| Literature DB >> 23519800 |
Jigang Yu1, Chengliang Wang, Yanjin Hu, Yuanqiu Dong, Ying Wang, Xiaoming Tu, Hui Peng, Xuecheng Zhang.
Abstract
AmyP is a raw-starch-degrading α-amylase newly identified from a marine metagenome library. It shares low sequence similarity with characterized glycoside hydrolases and was classified into a new subfamily of GH13. In particular, it showed preferential degradation to raw rice starch. Full-length AmyP was cloned and overexpressed in Escherichia coli, then purified and crystallized in the presence of its substrate analogue β-cyclodextrin. X-ray diffraction data were collected to a resolution of 2.1 Å. The crystal belonged to space group P2₁2₁2, with unit-cell parameters a=129.824, b=215.534, c=79.699 Å, α=β=γ=90°, and was estimated to contain two molecules in one asymmetric unit.Entities:
Keywords: AmyP; α-amylase
Mesh:
Substances:
Year: 2013 PMID: 23519800 PMCID: PMC3606570 DOI: 10.1107/S1744309113001693
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091