Medizinische Universität Graz - Research portal
Selected Publication:
SHR Neuro Cancer Cardio Lipid Metab Microb
Ruckenstuhl, C; Poschenel, A; Possert, R; Baral, PK; Gruber, K; Turnowsky, F.
Structure-function correlations of two highly conserved motifs in Saccharomyces cerevisiae squalene epoxidase.
Antimicrob Agents Chemother. 2008; 52(4):1496-1499
Doi: 10.1128/AAC.01282-07
[OPEN ACCESS]
Web of Science
PubMed
FullText
FullText_MUG
- Leading authors Med Uni Graz
- Ruckenstuhl Rudolf
- Altmetrics:
- Dimensions Citations:
- Plum Analytics:
- Scite (citation analytics):
- Abstract:
- Saccharomyces cerevisiae squalene epoxidase contains two highly conserved motifs, 1 and 2, of unknown function. Amino acid substitutions in both regions reduce enzyme activity and/or alter allylamine sensitivity. In the homology model, these motifs flank the flavin adenine dinucleotide cofactor and form part of the interface between cofactor and substrate binding domains.
- Find related publications in this database (using NLM MeSH Indexing)
- Allylamine - pharmacology
- Amino Acid Motifs -
- Amino Acid Sequence -
- Conserved Sequence -
- Models, Molecular -
- Saccharomyces cerevisiae - drug effects Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics
- Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism
- Squalene Monooxygenase - chemistry Squalene Monooxygenase - genetics Squalene Monooxygenase - metabolism
- Structure-Activity Relationship -