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Literature summary extracted from

  • Johnson, C.M.; Price, N.C.
    How similar are the phosphoglycerate mutases from yeast and rabbit muscle? (1987), Biochem. Soc. Trans., 15, 247-248.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.4.2.11 2,3-diphosphoglycerate
-
Saccharomyces cerevisiae
5.4.2.11 2,3-diphosphoglycerate
-
Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.2.11 2,3-Butanedione
-
Oryctolagus cuniculus
5.4.2.11 2,3-Butanedione
-
Saccharomyces cerevisiae
5.4.2.11 diethyldicarbonate
-
Oryctolagus cuniculus
5.4.2.11 diethyldicarbonate
-
Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
5.4.2.11 Oryctolagus cuniculus
-
-
-
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 ping-pong mechanism via a phosphorylated His-intermediate Saccharomyces cerevisiae
5.4.2.11 2-phospho-D-glycerate = 3-phospho-D-glycerate ping-pong mechanism via a phosphorylated His-intermediate Oryctolagus cuniculus

Renatured (Commentary)

EC Number Renatured (Comment) Organism
5.4.2.11 renatured after denaturation with guanidine-HCl Saccharomyces cerevisiae
5.4.2.11 renatured after denaturation with guanidine-HCl Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.4.2.11 muscle
-
Oryctolagus cuniculus
-

Subunits

EC Number Subunits Comment Organism
5.4.2.11 dimer
-
Oryctolagus cuniculus