Beta-phosphoglucomutase: Difference between revisions
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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> | 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 == | |||
[[Beta-phosphoglucomutase 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
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**[[5olw]] – LlBPGM + Ca <br /> | **[[5olw]] – LlBPGM + Ca <br /> | ||
**[[2wfa]] – LlBPGM + BeF3 + Mg <br /> | **[[2wfa]] – LlBPGM + BeF3 + Mg <br /> | ||
**[[5ojz]] – LlBPGM (mutant) + BeF3 + Mg <br /> | |||
**[[1lvh]] – LlBPGM + D8P + Mg <br /> | **[[1lvh]] – LlBPGM + D8P + Mg <br /> | ||
**[[3dv9]] – BPGM + Mg – ''Bacterioides vulgatus''<br /> | **[[3dv9]] – BPGM + Mg – ''Bacterioides vulgatus''<br /> | ||
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**[[1o03]], [[1o08]] – LlBPGM + α-D-glucose 1,6-bisphosphate + Mg <br /> | **[[1o03]], [[1o08]] – LlBPGM + α-D-glucose 1,6-bisphosphate + Mg <br /> | ||
**[[5ok0]] – LlBPGM (mutant) + α-D-glucose 1,6-bisphosphate + Mg <br /> | |||
**[[5ok1]] – LlBPGM (mutant) + α-D-glucose 1,6-bisphosphate + Mg <br /> | |||
**[[1z4n]], [[1z4o]] – LlBPGM + α-D-galactose-1-phosphate + Mg <br /> | **[[1z4n]], [[1z4o]] – LlBPGM + α-D-galactose-1-phosphate + Mg <br /> | ||
**[[2wf5]], [[5olx]], [[5oly]] – LlBPGM + β-D-glucose-6-phosphate + MgF3 + Mg <br /> | **[[2wf5]], [[5olx]], [[5oly]] – LlBPGM + β-D-glucose-6-phosphate + MgF3 + Mg <br /> | ||
**[[3zi4]] – LlBPGM + β-D-glucose-6-phosphate + ScF4 + Mg <br /> | **[[3zi4]] – LlBPGM + β-D-glucose-6-phosphate + ScF4 + Mg <br /> | ||
**[[2wf6]] – LlBPGM + β-D-glucose-6-phosphate + AlF4 + Mg <br /> | **[[2wf6]] – LlBPGM + β-D-glucose-6-phosphate + AlF4 + Mg <br /> | ||
**[[5o6r]] – LlBPGM (mutant) + β-D-glucose-1-phosphate + AlF4 + Mg <br /> | |||
**[[5ok2]] – LlBPGM (mutant) + β-D-glucose-6-phosphate + AlF4 + Mg <br /> | |||
**[[2wf7]] – LlBPGM + dideoxy-phosphono-β-D-gluco-heptopyranose + AlF4 + Mg <br /> | **[[2wf7]] – LlBPGM + dideoxy-phosphono-β-D-gluco-heptopyranose + AlF4 + Mg <br /> | ||
**[[4c4r]], [[4c4s]] – LlBPGM + β-phosphonomethylene-D-glucopyranose derivative + MgF3 + Mg <br /> | **[[4c4r]], [[4c4s]] – LlBPGM + β-phosphonomethylene-D-glucopyranose derivative + MgF3 + Mg <br /> | ||
Revision as of 10:17, 10 April 2019
FunctionBeta-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 highlightsBPGM structure shows the enzyme having . A and an . The is located in the core domain and contains a . [1] 3D Structures of β-phosphoglucomutaseBeta-phosphoglucomutase 3D structures
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3D Structures of β-phosphoglucomutase3D Structures of β-phosphoglucomutase
Updated on 10-April-2019