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Your query returned 1 entry. Printable version
EC | 5.4.2.11 | ||||||||||||||
Accepted name: | phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) | ||||||||||||||
Reaction: | 2-phospho-D-glycerate = 3-phospho-D-glycerate (overall reaction) (1a) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-N (1b) [enzyme]-N (1c) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-N (1d) [enzyme]-N |
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For diagram of the Entner-Doudoroff pathway, click here | |||||||||||||||
Glossary: | 2/3-phospho-D-glycerate = 2-phospho-D-glycerate or 3-phospho-D-glycerate | ||||||||||||||
Other name(s): | glycerate phosphomutase (diphosphoglycerate cofactor); 2,3-diphosphoglycerate dependent phosphoglycerate mutase; cofactor dependent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); MPGM; PGAM; PGAM-d; PGM; dPGM | ||||||||||||||
Systematic name: | D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-dependent) | ||||||||||||||
Comments: | The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi 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. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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