Document Detail

Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule.
MedLine Citation:
PMID:  8001545     Owner:  NLM     Status:  MEDLINE    
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].
K Watanabe; T Masuda; H Ohashi; H Mihara; Y Suzuki
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  226     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1994 Dec 
Date Detail:
Created Date:  1995-01-26     Completed Date:  1995-01-26     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  277-83     Citation Subset:  IM    
Department of Agricultural Chemistry, Kyoto Prefectural University, Japan.
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MeSH Terms
Amino Acid Sequence
Bacillus cereus / enzymology*
Enzyme Stability
Hot Temperature*
Molecular Sequence Data
Mutagenesis, Site-Directed
Oligo-1,6-Glucosidase / chemistry*,  genetics
Proline / chemistry*
Protein Structure, Secondary
Structure-Activity Relationship
Reg. No./Substance:
147-85-3/Proline; EC,6-Glucosidase

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