Beta-phosphoglucomutase: Difference between revisions

Revision as of 16:47, 16 November 2015

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 .

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

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 == 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 active site is located in the core domain and contains a phosphorylated Asp residue and the octahedral coordinated Mg+2 ion.
+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/6'>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>.
 </StructureSection>