Beta-phosphoglucomutase: Difference between revisions
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== 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/ | 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/5'>active site</scene> is located in the core domain and contains a <scene name='59/595758/Cv/6'>phosphorylated Asp residue and the octahedral coordinated Mg+2 ion</scene>. <ref>PMID:12081483</ref> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 16:50, 16 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. Structural highlightsBPGM structure shows the enzyme having . A and an . The is located in the core domain and contains a . [1] |
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3D Structures of β-phosphoglucomutase3D Structures of β-phosphoglucomutase
Updated on 16-November-2015