Beta-phosphoglucomutase
From Proteopedia
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3D Structures of β-phosphoglucomutase
Updated on 08-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 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] | ||||||||||||
Updated on 08-January-2019
This page was last modified 10:57, 8 January 2019.