Catalog # or name ...
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.
Phosphoglycerate mutase 1
262 amino acids
Ligand Chemical Component
citric acid; chloride ion
PGAMA; PGAM-B; PGAM1; RP11-452K12.8; OTTHUMP00000020190; OTTHUMP00000059414; phosphoglycerate mutase A, nonmuscle form; EC 188.8.131.52,EC 184.108.40.206,EC 220.127.116.11; BPG-dependent PGAM 1; Phosphoglycerate mutase isozyme B; phosphoglycerate mutase A, nonmuscle form
bisphosphoglycerate 2-phosphatase activity; bisphosphoglycerate mutase activity; hydrolase activity; isomerase activity; phosphoglycerate mutase activity; protein kinase binding
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
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