title: Catalytic activity of tripeptidase from Lactococcus lactis to which amino acid substitution was introduced according to natural mutation.
abstract: Four mutations observed between tripeptidases from Lactococcus lactis subsp. lactis and subsp. cremoris were introduced one by one to the corresponding points in wild-type tripeptidase from L. lactis subsp. lactis. The k(cat) values of four resultant mutants were analyzed and discussed in stereographical terms. Change in catalytic activity appeared to be related to the sequential and steric location of mutation point within the enzyme protein, even though no drastic change was observed with one point mutation.
authors.affiliation: National Food Research Institute, Ibaraki, Japan.
authors.forename: Sumiko
authors.initials: S
authors.lastname: Mori
authors.forename: Satoshi
authors.initials: S
authors.lastname: Kaneko
authors.forename: Takafumi
authors.initials: T
authors.lastname: Kasumi
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution / Q000235:genetics*; D000626:Aminopeptidases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D020134:Catalytic Domain / Q000235:genetics; D013294:Lactococcus lactis / Q000201:enzymology*; D008969:Molecular Sequence Data; D017354:Point Mutation / Q000235:genetics*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013379:Substrate Specificity
chemical_list: D000626:Aminopeptidases; C023191:PepT tripeptidase