from Escherichia coli and Bacillus circulans
-
recombinant protein
-
hanging-drop vapor diffusion method at 22C crystal. Structure of phosphoserine aminotransferase is determined at 1.2 and 1.5 A resolution at pH 8.5 and 4.6, respectively
energy-minimized average simulated model. the enzyme exists as a homodimer and each subunit of the protein is composed of two domains, a large pyridoxal phosphate-binding domain and a C-terminal domain. The enzyme harbors two active sites present at the subunit interface. The indole ring of residue Trp101 stacks with the pyridine ring of pyridoxal 5'-phopsphate at the active site and distance between the two moieties is about 5 A
-
space group P2(1)2(1)2(1)
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
apo-enzyme
58
pH 8.5, Tm: 58.4C
67
-
holo-enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Cm values obtained from the denaturation profile for holo-enzyme and apo-
-
enzyme are 2.8 and 2 M, respectively.
-
enzyme can be inactivated by dialysis against cysteine
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, stored in individual aliquots or stored as pellet concentrated by ammonium sulfate precipitation, stable for at least 3 months
-
Whereas the fusion protein is stable over several weeks, the cleaved protein shows a clear loss of activity within 2 weeks at 4C.
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
MalE/PdxC(SerC) fusion protein, affinity chromatography on an amylose resin, hydrolyzed in the presence of protease factor Xa
-
recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 forms results from alternative splicing, PSATalpha and PSATbeta, cDNA cloned and expressed in Escherichia coli and in human cell lines, leukaemia Jurkat, colon adenocarcinoma COLO 320DM, heptacellular carcinoma HepG2 and weakly in leukaemia MOLT-3, complementation of Saccharomyces cerevisiae SER-1 deletion mutation
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cDNA encoding PSAT, single gene mapped on the lower arm of chromosome 4, overexpressed in Escherichia coli AD494 and BL21
cloned and expressed in Escherichia coli
-
cloned and expressed in Escherichia coli KL282 and BL21
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cloning of the PSAT gene, expression in Escherichia coli
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expression in Escherichia coli
overexpressed as His6-tagged protein in Escherichia coli cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PSAT1 is overexpressed in colorectal tumor samples
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W101A
-
about 5% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. In mutant W101A, there are no big fluctuations but the stacking interaction is lost due to side chain truncation
W101F
-
about 70% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. The stacking interaction for mutants W101F and W101H are not as prominent as for the wild-type protein
W101H
-
about 20% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. The stacking interaction for mutants W101F and W101H are not as prominent as for the wild-type protein
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
synthesis
-
deletion of L-serine dehydratase in combination with overexpression of enzyme, L-serine insensitive 3-phosphoglycerate dehydrogenase, and phosphoserine phosphatase yields up to 86 mM L-serine in the culture medium
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