IPR005952
Phosphoglycerate mutase 1
InterPro entry
Short name | Phosphogly_mut1 |
Overlapping homologous superfamilies | |
family relationships |
Description
Most members of this family are phosphoglycerate mutases (
5.4.2.11)
[2]. This enzyme interconverts 2-phosphoglycerate and 3-phosphoglycerate. 2-phospho-D-glycerate + 2,3-diphosphoglycerate = 3-phospho-D-glycerate + 2,3-diphosphoglycerate. The enzyme is transiently phosphorylated on an active site histidine by 2,3-diphosphoglyerate, which is both substrate and product. Some members of this family have phosphoglycerate mutase as a minor activity and act primarily as a bisphoglycerate mutase, interconverting 2,3-diphosphoglycerate and 1,3-diphosphoglycerate (
5.4.2.4)
[1].
References
1.Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding. Patterson A, Price NC, Nairn J. Acta Crystallogr Sect F Struct Biol Cryst Commun 66, 1415-20, (2010). PMID: 21045285
2.Tyr26 phosphorylation of PGAM1 provides a metabolic advantage to tumours by stabilizing the active conformation. Hitosugi T, Zhou L, Fan J, Elf S, Zhang L, Xie J, Wang Y, Gu TL, Aleckovic M, Leroy G, Kang Y, Kang HB, Seo JH, Shan C, Jin P, Gong W, Lonial S, Arellano ML, Khoury HJ, Chen GZ, Shin DM, Khuri FR, Boggon TJ, Kang S, He C, Chen J. Nat Commun 4, 1790, (2013). View articlePMID: 23653202
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Genome Properties
Representative structure
1qhf: YEAST PHOSPHOGLYCERATE MUTASE-3PG COMPLEX STRUCTURE TO 1.7 A