EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.14.17 | expression of wild-type and mutant enzymes in erg1-knockout strain KLN1 | Saccharomyces cerevisiae |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.14.14.17 | homology model of enzyme based on p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens | Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.14.17 | D335F | mutation in FAD II binding site, nonfunctional enzyme | Saccharomyces cerevisiae |
1.14.14.17 | D335F | random mutagenesis, mutation in the FADII site, inactive mutant | Saccharomyces cerevisiae |
1.14.14.17 | D335P | mutation in FAD II binding site, nonfunctional enzyme | Saccharomyces cerevisiae |
1.14.14.17 | D335P | random mutagenesis, mutation in the FADII site, inactive mutant | Saccharomyces cerevisiae |
1.14.14.17 | D335W | mutation in FAD II binding site, nonfunctional enzyme | Saccharomyces cerevisiae |
1.14.14.17 | D335W | random mutagenesis, mutation in the FADII site, inactive mutant | Saccharomyces cerevisiae |
1.14.14.17 | G210A | mutation in nucleotide binding site, nonfunctional enzyme | Saccharomyces cerevisiae |
1.14.14.17 | G210A | random mutagenesis, mutation in the NB site, inactive mutant | Saccharomyces cerevisiae |
1.14.14.17 | G25S | mutation in FAD I binding site, nonfunctional enzyme | Saccharomyces cerevisiae |
1.14.14.17 | G25S | random mutagenesis, mutation in the FADI site, inactive mutant | Saccharomyces cerevisiae |
1.14.14.17 | G30S | decrease in enzyme activity, sevenfold increase in enzyme mRNA level. Cells exhibit altered sterol composition and increased sensitivity to allylamines and other ergosterol biosynthesis inhibitors | Saccharomyces cerevisiae |
1.14.14.17 | G30S | random mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, but a 7fold increased erg1 mRNA level and altered ergosterol composotion, the mutation renders KLN1 more sensitive not only to allylamines but also to other ergosterol biosynthesis inhibitors | Saccharomyces cerevisiae |
1.14.14.17 | L37P | decrease in enzyme activity, sevenfold increase in enzyme mRNA level. Cells exhibit altered sterol composition and increased sensitivity to allylamines and other ergosterol biosynthesis inhibitors | Saccharomyces cerevisiae |
1.14.14.17 | L37P | random mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, but a 7fold increased erg1 mRNA level and altered ergosterol composotion, the mutation renders KLN1 more sensitive not only to allylamines but also to other ergosterol biosynthesis inhibitors | Saccharomyces cerevisiae |
1.14.14.17 | additional information | isolation of erg1 allele mutants that confer increased terbinafine sensitivity or that show a lethal phenotype when they are expressed in erg1-knockout strain KLN1, overview | Saccharomyces cerevisiae |
1.14.14.17 | R269G | decrease in enzyme activity. Cells exhibit increased sensitivity to allylamines, but not to other ergosterol biosynthesis inhibitors | Saccharomyces cerevisiae |
1.14.14.17 | R269G | random mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme and a 5-10fold increase in allylamine sensitivity but no cross-sensitivity to the other ergosterol biosynthesis inhibitors | Saccharomyces cerevisiae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.17 | terbinafine | specific inhibition in a noncompetitive manner | Saccharomyces cerevisiae |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.17 | Saccharomyces cerevisiae | - |
- |
- |
1.14.14.17 | Saccharomyces cerevisiae | - |
gene ERG1 | - |
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 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.14.17 | More | enzyme structure homology modelling using the crystal structure of p-hydroxybenzoate hydroxylase, PHBH, from Pseudomonas fluorescens | Saccharomyces cerevisiae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.14.17 | Erg1 | - |
Saccharomyces cerevisiae |
1.14.14.17 | Erg1 protein | - |
Saccharomyces cerevisiae |
1.14.14.17 | Erg1p | - |
Saccharomyces cerevisiae |
1.14.14.17 | squalene epoxidase | - |
Saccharomyces cerevisiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.14.17 | 25 | - |
assay at | Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.14.17 | 7.4 | - |
assay at | Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.17 | FAD | contains two FAD domains | Saccharomyces cerevisiae |