Does single-amino-acid replacement work in favor of or against improvement of the thermostability of immobilized enzyme?
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.
Koizumi
J
J
Department of Applied Biology, Shimane University, Japan.
Zhang
M
M
Imanaka
T
T
Aiba
S
S
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
D000596:Amino Acids; D004269:DNA, Bacterial; D004800:Enzymes, Immobilized; D009713:Nucleotidyltransferases; C024251:kanamycin nucleotidyltransferase