Single amino acid exchanges in FAD-binding domains of squalene epoxidase of Saccharomyces cerevisiae lead to either loss of functionality or terbinafine sensitivity

Biochemical Society Transactions

Volumn 33, Issue 5, 2005, Pages 1197-1201

  Ruckenstuhl, C ^a   Eidenberger, A ^a   Lang, S ^a   Turnowsky, F ^a  

^a UNIVERSITY OF GRAZ   (Austria)

Author keywords

Allylamine; Ergosterol synthesis; FAD binding site; Squalene epoxidase; Terbinafine sensitivity; Yeast

Indexed keywords

AMINO ACID; ERGOSTEROL; FLAVINE ADENINE NUCLEOTIDE; SQUALENE MONOOXYGENASE; TERBINAFINE;

ALLELE; AMINO ACID ANALYSIS; BIOSYNTHESIS; CONFERENCE PAPER; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME SYNTHESIS; MUTAGENESIS; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; WILD TYPE; YEAST CELL;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CONSERVED SEQUENCE; FLAVIN-ADENINE DINUCLEOTIDE; HUMANS; MOLECULAR SEQUENCE DATA; NAD; NADP; PHYLOGENY; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SQUALENE MONOOXYGENASE;

SACCHAROMYCES CEREVISIAE;

EID: 27844536533     PISSN: 03005127     EISSN: None     Source Type: Journal    
DOI: 10.1042/BST20051197     Document Type: Conference Paper

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