| 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. | |
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MedLine Citation:
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PMID: 18071253 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Akihito Harada; Hiroshi Yagi; Akira Saito; Hiroyuki Azakami; Akio Kato |
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Publication Detail:
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Type: Journal Article Date: 2007-12-07 |
Journal Detail:
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Title: Bioscience, biotechnology, and biochemistry Volume: 71 ISSN: 1347-6947 ISO Abbreviation: Biosci. Biotechnol. Biochem. Publication Date: 2007 Dec |
Date Detail:
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Created Date: 2007-12-26 Completed Date: 2008-04-07 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9205717 Medline TA: Biosci Biotechnol Biochem Country: Japan |
Other Details:
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Languages: eng Pagination: 2952-61 Citation Subset: IM |
Affiliation:
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Department of Biological Chemistry, Yamaguchi University, Yamaguchi, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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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:
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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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