| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10536816 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2012 | 7 Pages |
Abstract
⺠We substituted Gly or Ala for Pro-Thr-Asn at β8-β9 turn of subtilisin Carlsberg (sC). ⺠This turn is located apart from the active site. ⺠These mutations increased kcat for peptide hydrolysis and decreased thermostability. ⺠P210G mutation had the largest effects among single Gly substitutions for PTN residues. ⺠Positive correlations were found between kcat and thermal inactivation rates.
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Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Naoki Fuchita, Saori Arita, Junya Ikuta, Masahiro Miura, Kaori Shimomura, Hiroyuki Motoshima, Keiichi Watanabe,