Structural highlights
Function
PMG1_YEAST Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of yeast phosphoglycerate mutase determined by X-ray crystallographic and amino acid sequence studies has been interpreted in terms of the chemical, kinetic and mechanistic observations made on this enzyme. There are two histidine residues at the active site, with imidazole groups almost parallel to each other and approximately 0.4 nm apart, positioned close to the 2 and 3 positions of the substrate. The simplest interpretation of the available information suggests that a ping-pong type mechanism operates in which at least one of these histidine residues participates in the phosphoryl transfer reaction. The flexible C-terminal region also plays an important role in the enzymic reaction.
Structure and activity of phosphoglycerate mutase.,Winn SI, Watson HC, Harkins RN, Fothergill LA Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26;293(1063):121-30. PMID:6115412[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Winn SI, Watson HC, Harkins RN, Fothergill LA. Structure and activity of phosphoglycerate mutase. Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26;293(1063):121-30. PMID:6115412
