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Literature summary extracted from

  • White, M.; Fothergill-Gilmore L.A.
    Mutase versus synthase: the phosphoglycerate mutase family studied by protein engineering (1990), Biochem. Soc. Trans., 18, 257.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.4.2.11 2,3-diphosphoglycerate Km: 0.005, wild-type enzyme, Km: 0.003, mutant K246G, Km: 0.048, mutant S11G Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
5.4.2.11 K246G mutant enzymes in which Ser11 is replaced by Gly, i.e. S11G and Lys246 by Gly, i.e. K246G do not have significantly altered kinetic values Saccharomyces cerevisiae
5.4.2.11 S11G mutant enzymes in which Ser11 is replaced by Gly, i.e. S11G and Lys246 by Gly, i.e. K246G do not have significantly altered kinetic values Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.4.2.11 0.041
-
 2-phosphoglycerate wild-type enzyme Saccharomyces cerevisiae
5.4.2.11 0.06
-
 2-phosphoglycerate mutant K246G Saccharomyces cerevisiae
5.4.2.11 0.067
-
 2-phosphoglycerate mutant S11G Saccharomyces cerevisiae
5.4.2.11 0.65
-
 3-phosphoglycerate wild-type enzyme Saccharomyces cerevisiae
5.4.2.11 0.67
-
 3-phosphoglycerate mutant S11G Saccharomyces cerevisiae
5.4.2.11 0.68
-
 3-phosphoglycerate mutant K246G Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.2.11 3-Phosphoglycerate Saccharomyces cerevisiae glycolysis/gluconeogenesis ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.4.2.11 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.2.11 2-phospho-D-glycerate = 3-phospho-D-glycerate mechanism: after the active site His-8 is phosphorylated by the cofactor 2,3-diphosphoglycerate a substrate molecule binds. Subsequently a phospho-transfer takes place via a ping-pong-mechanism. After release of the product the enzyme remains phosphorylated and catalytically competent Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.2.11 2-Phosphoglycerate
-
 Saccharomyces cerevisiae 3-Phosphoglycerate
-
 ?
5.4.2.11 3-Phosphoglycerate
-
 Saccharomyces cerevisiae 2-Phosphoglycerate
-
 ?
5.4.2.11 3-Phosphoglycerate glycolysis/gluconeogenesis Saccharomyces cerevisiae ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.4.2.11 2.1
-
 3-phosphoglycerate mutant S11G Saccharomyces cerevisiae
5.4.2.11 324
-
 3-phosphoglycerate mutant K246G Saccharomyces cerevisiae
5.4.2.11 384
-
 3-phosphoglycerate wild-type enzyme Saccharomyces cerevisiae