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Identification of residues important for the catalysis, structure maintenance, and substrate specificity of yeast 3-hydroxyacyl-CoA dehydratase Phs1

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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)

Submitter: 木原 章雄

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