Beta-phosphoglucomutase

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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.

Structure of phosphorylated β-phosphoglucomutase complex with Mg+2 ion (PDB code 1lvh).

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3D Structures of β-phosphoglucomutase3D Structures of β-phosphoglucomutase

Updated on 16-November-2015

ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky