Catalytic activity of tripeptidase from Lactococcus lactis to which amino acid substitution was introduced according to natural mutation.
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.
Mori
Sumiko
S
National Food Research Institute, Ibaraki, Japan.
Kaneko
Satoshi
S
Kasumi
Takafumi
T
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
D000626:Aminopeptidases; C023191:PepT tripeptidase