Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in erg1-knockout strain KLN1 | Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
---|---|
homology model of enzyme based on p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
D335F | mutation in FAD II binding site, nonfunctional enzyme | Saccharomyces cerevisiae |
D335F | random mutagenesis, mutation in the FADII site, inactive mutant | Saccharomyces cerevisiae |
D335P | mutation in FAD II binding site, nonfunctional enzyme | Saccharomyces cerevisiae |
D335P | random mutagenesis, mutation in the FADII site, inactive mutant | Saccharomyces cerevisiae |
D335W | mutation in FAD II binding site, nonfunctional enzyme | Saccharomyces cerevisiae |
D335W | random mutagenesis, mutation in the FADII site, inactive mutant | Saccharomyces cerevisiae |
G210A | mutation in nucleotide binding site, nonfunctional enzyme | Saccharomyces cerevisiae |
G210A | random mutagenesis, mutation in the NB site, inactive mutant | Saccharomyces cerevisiae |
G25S | mutation in FAD I binding site, nonfunctional enzyme | Saccharomyces cerevisiae |
G25S | random mutagenesis, mutation in the FADI site, inactive mutant | Saccharomyces cerevisiae |
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 |
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 |
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 |
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 |
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 |
R269G | decrease in enzyme activity. Cells exhibit increased sensitivity to allylamines, but not to other ergosterol biosynthesis inhibitors | Saccharomyces cerevisiae |
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 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
terbinafine | specific inhibition in a noncompetitive manner | 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 | - |
- |
- |
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 | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | enzyme structure homology modelling using the crystal structure of p-hydroxybenzoate hydroxylase, PHBH, from Pseudomonas fluorescens | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
Erg1 | - |
Saccharomyces cerevisiae |
Erg1 protein | - |
Saccharomyces cerevisiae |
Erg1p | - |
Saccharomyces cerevisiae |
squalene epoxidase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | contains two FAD domains | Saccharomyces cerevisiae |