Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • White, M.F.; Fothergill-Gilmore, L.A.
    Development of a mutagenesis, expression and purification system for yeast phosphoglycerate mutase (1992), Eur. J. Biochem., 207, 709-714.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.4.2.11 2,3-diphosphoglycerate Km: 0.0081, wild-type enzyme, Km: 0.087, H181A-mutant Saccharomyces cerevisiae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.2.11
-
Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
5.4.2.11 H181A His181 is substituted by Ala in site-directed mutagenesis. The resulting enzyme has a reduced activity and still requires 2,3-diphosphoglycerate. His181 seems to be important for cofactor-binding Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.4.2.11 0.026
-
3-phosphoglycerate H181A mutant Saccharomyces cerevisiae
5.4.2.11 0.74
-
3-phosphoglycerate wild-type enzyme Saccharomyces cerevisiae

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.2.11
-
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 0.078
-
3-phosphoglycerate mutant H181A Saccharomyces cerevisiae
5.4.2.11 490
-
3-phosphoglycerate wild-type enzyme Saccharomyces cerevisiae