Beta-phosphoglucomutase
From Proteopedia
(Difference between revisions)
(New page: <StructureSection load='2wf5' size='340' side='right' caption='Structure of β-phosphoglucomutase complex with β-D-glucose-6-phosphate, MgF3 and Mg+2 ion (PDB code 2wf5).' scene=''> ...) |
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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/14'> | |
- | <StructureSection load=' | + | |
== Function == | == Function == | ||
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'''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. | '''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 <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> |
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== 3D Structures of β-phosphoglucomutase == | == 3D Structures of β-phosphoglucomutase == | ||
+ | [[Beta-phosphoglucomutase 3D structures]] | ||
- | + | </StructureSection> | |
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== References == | == References == |
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