|
|
Line 7: |
Line 7: |
| == Structural highlights == | | == Structural highlights == |
|
| |
|
| BPGM structure shows the enzyme having <scene name='59/595758/Cv/2'>2 domains</scene>. A <scene name='59/595758/Cv/3'>helical cap domain</scene> and an <scene name='59/595758/Cv/4'>α/β core domain</scene>. The <scene name='59/595758/Cv/7'>active site</scene> is located in the core domain and contains a <scene name='59/595758/Cv/8'>phosphorylated Asp residue and the octahedral coordinated Mg+2 ion</scene>. <ref>PMID:12081483</ref> | | BPGM structure shows the enzyme having <scene name='59/595758/Cv/9'>2 domains</scene>. A <scene name='59/595758/Cv/10'>helical cap domain</scene> and an <scene name='59/595758/Cv/11'>α/β core domain</scene>. The <scene name='59/595758/Cv/12'>active site</scene> is located in the core domain and contains a <scene name='59/595758/Cv/13'>phosphorylated Asp residue and the octahedral coordinated Mg+2 ion</scene>. <ref>PMID:12081483</ref> |
| </StructureSection> | | </StructureSection> |
|
| |
|
Revision as of 13:56, 8 January 2019
FunctionBeta-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 highlightsBPGM structure shows the enzyme having . A and an . The is located in the core domain and contains a . [1]
| |
3D Structures of β-phosphoglucomutase3D Structures of β-phosphoglucomutase
Updated on 08-January-2019
{"openlevels":0}
- β-phosphoglucomutase
- 3nas – BPGM – Bacillus subtilis
- 4g9b – BPGM + Mg – Escherichia coli
- 1zol, 2whe – LlBPGM + Mg – Lactococcus lactis
- 3fm9 – LlBPGM (mutant) + Mg
- 5olw – LlBPGM + Ca
- 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, 5olx, 5oly – 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
ReferencesReferences
- ↑ 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
proteopedia link