bisphosphoglycerate/phosphoglycerate mutase [EC:5.4.2.4 5.4.2.11]

PMID:15258155

Wang Y, Wei Z, Bian Q, Cheng Z, Wan M, Liu L, Gong W

Crystal structure of human bisphosphoglycerate mutase.

J Biol Chem 279:39132-8 (2004)
DOI:10.1074/jbc.M405982200

[hsa:669]

Isomerases;
Intramolecular transferases;
Phosphotransferases (phosphomutases)

D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-dependent)

2-phospho-D-glycerate = 3-phospho-D-glycerate (overall reaction) [RN:R01518];
(1a) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-Ntau-phospho-L-histidine + 2/3-phospho-D-glycerate [RN:R01516];
(1b) [enzyme]-Ntau-phospho-L-histidine + 2-phospho-D-glycerate = [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate;
(1c) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-Ntau-phospho-L-histidine + 3-phospho-D-glycerate;
(1d) [enzyme]-Ntau-phospho-L-histidine + 2/3-bisphospho-D-glycerate = [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate

R01516 R01518

2-phospho-D-glycerate [CPD:C00631];
[enzyme]-L-histidine;
2,3-bisphospho-D-glycerate [CPD:C01159];
[enzyme]-Ntau-phospho-L-histidine;
2/3-bisphospho-D-glycerate

The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.

EC 5.4.2.11 created 1961 as EC 5.4.2.1 (EC 2.7.5.3 created 1961, incorporated 1984) transferred 2013 to 5.4.2.11, modified 2014