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

• Yazawa, Tomoyo

• Naganuma, Tatsuro

• Yamagata, Maki

• Kihara, Akio

抄録

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.

収録刊行物

• FEBS LETTERS

  FEBS LETTERS 587 (6), 804-809, 2013-03-18

  ELSEVIER

キーワード

• Very long-chain fatty acid
• 3-Hydroxyacyl-CoA dehydratase
• Fatty acid
• Lipid
• Phs1
• Membrane

詳細情報

• CRID: 1050282813990111488
• NII論文ID: 120005228604
• HANDLE: 2115/52639
• ISSN: 00145793
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles