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

Tomoyo Yazawa, Tatsuro Naganuma, Maki Yamagata, Akio Kihara

Research output: Contribution to journalArticle

3 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)804-809
Number of pages6
JournalFEBS Letters
Volume587
Issue number6
DOIs
Publication statusPublished - 2013 Mar 18
Externally publishedYes

Fingerprint

Enoyl-CoA Hydratase
Hydro-Lyases
Coenzyme A
Substrate Specificity
Catalysis
Yeast
Elongation
Fatty Acids
Yeasts
Maintenance
Digitonin
Enzyme kinetics
Structural integrity
Substrates
Substitution reactions
Membranes
Amino Acids
Mutation
Enzymes

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

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.

In: FEBS Letters, Vol. 587, No. 6, 18.03.2013, p. 804-809.

Research output: Contribution to journalArticle

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