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Literature summary for 1.1.1.95 extracted from

  • Grant, G.A.; Hu, Z.; Xu, X.L.
    Identification of amino acid residues contributing to the mechanism of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase (2005), Biochemistry, 44, 16844-16852.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.95

Protein Variants

Protein Variants Comment Organism
A143A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
A144V site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
A374V site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
D317A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
D386A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
E299A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
E302A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
E307A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
E345A site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme Escherichia coli
E360A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
E387A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
G145V site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
G336V site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
G337V site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
G349V site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme Escherichia coli
G362V site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
H335A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
H344A site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme Escherichia coli
K141A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
K311A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
N190A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, no protein expression Escherichia coli
N303A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
N303A/K311A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
N346A site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme Escherichia coli
N364A site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme Escherichia coli
P348A site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme Escherichia coli
Q298A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
Q301A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
Q361A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
Q375A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
R338A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
R347A site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme Escherichia coli
S107A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
S107A/S111A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
S111A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
S111A/K311A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
S296A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
S316A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
S323A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
S373A site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
T297A site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-serine the enzyme contains an ACT regulatory domain which binds L-serine for feedback regulation, binding site lies around residues H344-N364 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.19
-
 3-phospho-D-glycerate pH 7.5, mutant G336V Escherichia coli
0.23
-
 3-phospho-D-glycerate pH 7.5, mutant H344A Escherichia coli
0.26
-
 3-phospho-D-glycerate pH 7.5, mutant A144V Escherichia coli
0.28
-
 3-phospho-D-glycerate pH 7.5, mutant E387A Escherichia coli
0.29
-
 3-phospho-D-glycerate pH 7.5, mutant N364A Escherichia coli
0.3
-
 3-phospho-D-glycerate pH 7.5, mutant E302A Escherichia coli
0.33
-
 3-phospho-D-glycerate pH 7.5, mutant R338A Escherichia coli
0.35
-
 3-phospho-D-glycerate pH 7.5, mutants A374V and D386A Escherichia coli
0.39
-
 3-phospho-D-glycerate pH 7.5, mutant N346A Escherichia coli
0.45
-
 3-phospho-D-glycerate pH 7.5, mutant R347A Escherichia coli
0.47
-
 3-phospho-D-glycerate pH 7.5, mutant Q361A Escherichia coli
0.49
-
 3-phospho-D-glycerate pH 7.5, wild-type enzyme and mutant Q375A Escherichia coli
0.58
-
 3-phospho-D-glycerate pH 7.5, mutant P348A Escherichia coli
0.63
-
 3-phospho-D-glycerate pH 7.5, mutant S316A Escherichia coli
0.64
-
 3-phospho-D-glycerate pH 7.5, mutant G337V Escherichia coli
0.66
-
 3-phospho-D-glycerate pH 7.5, mutant E360A Escherichia coli
0.68
-
 3-phospho-D-glycerate pH 7.5, mutants S323A and G362V Escherichia coli
0.69
-
 3-phospho-D-glycerate pH 7.5, mutant G349V Escherichia coli
0.72
-
 3-phospho-D-glycerate pH 7.5, mutant S373A Escherichia coli
0.76
-
 3-phospho-D-glycerate pH 7.5, mutant E345A Escherichia coli
0.79
-
 3-phospho-D-glycerate pH 7.5, mutant H335A Escherichia coli
0.97
-
 3-phospho-D-glycerate pH 7.5, mutant S107A Escherichia coli
1.19
-
 3-phospho-D-glycerate pH 7.5, mutant A143V Escherichia coli
1.37
-
 3-phospho-D-glycerate pH 7.5, mutant S296A Escherichia coli
1.41
-
 3-phospho-D-glycerate pH 7.5, mutants Q298A and N303A Escherichia coli
1.6
-
 3-phospho-D-glycerate pH 7.5, mutant D317A Escherichia coli
1.77
-
 3-phospho-D-glycerate pH 7.5, mutant E307A Escherichia coli
1.99
-
 3-phospho-D-glycerate pH 7.5, mutant E299A Escherichia coli
4.33
-
 3-phospho-D-glycerate pH 7.5, mutant S111A Escherichia coli
4.78
-
 3-phospho-D-glycerate pH 7.5, mutant Q301A Escherichia coli
6.6
-
 3-phospho-D-glycerate pH 7.5, mutant S107A/S111A Escherichia coli
7.2
-
 3-phospho-D-glycerate pH 7.5, mutant G145V Escherichia coli
12
-
 3-phospho-D-glycerate pH 7.5, mutant K311A Escherichia coli
13.1
-
 3-phospho-D-glycerate pH 7.5, mutant N303A/K311A Escherichia coli
16.9
-
 3-phospho-D-glycerate pH 7.5, mutant T297A Escherichia coli
29.1
-
 3-phospho-D-glycerate pH 7.5, mutant K141A Escherichia coli
320
-
 3-phospho-D-glycerate pH 7.5, mutant S111A/K311A Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-phospho-D-glycerate + NAD+ Escherichia coli first step in biosynthesis of L-serine, the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism, residue W139 is involved 3-phosphohydroxypyruvate + NADH
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9T0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-phospho-D-glycerate + NAD+ first step in biosynthesis of L-serine, the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism, residue W139 is involved Escherichia coli 3-phosphohydroxypyruvate + NADH
-
 ?
3-phospho-D-glycerate + NAD+ D-isomer-specific Escherichia coli 3-phosphohydroxypyruvate + NADH
-
 ?

Subunits

Subunits Comment Organism
More the enzyme contains an ACT regulatory domain, enzyme domain structure Escherichia coli

Synonyms

Synonyms Comment Organism
D-3-phosphoglycerate dehydrogenase
-
 Escherichia coli
PGDH
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2
-
 3-phospho-D-glycerate pH 7.5, mutant K141A Escherichia coli
4.2
-
 3-phospho-D-glycerate pH 7.5, mutant S111A/K311A Escherichia coli
4.6
-
 3-phospho-D-glycerate pH 7.5, mutant D317A Escherichia coli
4.9
-
 3-phospho-D-glycerate pH 7.5, mutants E299A and G337V Escherichia coli
5.2
-
 3-phospho-D-glycerate pH 7.5, mutant K311A Escherichia coli
5.8
-
 3-phospho-D-glycerate pH 7.5, mutant R338A Escherichia coli
6
-
 3-phospho-D-glycerate pH 7.5, mutant G349V Escherichia coli
6.4
-
 3-phospho-D-glycerate pH 7.5, mutant G362V Escherichia coli
7
-
 3-phospho-D-glycerate pH 7.5, mutant T297A Escherichia coli
7.4
-
 3-phospho-D-glycerate pH 7.5, mutant S296A Escherichia coli
7.5
-
 3-phospho-D-glycerate pH 7.5, mutant S111A Escherichia coli
7.8
-
 3-phospho-D-glycerate pH 7.5, mutant H335A Escherichia coli
8.6
-
 3-phospho-D-glycerate pH 7.5, mutant A143V Escherichia coli
8.7
-
 3-phospho-D-glycerate pH 7.5, mutant G145V Escherichia coli
9
-
 3-phospho-D-glycerate pH 7.5, mutants S107A and Q361A Escherichia coli
9.3
-
 3-phospho-D-glycerate pH 7.5, mutant P348A Escherichia coli
9.6
-
 3-phospho-D-glycerate pH 7.5, mutant N303A/K311A Escherichia coli
9.8
-
 3-phospho-D-glycerate pH 7.5, mutant H344A Escherichia coli
9.9
-
 3-phospho-D-glycerate pH 7.5, mutant G336V Escherichia coli
10.6
-
 3-phospho-D-glycerate pH 7.5, mutant Q301A Escherichia coli
10.8
-
 3-phospho-D-glycerate pH 7.5, mutant E360A Escherichia coli
11
-
 3-phospho-D-glycerate pH 7.5, mutant S323A Escherichia coli
11.2
-
 3-phospho-D-glycerate pH 7.5, mutant E302A Escherichia coli
11.4
-
 3-phospho-D-glycerate pH 7.5, mutant S107A/S111A Escherichia coli
11.5
-
 3-phospho-D-glycerate pH 7.5, mutants Q298A and S316A Escherichia coli
11.7
-
 3-phospho-D-glycerate pH 7.5, mutant A374V Escherichia coli
11.8
-
 3-phospho-D-glycerate pH 7.5, mutant N364A Escherichia coli
11.9
-
 3-phospho-D-glycerate pH 7.5, mutant E345A Escherichia coli
11.9
-
 3-phospho-D-glycerate pH 7.5, mutant S373A Escherichia coli
12.1
-
 3-phospho-D-glycerate pH 7.5, mutant R347A Escherichia coli
12.3
-
 3-phospho-D-glycerate pH 7.5, mutant E307A Escherichia coli
12.4
-
 3-phospho-D-glycerate pH 7.5, mutant N303A Escherichia coli
12.8
-
 3-phospho-D-glycerate pH 7.5, mutant E387A Escherichia coli
13.1
-
 3-phospho-D-glycerate pH 7.5, mutant D386A Escherichia coli
13.5
-
 3-phospho-D-glycerate pH 7.5, wild-type enzyme Escherichia coli
13.8
-
 3-phospho-D-glycerate pH 7.5, mutant A144V Escherichia coli
14.9
-
 3-phospho-D-glycerate pH 7.5, mutant N346A Escherichia coli
18.7
-
 3-phospho-D-glycerate pH 7.5, mutant Q375A Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli