| Autor: |
MORI, Sumiko, KANEKO, Satoshi, KASUMI, Takafumi |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; January 2004, Vol. 68 Issue: 5 p1149-1152, 4p |
| Abstrakt: |
Four mutations observed between tripeptidases from Lactococcus lactissubsp. lactisand subsp. cremoriswere introduced one by one to the corresponding points in wild-type tripeptidase from L. lactissubsp. lactis. The kcatvalues 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. |
| Databáze: |
Supplemental Index |
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