Document Detail


Relationship between the stability of hen egg-white lysozymes mutated at sites designed to interact with alpha-helix dipoles and their secretion amounts in yeast.
MedLine Citation:
PMID:  18071253     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The positively charged lysine at the C-terminals of three long alpha-helices (5-15, 25-35, and 88-99) was replaced with alanine (K13A, K33A, K97A) or aspartic acid (K13D, K33D, K97D) in hen lysozyme by genetic engineering. The denaturation transition point (Tm) and Gibbs energy change Delta G of the mutant lysozymes decreased remarkably, suggesting that the positive charge at the C-terminals of helices is involved in the stabilization of the helix dipole. On the other hand, the non-charged asparagine at the N-terminal of the long alpha-helices (25-35 and 88-99) was replaced with negatively charged aspartic acid (N27D and N93D). The Tm and Delta G of N27D increased, suggesting that the dipole moment of the N-terminal of the helices is diminished by replacement with negatively charged amino acid strengthening the stability of the helices. The stabilities of those hen egg white lysozymes mutated at the N- or C-terminal sites of the three long alpha-helices were related with their secretion amounts in yeast (Pichia pastoris). The secretion amounts of these mutant lysozymes in yeast were closely correlated with their stability.
Authors:
Akihito Harada; Hiroshi Yagi; Akira Saito; Hiroyuki Azakami; Akio Kato
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Publication Detail:
Type:  Journal Article     Date:  2007-12-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  71     ISSN:  1347-6947     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2007 Dec 
Date Detail:
Created Date:  2007-12-26     Completed Date:  2008-04-07     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  2952-61     Citation Subset:  IM    
Affiliation:
Department of Biological Chemistry, Yamaguchi University, Yamaguchi, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Binding Sites
Cloning, Molecular
Enzyme Stability
Models, Molecular
Molecular Sequence Data
Muramidase / chemistry*,  genetics,  secretion
Mutation
Pichia / metabolism*
Protein Binding
Protein Structure, Secondary
Structure-Activity Relationship
Thermodynamics
Chemical
Reg. No./Substance:
EC 3.2.1.-/hen egg lysozyme; EC 3.2.1.17/Muramidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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