Protein Variants | Comment | Organism |
---|---|---|
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 |
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 |
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 |
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 |
G66A | site-directed mutagenesis in the highly conserved motif 1, the mutant shows increased allylamine sensitivity compared to the wild-type enzyme | Saccharomyces cerevisiae |
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 |
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 |
R269 | site-directed mutagenesis, the mutant enzyme shows increased allylamine sensitivity | Saccharomyces cerevisiae |
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 | Comment | Organism | Structure |
---|---|---|---|
ketoconazole | the sensitive of conserved motif 1 mutant enzymes is increased compared tot he wild-type enzyme | Saccharomyces cerevisiae | |
naftifine | the sensitive of conserved motif 1 mutant enzymes is increased compared tot he wild-type enzyme | Saccharomyces cerevisiae | |
terbinafine | the sensitive of conserved motif 1 mutant enzymes is increased compared tot he wild-type enzyme | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
squalene + AH2 + O2 | Saccharomyces cerevisiae | - |
(S)-squalene-2,3-epoxide + A + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
gene ERG1 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
squalene + AH2 + O2 | - |
Saccharomyces cerevisiae | (S)-squalene-2,3-epoxide + A + H2O | - |
? | |
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 | Comment | Organism |
---|---|---|
More | enzyme structure modelling, overview | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
Erg1p | - |
Saccharomyces cerevisiae |
squalene epoxidase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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 |