| Entry |
|
| Name |
2,3-bisphosphoglycerate 3-phosphatase;
MIPP1;
2,3-BPG 3-phosphatase
|
| Class |
Hydrolases;
Acting on ester bonds;
Phosphoric-monoester hydrolases
 |
| Sysname |
2,3-bisphospho-D-glycerate 3-phosphohydrolase
|
| Reaction(IUBMB) |
2,3-bisphospho-D-glycerate + H2O = 2-phospho-D-glycerate + phosphate [RN: R09532]
|
| Reaction(KEGG) |
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| Substrate |
|
| Product |
|
| Comment |
This reaction is a shortcut in the Rapoport-Luebering shunt. It bypasses the reactions of EC 3.1.3.13/EC 5.4.2.1 (bisphosphoglycerate phosphatase/phosphoglycerate mutase) and directly forms 2-phospho-D-glycerate by removing the 3-phospho-group of 2,3-diphospho-D-glycerate [1]. The MIPP1 protein also catalyses the reaction of EC 3.1.3.62 (multiple inositol-polyphosphate phosphatase).
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| Reference |
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| Authors |
Cho J, King JS, Qian X, Harwood AJ, Shears SB |
| Title |
Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt. |
| Journal |
Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 5998-6003. |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |