Literature summary for 5.4.2.11 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.

Search for more literature for 5.4.2.11

Activating Compound

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

Cloned(Commentary)

Cloned (Comment)	Organism
-	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
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]

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

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.078	-	3-phosphoglycerate	mutant H181A	Saccharomyces cerevisiae
490	-	3-phosphoglycerate	wild-type enzyme	Saccharomyces cerevisiae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)