NDLI: Design and creation of a Ca2+ binding site in human lysozyme to enhance structural stability.

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Design and creation of a Ca2+ binding site in human lysozyme to enhance structural stability.

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Design and creation of a Ca2+ binding site in human lysozyme to enhance structural stability.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kikuchi, M. Kuroki, R. Seko, C. Ikehara, M. Taniyama, Y. Nakamura, H.
Description	Author Affiliation: Kuroki R ( Protein Engineering Research Institute, Osaka, Japan.);
Abstract	A Ca2+ binding site like an EF-hand motif was designed and created in human lysozyme by replacing both Gln-86 and Ala-92 with aspartic acids by site-directed mutagenesis. The mutant human lysozyme (D86/92-lysozyme) was expressed and secreted by yeast. One Ca2+ was found to bind one molecule of the purified protein with the binding constant 5.0 x 10(6) M-1. The enzymatic activity of holo-D86/92-lysozyme against glycol chitin at 40 degrees C was 2-fold higher than that of the native lysozyme. Maximal activity of the holo-D86/92-lysozyme was observed at 80 degrees C, where its relative activity normalized to the value at 40 degrees C was 6-fold and 17-fold higher than those of the native and apoenzymes, respectively. The activities of the native lysozyme and apo-D86/92-lysozyme were maximum at 65 degrees C-70 degrees C. Moreover, D86/92-lysozyme was more stable against protease digestion than the native lysozyme. These results indicate that the creation of the calcium binding site like an EF-hand motif in the human lysozyme enhances its structural stability.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	18
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium Metabolism Muramidase Amino Acid Sequence Binding Sites DNA Genetics Enzyme Stability Kinetics Molecular Sequence Data Mutation Plasmids Protein Conformation Protein Denaturation Saccharomyces Cerevisiae Sequence Homology, Nucleic Acid Thermodynamics Comparative Study Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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