Insight into the structure, dynamics and the unfolding property of amylosucrases: implications of rational engineering on thermostability

• Published in: PloS one Vol. 7; no. 7; p. e40441
• Main Authors: Liu, Ming, Wang, Shuang, Sun, Tingguang, Su, Jiguo, Zhang, Yuanxing, Yue, Junjie, Sun, Zhiwei
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 06.07.2012; Public Library of Science (PLoS)
• Subjects: Addition polymerization; Algorithms; Amino Acid Sequence; Amino Acid Substitution; Amylose; Amylosucrase; Analysis; Biology; Biotechnology; Catalytic Domain; Chemical synthesis; Conserved Sequence; Deinococcus - enzymology; Engineering; Enzyme Stability; Enzymes; Glucosyltransferases - chemistry; Glycoside hydrolase; Growth hormone; Hydrogen Bonding; Hydrolase; Industrial applications; Laboratories; Methods; Molecular Dynamics Simulation; Molecular Sequence Data; Mutants; Mutation; Neisseria; Neisseria - enzymology; Neisseria polysaccharea; Physics; Polymers; Polysaccharides; Properties (attributes); Protein Engineering; Protein Structure, Secondary; Protein Unfolding; Proteins; Sucrose; Sugar; Thermal stability; Thermodynamics; Topology; Beijing China; China

Amylosucrase (AS) is a kind of glucosyltransferases (E.C. 2.4.1.4) belonging to the Glycoside Hydrolase (GH) Family 13. In the presence of an activator polymer, in vitro, AS is able to catalyze the synthesis of an amylose-like polysaccharide composed of only α-1,4-linkages using sucrose as the only...