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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Shimomura, Kaori Fuchita, Naoki Miura, Masahiro Watanabe, Keiichi Arita, Saori Ikuta, Junya Motoshima, Hiroyuki |
| Description | Author Affiliation: Fuchita N ( Department of Applied Biochemistry and Food Science, Saga University, Saga, Japan.) |
| Abstract | A comparison of the primary structures among psychrophilic, mesophilic, and thermophilic subtilases revealed that the turn between the β8 and β9 strands (β8–β9 turn, BPN′ numbering) of psychrophilic subtilases are more flexible than those of their mesophilic and thermophilic counterparts. To investigate the relationship between structure of this turn and enzyme activity as well as thermostability of mesophilic subtilisin Carlsberg (sC), we analyzed 6 mutants of sC with a single, double, or triple Gly or Ala substitutions for Pro $^{210}$ Thr $^{211}$ Asn $^{212}$ at the β8–β9 turn. Among the single Gly substitutions, the P210G substitution most significantly (1.5-fold) increased the specific activity on N -succinyl-Ala-Ala-Pro-Phe- p -nitroanilide (AAPF) substrate and 12-fold decreased the thermostability. All mutants tested showed the increased $k_{cat}$ for the AAPF substrate and reduced thermostability compared with the wild-type sC. The $k_{cat}$ values of the P210G, P210G/T211G, and P210G/T211G/N212G mutants were 1.5-, 1.7-, and 1.8-fold higher than that of the wild-type sC. There were significant positive correlations between $k_{cat}$ and thermal inactivation rates as well as $k_{cat}$ and $K_{m}$ of the wild-type and mutants. These results demonstrate that the structure of β8–β9 turn, despite its distance from the active site, has significant effects on the catalytic rate and thermostability of sC through a global network of intramolecular interactions and suggest that the lack of flexibility of this turn stabilizes the wild-type sC against thermal inactivation in compensation for some loss of catalytic activity. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 4 |
| Volume Number | 1824 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2012-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Alanine Genetics Bacillus Enzymology Bacterial Proteins Chemistry Glycine Subtilisins Amino Acid Motifs Amino Acid Sequence Amino Acid Substitution Asparagine Biocatalysis Catalytic Domain Enzyme Stability Kinetics Molecular Sequence Data Mutagenesis, Site-Directed Peptides Proline Proteolysis Sequence Homology, Amino Acid Threonine Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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