Member database | CATH-Gene3D |
CATH-Gene3D type | homologous superfamily |
Description Imported from IPR043169
Phosphomannomutase (PMM) catalyses the conversion of mannose-6-phosphate to mannose-1-phosphate, an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes
[2]. Bacterial alpha-phosphoglucomutases share an overall fold similar to that of eukaryotic phosphomannomutases
[1]. PMM can be divided into two domains: the cap and core. This entry represents the cap domain. The heart of the cap domain is a four-stranded antiparallel β-sheet elaborated on one face with three α-helices
[2].
References Imported from IPR043169
1.High-resolution structure of an atypical α-phosphoglucomutase related to eukaryotic phosphomannomutases. Nogly P, Matias PM, de Rosa M, Castro R, Santos H, Neves AR, Archer M. Acta Crystallogr. D Biol. Crystallogr. 69, 2008-16, (2013). PMID: 24100319
2.Structure of Leishmania mexicana phosphomannomutase highlights similarities with human isoforms. Kedzierski L, Malby RL, Smith BJ, Perugini MA, Hodder AN, Ilg T, Colman PM, Handman E. J. Mol. Biol. 363, 215-27, (2006). View articlePMID: 16963079