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Literature summary extracted from

  • Ruckenstuhl, C.; Poschenel, A.; Possert, R.; Baral, P.K.; Gruber, K.; Turnowsky, F.
    Structure-function correlations of two highly conserved motifs in Saccharomyces cerevisiae squalene epoxidase (2008), Antimicrob. Agents Chemother., 52, 1496-1499.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.17 E60A site-directed mutagenesis in the highly conserved motif 1, the E60A variant poorly complements growth of KLN1, and shows reduced activity and about 50fold increased sensitivity to terbinafine and naftifine and 5fold to ketoconazole compared to that in the wild type, and confers temperature-sensitive growth Saccharomyces cerevisiae
1.14.14.17 E60Q site-directed mutagenesis in the highly conserved motif 1, the E60A variant poorly complements growth of KLN1, and shows highly reduced activity and about 50fold increased sensitivity to terbinafine and naftifine and 5fold to ketoconazole compared to that in the wild type, and confers temperature-sensitive growth Saccharomyces cerevisiae
1.14.14.17 G345A site-directed mutagenesis, the mutation of the highly conserved motif 2 results in increased allylamine sensitivity without cross-sensitivity to ketoconazole, decreased enzyme activity, and induced Erg1p levels compared to the wild-type enzyme Saccharomyces cerevisiae
1.14.14.17 G346A the mutant exhibits wild-type enzyme activity, steady-state protein levels, and naftifine and ketoconazole sensitivity, but is less sensitive toward terbinafine Saccharomyces cerevisiae
1.14.14.17 G66A site-directed mutagenesis in the highly conserved motif 1, the mutant shows increased allylamine sensitivity compared to the wild-type enzyme Saccharomyces cerevisiae
1.14.14.17 M348A site-directed mutagenesis in the highly conserved motif 2, the mutant is more sensitive toward terbinafine and naftifine and slightly more sensitive toward ketoconazole compared to the wild-type enzyme, while enzyme activity is reduced and protein levels are induced Saccharomyces cerevisiae
1.14.14.17 additional information amino acid substitutions in both highly conserved motifs 1 and 2 regions reduce enzyme activity and/or alter allylamine sensitivity, overview Saccharomyces cerevisiae
1.14.14.17 R269 site-directed mutagenesis, the mutant enzyme shows increased allylamine sensitivity Saccharomyces cerevisiae
1.14.14.17 R340A site-directed mutagenesis in the highly conserved motif 2, the mutant enzyme shows highly reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.17 ketoconazole the sensitive of conserved motif 1 mutant enzymes is increased compared tot he wild-type enzyme Saccharomyces cerevisiae
1.14.14.17 naftifine the sensitive of conserved motif 1 mutant enzymes is increased compared tot he wild-type enzyme Saccharomyces cerevisiae
1.14.14.17 terbinafine the sensitive of conserved motif 1 mutant enzymes is increased compared tot he wild-type enzyme Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.17 squalene + AH2 + O2 Saccharomyces cerevisiae
-
 (S)-squalene-2,3-epoxide + A + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.17 Saccharomyces cerevisiae
-
 gene ERG1
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.17 squalene + AH2 + O2
-
 Saccharomyces cerevisiae (S)-squalene-2,3-epoxide + A + H2O
-
 ?
1.14.14.17 squalene + AH2 + O2 the enzyme contains two highly conserved motifs 1 and 2, which flank the FAD cofactor and form part of the interface between cofactor and substrate binding domains in the structure modelling, substrate binding domain structure, overview Saccharomyces cerevisiae (S)-squalene-2,3-epoxide + A + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.14.17 More enzyme structure modelling, overview Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.14.14.17 Erg1p
-
 Saccharomyces cerevisiae
1.14.14.17 squalene epoxidase
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.17 FAD binding domain structure, the enzyme contains two highly conserved motifs 1 and 2, which flank the FAD cofactor and form part of the interface between cofactor and substrate binding domains in the structure modelling, overview Saccharomyces cerevisiae