| Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule. | |
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MedLine Citation:
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PMID: 8001545 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Nine residues of Bacillus cereus ATCC7064 oligo-1,6-glucosidase were replaced stepwise with proline residues. Of the nine residues, Lys121, Glu208 and Glu290 were at second sites of beta turns; Asn109, Glu175 and Thr261 were at N-caps of alpha helices; Glu216, Glu270 and Glu378 were in coils within loops. The replacements were carried out in the order, Lys121-->Pro, Glu175-->Pro, Glu290-->Pro, Glu208-->Pro, Glu270-->Pro, Glu378-->Pro, Thr261-->Pro, Glu216-->Pro and Asn109-->Pro. The resultant nine active mutant enzymes contained 1-9 more proline residues than B. cereus oligo-1,6-glucosidase. The thermostability of these mutants was additively enhanced with the increase in the number of proline residues introduced. The increase in the thermostability was most remarkable when proline residues were introduced at second sites of beta turns or at N-caps of alpha helices. The above results afforded irrefragable proof for the proline rule as an effective principle for increasing protein thermostability [Suzuki, Y., Oishi, K., Nakano, H. & Nagayama, T. (1987) Appl. Microbiol. Biotechnol. 26, 546-551]. |
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Authors:
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K Watanabe; T Masuda; H Ohashi; H Mihara; Y Suzuki |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: European journal of biochemistry / FEBS Volume: 226 ISSN: 0014-2956 ISO Abbreviation: Eur. J. Biochem. Publication Date: 1994 Dec |
Date Detail:
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Created Date: 1995-01-26 Completed Date: 1995-01-26 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0107600 Medline TA: Eur J Biochem Country: GERMANY |
Other Details:
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Languages: eng Pagination: 277-83 Citation Subset: IM |
Affiliation:
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Department of Agricultural Chemistry, Kyoto Prefectural University, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Bacillus cereus / enzymology* Enzyme Stability Hot Temperature* Kinetics Molecular Sequence Data Mutagenesis, Site-Directed Oligo-1,6-Glucosidase / chemistry*, genetics Proline / chemistry* Protein Structure, Secondary Structure-Activity Relationship |
| Chemical | |
Reg. No./Substance:
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147-85-3/Proline; EC 3.2.1.10/Oligo-1,6-Glucosidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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