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Literature summary 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)

EC Number Cloned (Comment) Organism
1.1.1.95
-
Mycobacterium tuberculosis
1.1.1.95
-
Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.95 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
1.1.1.95 R132K mutation decreases the Km-value for 3-phosphooxypyruvate by approximately 10fold Mycobacterium tuberculosis
1.1.1.95 R72A mutant enzyme utilize 2-oxoglutarate as substrate Mycobacterium tuberculosis
1.1.1.95 R72L mutant enzyme utilize 2-oxoglutarate as substrate Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.95 0.015
-
3-phosphooxypyruvate mutant enzyme R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 0.068
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 0.081
-
3-phosphooxypyruvate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 0.153
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 0.169
-
3-phosphooxypyruvate mutant enzyme R72A/R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 0.45
-
2-oxoglutarate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 5
-
2-oxoglutarate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 30.6
-
2-oxoglutarate mutant enzyme R72L, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 53.1
-
2-oxoglutarate mutant enzyme R72A, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.95 3-phospho-D-glycerate + NAD+ Mycobacterium tuberculosis first step of L-serine biosynthesis 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+ Escherichia coli first step of L-serine biosynthesis 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+ Mycobacterium tuberculosis H37Rv first step of L-serine biosynthesis 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+ Escherichia coli K12 first step of L-serine biosynthesis 3-phosphooxypyruvate + NADH + H+
-
r

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.95
-
Mycobacterium tuberculosis
1.1.1.95
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.95 2-oxoglutarate + NADH + H+
-
Escherichia coli D-2-hydroxyglutarate + NAD+
-
?
1.1.1.95 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+
-
?
1.1.1.95 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+
-
?
1.1.1.95 2-oxoglutarate + NADH + H+
-
Escherichia coli K12 D-2-hydroxyglutarate + NAD+
-
?
1.1.1.95 3-phospho-D-glycerate + NAD+
-
Mycobacterium tuberculosis 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+
-
Escherichia coli 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+ first step of L-serine biosynthesis Mycobacterium tuberculosis 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+ first step of L-serine biosynthesis Escherichia coli 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+
-
Mycobacterium tuberculosis H37Rv 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+ first step of L-serine biosynthesis Mycobacterium tuberculosis H37Rv 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+
-
Escherichia coli K12 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+ first step of L-serine biosynthesis Escherichia coli K12 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phosphooxypyruvate + NADH + H+
-
Mycobacterium tuberculosis 3-phospho-D-glycerate + NAD+
-
r
1.1.1.95 3-phosphooxypyruvate + NADH + H+
-
Escherichia coli 3-phospho-D-glycerate + NAD+
-
r
1.1.1.95 3-phosphooxypyruvate + NADH + H+
-
Mycobacterium tuberculosis H37Rv 3-phospho-D-glycerate + NAD+
-
r
1.1.1.95 3-phosphooxypyruvate + NADH + H+
-
Escherichia coli K12 3-phospho-D-glycerate + NAD+
-
r

Synonyms

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.95 0.49
-
2-oxoglutarate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 2.1
-
2-oxoglutarate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 3.1
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 4.3
-
2-oxoglutarate mutant enzyme R72L, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 9.6
-
3-phosphooxypyruvate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 16.1
-
2-oxoglutarate mutant enzyme R72A, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 458
-
3-phosphooxypyruvate mutant enzyme R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 490
-
3-phosphooxypyruvate mutant enzyme R72A/R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 606
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis

Cofactor

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

General Information

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.95 0.14
-
2-oxoglutarate mutant enzyme R72L, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 0.3
-
2-oxoglutarate mutant enzyme R72A, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 0.98
-
2-oxoglutarate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 4.7
-
2-oxoglutarate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 46
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 120
-
3-phosphooxypyruvate mutant enzyme K141R, pH 7.0, temperature not specified in the publication Escherichia coli
1.1.1.95 2900
-
3-phosphooxypyruvate mutant enzyme R72A/R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 4000
-
3-phosphooxypyruvate wild-type enzyme, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 31000
-
3-phosphooxypyruvate mutant enzyme R132K, pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis