Beta-phosphoglucomutase: Difference between revisions
Jump to navigation
Jump to search
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
Line 10: | Line 10: | ||
== Structural highlights == | == 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. | |||
</StructureSection> | </StructureSection> | ||
Revision as of 10:19, 11 November 2015
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. DiseaseRelevanceStructural highlightsBPGM 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. |
|
3D Structures of β-phosphoglucomutase3D Structures of β-phosphoglucomutase
Updated on 11-November-2015