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Identification of residues important for the catalysis, structure maintenance, and substrate specificity of yeast 3-hydroxyacyl-CoA dehydratase Phs1
Title: | Identification of residues important for the catalysis, structure maintenance, and substrate specificity of yeast 3-hydroxyacyl-CoA dehydratase Phs1 |
Authors: | Yazawa, Tomoyo Browse this author | Naganuma, Tatsuro Browse this author | Yamagata, Maki Browse this author | Kihara, Akio Browse this author →KAKEN DB |
Keywords: | Very long-chain fatty acid | 3-Hydroxyacyl-CoA dehydratase | Fatty acid | Lipid | Phs1 | Membrane |
Issue Date: | 18-Mar-2013 |
Publisher: | ELSEVIER |
Journal Title: | FEBS LETTERS |
Volume: | 587 |
Issue: | 6 |
Start Page: | 804 |
End Page: | 809 |
Publisher DOI: | 10.1016/j.febslet.2013.02.006 |
PMID: | 23416297 |
Abstract: | Yeast Phs1 is a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation. In the present study, we biochemically characterized Phs1 mutants with Ala-substitution at each of seven highly conserved amino-acid residues. All mutants exhibited reduced Phs1 activity. The E60A, Q79A, and R141A mutants were sensitive to digitonin, indicative of their reduced structural integrity. The fatty acid elongation cycle was greatly inhibited in the R83A, R141A, and G152A mutant membranes. The enzyme kinetics study implicated the direct involvement of the Arg83 and Gly152 residues in the catalytic process. The E60A mutation was found to affect the substrate specificity. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved. |
Relation: | http://www.sciencedirect.com/science/article/pii/S0014579313001245 |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/52639 |
Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 木原 章雄
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