Structure-function correlations of two highly conserved motifs in Saccharomyces cerevisiae squalene epoxidase

Antimicrobial Agents and Chemotherapy

Volumn 52, Issue 4, 2008, Pages 1496-1499

  Ruckenstuhl, Christoph ^a   Poschenel, Andrea ^a   Possert, Reinhard ^a   Baral, Pravas Kumar ^a   Gruber, Karl ^a   Turnowsky, Friederike ^a  

^a UNIVERSITY OF GRAZ   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

ALLYLAMINE; ASPARAGINYLMETHIONYLARGINYLHISTIDYLPROLYLLEUCYLTHREONYLGLYCYL GLYCYLGLYCYLMETHIONYLTHREONYLVALINE; ASPARTYLARGINYLISOLEUCYLVALYLGLYCYLGLUTAMYLLEUCYLMETHIONYL GLUTAMINYLPROLYLGLYCYLGLYCINE; FLAVINE ADENINE NUCLEOTIDE; PEPTIDE FRAGMENT; SQUALENE MONOOXYGENASE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; GENETIC CONSERVATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN MOTIF; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

ALLYLAMINE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; CONSERVED SEQUENCE; MODELS, MOLECULAR; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SQUALENE MONOOXYGENASE; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 42049093979     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.01282-07     Document Type: Article

References (13)

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