Literature summary for 1.14.14.17 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.

Search for more literature for 1.14.14.17

Protein Variants

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

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/ 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	-	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	-	?
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

Subunits	Comment	Organism
More	enzyme structure modelling, overview	Saccharomyces cerevisiae

Synonyms

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

Cofactor

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

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Release 2023.1 (January 2023)