Beta-phosphoglucomutase: Difference between revisions
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==Structural studies== |
==Structural studies== |
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20 [[tertiary structure|structures]] have been solved for this enzyme [[Protein Data Bank|PDB]]. Some of the accession codes are {{PDB link|1LVH}}, {{PDB link|1O03}}, {{PDB link|1O08}}, {{PDB link|1Z4N}}, {{PDB link|1Z4O}}, and {{PDB link|1ZOL}}. Most of these structures detail metal fluoride analogue complexes which are used to mimic different states along the reaction coordinate. |
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==References== |
==References== |
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Revision as of 13:10, 6 June 2015
| beta-phosphoglucomutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.2.6 | ||||||||
| CAS no. | 68651-99-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a beta-phosphoglucomutase (EC 5.4.2.6) is an enzyme that catalyzes the chemical reaction
- beta-D-glucose 1-phosphate beta-D-glucose 6-phosphate
Hence, this enzyme has one substrate, beta-D-glucose 1-phosphate, and one product, beta-D-glucose 6-phosphate.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is beta-D-glucose 1,6-phosphomutase. This enzyme participates in starch and sucrose metabolism.
Structural studies
20 structures have been solved for this enzyme PDB. Some of the accession codes are 1LVH, 1O03, 1O08, 1Z4N, 1Z4O, and 1ZOL. Most of these structures detail metal fluoride analogue complexes which are used to mimic different states along the reaction coordinate.
References
- Ben-Zvi R and Schramm M (1961). "A phosphoglucomutase specific for beta-glucose 1-phosphate". J. Biol. Chem. 236: 2186–2189.
- Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.