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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/38416

Title: Site-directed mutagenesis of Asp313, Glu315, and Asp391 residues in chitinase of Aeromonas caviae.
Authors: Fu-Pang Lin
Hsing-Chen Chen
Chung-Saint Lin
Contributors: 國立臺灣海洋大學:生命科學暨生物科技學系
Date: 1999
Issue Date: 2016-09-01T01:32:38Z
Publisher: IUBMB Life
Abstract: Abstract: Site-directed mutagenesis was used to explore the roles of amino acid residues involved in the activity of chitinase from Aeromonas caviae. Kinetic parameters for 4-methylumbelliferyl-N,N'-diacetyl-chitobiose or 4-methylumbelliferyl-N,N',N"-triacetylchitotriose hydrolysis were determined with wild-type and mutant chitinases. Chitinases with the mutations E315D (or Q) and D391E (or N) were severely impaired and had dramatically decreased kcat. However, the effect of the these mutations on the Km values were different. The function of the carboxyl group of Asp313 was partially replaced by the amide of Asn when the 4-methylumbelliferyl-N,N',N"-triacetylchitotriose substrate was used. Results indicated that Asp313, Glu315, and Asp391 might be the best candidates for the catalytic residues of chitinase A from Aeromonas caviae.
Relation: 48(2)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/38416
Appears in Collections:[生命科學系] 期刊論文

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