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/7'>active site</scene> is located in the core domain and contains a <scene name='59/595758/Cv/8'>phosphorylated Asp residue and the octahedral coordinated Mg+2 ion</scene>. <ref>PMID:12081483</ref>
BPGM structure shows the enzyme having <scene name='59/595758/Cv/9'>2 domains</scene>. A <scene name='59/595758/Cv/10'>helical cap domain</scene> and an <scene name='59/595758/Cv/11'>α/β core domain</scene>. The <scene name='59/595758/Cv/12'>active site</scene> is located in the core domain and contains a <scene name='59/595758/Cv/13'>phosphorylated Asp residue and the octahedral coordinated Mg+2 ion</scene>. <ref>PMID:12081483</ref>
</StructureSection>
</StructureSection>



Revision as of 13:56, 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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