title: Does single-amino-acid replacement work in favor of or against improvement of the thermostability of immobilized enzyme?
abstract: Thermostabilities of kanamycin nucleotidyltransferase and of its mutants that became thermostable, in the free state, because of single-amino-acid replacements were studied after immobilization of the enzymes on cyanogen bromide-activated Sephadex G-200 particles. Lys in place of Gln at position 102 decreased the thermostability of the immobilized enzyme, whereas replacement with other amino acids enhanced it.
authors.affiliation: Department of Applied Biology, Shimane University, Japan.
authors.forename: J
authors.initials: J
authors.lastname: Koizumi
authors.forename: M
authors.initials: M
authors.lastname: Zhang
authors.forename: T
authors.initials: T
authors.lastname: Imanaka
authors.forename: S
authors.initials: S
authors.lastname: Aiba
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D001483:Base Sequence; D004269:DNA, Bacterial / Q000235:genetics; D004355:Drug Stability; D004800:Enzymes, Immobilized / Q000037:antagonists & inhibitors / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D001411:Geobacillus stearothermophilus / Q000201:enzymology / Q000235:genetics; D006358:Hot Temperature; D008969:Molecular Sequence Data; D009713:Nucleotidyltransferases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics; D015202:Protein Engineering
chemical_list: D000596:Amino Acids; D004269:DNA, Bacterial; D004800:Enzymes, Immobilized; D009713:Nucleotidyltransferases; C024251:kanamycin nucleotidyltransferase