Beta-phosphoglucomutase: Difference between revisions
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<StructureSection load='1lvh' size=' | <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 == | ||
'''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 == | == Structural highlights == | ||
BPGM structure shows the enzyme having 2 domains. | 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> | ||
</ | |||
== 3D Structures of β-phosphoglucomutase == | == 3D Structures of β-phosphoglucomutase == | ||
[[Beta-phosphoglucomutase 3D structures]] | |||
</StructureSection> | |||
== References == | == References == |