Beta-phosphoglucomutase: Difference between revisions

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<StructureSection load='1lvh' size='350' side='right' caption='Structure of phosphorylated β-phosphoglucomutase complex with Mg+2 ion (PDB code [[1lvh]]).' scene='59/595758/Cv/1'>
<StructureSection load='1lvh' size='350' side='right' caption='Structure of phosphorylated β-phosphoglucomutase complex with Mg+2 ion (PDB code [[1lvh]]).' scene='59/595758/Cv/14'>


== Function ==
== Function ==

Revision as of 13:57, 8 January 2019


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 . A and an . The is located in the core domain and contains a . [1]

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 08-January-2019

ReferencesReferences

  1. 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

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