CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.50 | Rossmann fold | |
3.40.50.1240 | Phosphoglycerate mutase-like |
Domain Context
CATH Clusters
Superfamily | Phosphoglycerate mutase-like |
Functional Family | Phosphoglycerate mutase 1 |
Enzyme Information
5.4.2.4 |
Bisphosphoglycerate mutase.
based on mapping to UniProt P07738
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
-!- In the direction shown, the enzyme is phosphorylated by 3-phosphoglyceroyl phosphate to give phosphoenzyme and 3-phosphoglycerate. -!- The latter is rephosphorylated by the enzyme to yield 2,3- diphosphoglycerate, but this reaction is slowed down by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. -!- Also catalyzes, slowly, the reaction of EC 5.4.2.12. -!- Formerly EC 2.7.5.4.
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5.4.2.11 |
Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).
based on mapping to UniProt P07738
2-phospho-D-glycerate = 3-phospho-D-glycerate.
-!- The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some 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 (His(10) in man and Escherichia coli, His(8) 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. -!- The enzyme has no requirement for metal ions. -!- This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1.
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UniProtKB Entries (1)
P07738 |
PMGE_HUMAN
Homo sapiens
Bisphosphoglycerate mutase
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PDB Structure
PDB | 2H4X |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.
J.Biol.Chem.
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