title: Site-directed mutagenesis of methionine residues for improving the oxidative stability of α-amylase from Thermotoga maritima.
abstract: The oxidative stability of α-amylase (AmyC) from Thermotoga maritima was improved by mutating the methionine residues at positions 43 and 44, 55, and 62 to oxidative-resistant alanine residues. The most resistant M55A variant showed 50% residual activity in the presence of 100 mM H₂O₂, whereas the wild-type enzyme was inactive.
authors.affiliation: Department of Biochemistry, Faculty of Science, Ege University, Izmir 35100, Turkey.
authors.forename: Handan
authors.initials: H
authors.lastname: Ozturk
authors.forename: Selin
authors.initials: S
authors.lastname: Ece
authors.forename: Ersin
authors.initials: E
authors.lastname: Gundeger
authors.forename: Serap
authors.initials: S
authors.lastname: Evran
mesh_terms: D000409:Alanine / Q000235:genetics / Q000378:metabolism; D004795:Enzyme Stability / Q000187:drug effects; D006861:Hydrogen Peroxide / Q000494:pharmacology; D008715:Methionine / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010084:Oxidation-Reduction / Q000187:drug effects; D020124:Thermotoga maritima / Q000201:enzymology* / Q000235:genetics; D000516:alpha-Amylases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism
chemical_list: D008715:Methionine; D006861:Hydrogen Peroxide; D000516:alpha-Amylases; D000409:Alanine
keywords: Oxidative stability; Protein engineering; Site-directed mutagenesis of methionine; Thermotoga maritima; α-Amylase