| EC |
5.4.2.6 |
| Accepted name: |
β-phosphoglucomutase |
| Reaction: |
β-D-glucose 1-phosphate = β-D-glucose 6-phosphate |
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For diagram of reaction, click here |
| Other name(s): |
β-pgm (gene name) |
| Systematic name: |
β-D-glucose 1,6-phosphomutase |
| Comments: |
The enzyme requires Mg2+ and phosphorylation of an aspartate residue at the active site. The enzyme is able to autophosphorylate itself with its substrate β-D-glucose 1-phosphate. Although this is a slow reaction, only a single turnover is required for activation. Once the phosphorylated enzyme is formed, it generates the reaction intermediate β-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles [4]. cf. EC 5.4.2.2, phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent). |
| Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 68651-99-0 |
| References: |
| 1. |
Ben-Zvi, R. and Schramm, M. A phosphoglucomutase specific for β-glucose 1-phosphate. J. Biol. Chem. 236 (1961) 2186–2189. |
| 2. |
Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, 1972, pp. 407–477. |
| 3. |
Lahiri, S.D., Zhang, G., Dunaway-Mariano, D. and Allen, K.N. The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction. Science 299 (2003) 2067–2071. [DOI] [PMID: 12637673] |
| 4. |
Dai, J., Wang, L., Allen, K.N., Radstrom, P. and Dunaway-Mariano, D. Conformational cycling in β-phosphoglucomutase catalysis: reorientation of the β-D-glucose 1,6-(Bis)phosphate intermediate. Biochemistry 45 (2006) 7818–7824. [DOI] [PMID: 16784233] |
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| [EC 5.4.2.6 created 1984] |
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