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Function
Beta-phosphoglucomutase (BPGM) catalyzes the conversion of β-D-glucose 1-phosphate to β-D-glucose 6-phosphate. Mg+2 ion is the cofactor of the reaction and BPGM activation is achieved by Asp8 phosphorylation (D8P). α-D-galactose-1-phosphate is an inhibitor of BPGM. BPGM participates in sugar and starch metabolism.
Structural highlights
BPGM structure shows the enzyme having 2 domains. A helical cap domain and an α/β core domain. The active site is located in the core domain and contains a phosphorylated Asp residue and the octahedral coordinated Mg+2 ion. [1]
- ↑ Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN. Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis. Biochemistry. 2002 Jul 2;41(26):8351-9. PMID:12081483
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3D Structures of β-phosphoglucomutase
Updated on 30-November-2015
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- β-phosphoglucomutase
- 3nas – BPGM – Bacillus subtilis
- 4g9b – BPGM + Mg – Escherichia coli
- 1zol, 2whe – LlBPGM + Mg – Lactococcus lactis
- 3fm9 – LlBPGM (mutant) + Mg
- 2wfa – LlBPGM + BeF3 + Mg
- 1lvh – LlBPGM + D8P + Mg
- 3dv9 – BPGM + Mg – Bacterioides vulgatus
- 4gib – BPGM – Clostridium difficile
- 4uw9 – BPGM + Mg – Pyrococcusus
- β-phosphoglucomutase complex with glucophosphate derivatives
- 1o03, 1o08 – LlBPGM + α-D-glucose 1,6-bisphosphate + Mg
- 1z4n, 1z4o – LlBPGM + α-D-galactose-1-phosphate + Mg
- 2wf5 – LlBPGM + β-D-glucose-6-phosphate + MgF3 + Mg
- 3zi4 – LlBPGM + β-D-glucose-6-phosphate + ScF4 + Mg
- 2wf6 – LlBPGM + β-D-glucose-6-phosphate + AlF4 + Mg
- 2wf7 – LlBPGM + dideoxy-phosphono-β-D-gluco-heptopyranose + AlF4 + Mg
- 4c4r, 4c4s – LlBPGM + β-phosphonomethylene-D-glucopyranose derivative + MgF3 + Mg
- 4c4t – LlBPGM + β-phosphonomethylene-D-glucopyranose derivative + AlF4 + Mg
- 2wf8 – LlBPGM + β-D-glucose-6-phosphate + α-D-glucose-1-phosphate + BeF3 + Mg
- 2wf9 – LlBPGM + β-D-glucose-6-phosphate + α-D-glucose-6-phosphate + BeF3 + Mg
References
