Phosphoglycerate Mutase 1


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Phosphoglycerate Mutase 1

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Cat. No. : CBCRY11
Background : The B-type cofactor-dependent phosphoglycerate mutase (dPGM-B) catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in glycolysis and gluconeogenesis pathways using 2,3-bisphosphoglycerate as the cofactor. The crystal structures of human dPGM-B bound with citrate were determined in two crystal forms. These structures reveal a dimerization mode conserved in both of dPGM and BPGM (bisphosphoglycerate mutase), based on which a dPGM/BPGM heterodimer structure is proposed. Structural comparison supports that the conformational changes of residues 13-21 and 98-117 determine PGM/BPGM activity differences.
Protein Classification : isomerase hydrase
Structure Weight : 361525.84
Polymer : 1
Molecule : Phosphoglycerate mutase 1
Chain Length : 262 amino acids
MMDB ID : 33356
Source : E.coli
Method : X-Ray Diffraction
Resolution : 2.8?
Ligand Chemical Component : citric acid; chloride ion
Reference : Wang, Y., Wei, Z., Liu, L., Cheng, Z., Lin, Y., Ji, F., Gong, W.(2005) Crystal structure of human B-type phosphoglycerate mutase bound with citrate. Biochem.Biophys.Res.Commun. 331: 1207-1215
Gene Name : PGAM1
Synonyms : PGAMA; PGAM-B; PGAM1; RP11-452K12.8; OTTHUMP00000020190; OTTHUMP00000059414; phosphoglycerate mutase A, nonmuscle form; EC,EC,EC; BPG-dependent PGAM 1; Phosphoglycerate mutase isozyme B; phosphoglycerate mutase A, nonmuscle form
UniProt ID : P18669
Gene ID : 5223
Chromosome Location : 10q25.3
Function : bisphosphoglycerate 2-phosphatase activity; bisphosphoglycerate mutase activity; hydrolase activity; isomerase activity; phosphoglycerate mutase activity; protein kinase binding
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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