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Literature summary for 1.1.1.95 extracted from

  • Xu, X.L.; Grant, G.A.
    Determinants of substrate specificity in D-3-phosphoglycerate dehydrogenase. Conversion of the M. tuberculosis enzyme from one that does not use alpha-ketoglutarate as a substrate to one that does (2019), Arch. Biochem. Biophys., 671, 218-224 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Mycobacterium tuberculosis
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
K141R kcat/KM for 2-oxoglutarate is 4.8fold lower than the value for the wild-type enzyme, kcat/KM for 3-phosphooxypyruvate is 2.6fold higher than the value for the wild-type enzyme Escherichia coli
R132K mutation decreases the Km-value for 3-phosphooxypyruvate by approximately 10fold Mycobacterium tuberculosis
R72A mutant enzyme utilize 2-oxoglutarate as substrate Mycobacterium tuberculosis
R72L mutant enzyme utilize 2-oxoglutarate as substrate Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.015
-
3-phosphooxypyruvate mutant enzyme R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
0.068
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
0.081
-
3-phosphooxypyruvate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
0.153
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
0.169
-
3-phosphooxypyruvate mutant enzyme R72A/R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
0.45
-
2-oxoglutarate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
5
-
2-oxoglutarate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
30.6
-
2-oxoglutarate mutant enzyme R72L, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
53.1
-
2-oxoglutarate mutant enzyme R72A, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-phospho-D-glycerate + NAD+ Mycobacterium tuberculosis first step of L-serine biosynthesis 3-phosphooxypyruvate + NADH + H+
-
r
3-phospho-D-glycerate + NAD+ Escherichia coli first step of L-serine biosynthesis 3-phosphooxypyruvate + NADH + H+
-
r
3-phospho-D-glycerate + NAD+ Mycobacterium tuberculosis H37Rv first step of L-serine biosynthesis 3-phosphooxypyruvate + NADH + H+
-
r
3-phospho-D-glycerate + NAD+ Escherichia coli K12 first step of L-serine biosynthesis 3-phosphooxypyruvate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9T0
-
-
Escherichia coli K12 P0A9T0
-
-
Mycobacterium tuberculosis P9WNX3
-
-
Mycobacterium tuberculosis H37Rv P9WNX3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mycobacterium tuberculosis
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + NADH + H+
-
Escherichia coli D-2-hydroxyglutarate + NAD+
-
?
2-oxoglutarate + NADH + H+ wild-type enzyme shows no activity. Mutant enzymes R72A and R72L utilize 2-oxoglutarate as substrate Mycobacterium tuberculosis D-2-hydroxyglutarate + NAD+
-
?
2-oxoglutarate + NADH + H+ wild-type enzyme shows no activity. Mutant enzymes R72A and R72L utilize 2-oxoglutarate as substrate Mycobacterium tuberculosis H37Rv D-2-hydroxyglutarate + NAD+
-
?
2-oxoglutarate + NADH + H+
-
Escherichia coli K12 D-2-hydroxyglutarate + NAD+
-
?
3-phospho-D-glycerate + NAD+
-
Mycobacterium tuberculosis 3-phosphooxypyruvate + NADH + H+
-
r
3-phospho-D-glycerate + NAD+
-
Escherichia coli 3-phosphooxypyruvate + NADH + H+
-
r
3-phospho-D-glycerate + NAD+ first step of L-serine biosynthesis Mycobacterium tuberculosis 3-phosphooxypyruvate + NADH + H+
-
r
3-phospho-D-glycerate + NAD+ first step of L-serine biosynthesis Escherichia coli 3-phosphooxypyruvate + NADH + H+
-
r
3-phospho-D-glycerate + NAD+
-
Mycobacterium tuberculosis H37Rv 3-phosphooxypyruvate + NADH + H+
-
r
3-phospho-D-glycerate + NAD+ first step of L-serine biosynthesis Mycobacterium tuberculosis H37Rv 3-phosphooxypyruvate + NADH + H+
-
r
3-phospho-D-glycerate + NAD+
-
Escherichia coli K12 3-phosphooxypyruvate + NADH + H+
-
r
3-phospho-D-glycerate + NAD+ first step of L-serine biosynthesis Escherichia coli K12 3-phosphooxypyruvate + NADH + H+
-
r
3-phosphooxypyruvate + NADH + H+
-
Mycobacterium tuberculosis 3-phospho-D-glycerate + NAD+
-
r
3-phosphooxypyruvate + NADH + H+
-
Escherichia coli 3-phospho-D-glycerate + NAD+
-
r
3-phosphooxypyruvate + NADH + H+
-
Mycobacterium tuberculosis H37Rv 3-phospho-D-glycerate + NAD+
-
r
3-phosphooxypyruvate + NADH + H+
-
Escherichia coli K12 3-phospho-D-glycerate + NAD+
-
r

Synonyms

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.49
-
2-oxoglutarate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
2.1
-
2-oxoglutarate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
3.1
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
4.3
-
2-oxoglutarate mutant enzyme R72L, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
9.6
-
3-phosphooxypyruvate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
16.1
-
2-oxoglutarate mutant enzyme R72A, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
458
-
3-phosphooxypyruvate mutant enzyme R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
490
-
3-phosphooxypyruvate mutant enzyme R72A/R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
606
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Mycobacterium tuberculosis
NAD+
-
Escherichia coli
NADH
-
Mycobacterium tuberculosis
NADH
-
Escherichia coli

General Information

General Information Comment Organism
metabolism first step of L-serine biosynthesis Mycobacterium tuberculosis
metabolism first step of L-serine biosynthesis Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.14
-
2-oxoglutarate mutant enzyme R72L, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
0.3
-
2-oxoglutarate mutant enzyme R72A, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
0.98
-
2-oxoglutarate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
4.7
-
2-oxoglutarate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
46
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
120
-
3-phosphooxypyruvate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
2900
-
3-phosphooxypyruvate mutant enzyme R72A/R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
4000
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
31000
-
3-phosphooxypyruvate mutant enzyme R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis