Structural highlights
Function
[CEEP_RUMA7] Catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man).[HAMAP-Rule:MF_00929]
Publication Abstract from PubMed
Enzymatic epimerization is an important modification for carbohydrates to acquire diverse functions attributable to their stereoisomers. Cellobiose 2-epimerase (CE) catalyzes interconversion between d-glucose and d-mannose residues at the reducing end of beta-1,4-linked oligosaccharides. Here, we solved the structure of Ruminococcus albus CE (RaCE). The structure of RaCE showed strong similarity to those of N-acetyl-D-glucosamine 2-epimerase and aldose-ketose isomerase YihS with a high degree of conservation of residues around the catalytic center, although sequence identity between them is low. Based on structural comparison, we found that His184 is required for RaCE activity as the third histidine added to two essential histidines in other sugar epimerases/isomerases. This finding was confirmed by mutagenesis, suggesting a new catalytic mechanism for CE involving three histidines.
Crystal structure of Ruminococcus albus cellobiose 2-epimerase: structural insights into epimerization of unmodified sugar.,Fujiwara T, Saburi W, Inoue S, Mori H, Matsui H, Tanaka I, Yao M FEBS Lett. 2013 Apr 2;587(7):840-6. doi: 10.1016/j.febslet.2013.02.007. Epub 2013, Feb 24. PMID:23462136[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fujiwara T, Saburi W, Inoue S, Mori H, Matsui H, Tanaka I, Yao M. Crystal structure of Ruminococcus albus cellobiose 2-epimerase: structural insights into epimerization of unmodified sugar. FEBS Lett. 2013 Apr 2;587(7):840-6. doi: 10.1016/j.febslet.2013.02.007. Epub 2013, Feb 24. PMID:23462136 doi:10.1016/j.febslet.2013.02.007
