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Literature summary for 1.14.14.17 extracted from

  • Ruckenstuhl, C.; Lang, S.; Poschenel, A.; Eidenberger, A.; Baral, P.K.; Kohut, P.; Hapala, I.; Gruber, K.; Turnowsky, F.
    Characterization of squalene epoxidase of Saccharomyces cerevisiae by applying terbinafine-sensitive variants (2007), Antimicrob. Agents Chemother., 51, 275-284.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in erg1-knockout strain KLN1 Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
homology model of enzyme based on p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens Saccharomyces cerevisiae

Protein Variants

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

Inhibitors Comment Organism Structure
terbinafine specific inhibition in a noncompetitive manner Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae
-
gene ERG1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
squalene + AH2 + O2
-
Saccharomyces cerevisiae (S)-squalene-2,3-epoxide + A + H2O
-
?

Subunits

Subunits Comment Organism
More enzyme structure homology modelling using the crystal structure of p-hydroxybenzoate hydroxylase, PHBH, from Pseudomonas fluorescens Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Erg1
-
Saccharomyces cerevisiae
Erg1 protein
-
Saccharomyces cerevisiae
Erg1p
-
Saccharomyces cerevisiae
squalene epoxidase
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
FAD contains two FAD domains Saccharomyces cerevisiae