3ren

Publication Abstract from PubMed

CPF_2247 from Clostridium perfringens ATCC 13124 was identified as a putative carbohydrate-active enzyme by its low sequence identity to endo-beta-1,4-glucanases belonging to family 8 of the glycoside hydrolase classification. The X-ray crystal structure of CPF_2247 determined to 2.0 A resolution by single-wavelength anomalous dispersion using seleno-methionine-substituted protein revealed an (alpha/alpha)(6) barrel fold. A large cleft on the surface of the protein contains residues that are structurally conserved with key elements of the catalytic machinery in clan GH-M glycoside hydrolases. Assessment of CPF_2247 as a carbohydrate-active enzyme disclosed alpha-glucanase activity on amylose, glycogen, and malto-oligosaccharides.

Structural analysis of CPF_2247, a novel alpha-amylase from Clostridium perfringens.,Ficko-Blean E, Stuart CP, Boraston AB Proteins. 2011 Oct;79(10):2771-7. doi: 10.1002/prot.23116. Epub 2011 Aug 26. PMID:21905105^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.