Enzymes
| UniProtKB help_outline | 2,245 proteins |
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| GO Molecular Function help_outline |
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- Name help_outline (2R)-3-phospho-glyceroyl phosphate Identifier CHEBI:57604 Charge -4 Formula C3H4O10P2 InChIKeyhelp_outline LJQLQCAXBUHEAZ-UWTATZPHSA-J SMILEShelp_outline O[C@H](COP([O-])([O-])=O)C(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2R)-2,3-bisphosphoglycerate Identifier CHEBI:58248 Charge -5 Formula C3H3O10P2 InChIKeyhelp_outline XOHUEYCVLUUEJJ-UWTATZPHSA-I SMILEShelp_outline [O-]C(=O)[C@@H](COP([O-])([O-])=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,717 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:17765 | RHEA:17766 | RHEA:17767 | RHEA:17768 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The enzymology of 2,3-bisphosphoglycerate.
Rose Z.B.
Adv Enzymol Relat Areas Mol Biol 51:211-253(1980) [PubMed] [EuropePMC]
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Crystal structure of human B-type phosphoglycerate mutase bound with citrate.
Wang Y., Wei Z., Liu L., Cheng Z., Lin Y., Ji F., Gong W.
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 determi ... >> More
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. The citrate-binding mode suggests a substrate-binding model, consistent with the structure of Escherichia coli dPGM/vanadate complex. A chloride ion was found in the center of the dimer, providing explanation for the contribution of chloride ion to dPGM activities. Based on the structural information, the possible reasons for the deficient human dPGM mutations found in some patients are also discussed. << Less
Biochem. Biophys. Res. Commun. 331:1207-1215(2005) [PubMed] [EuropePMC]