Plant cyclopropylsterol-cycloisomerase: Key amino acids affecting activity and substrate specificity

Biochemical Journal

Volumn 459, Issue 2, 2014, Pages 289-299

  Rahier, Alain ^a   Karst, Francis ^b  

^a CNRS   (France)

^b UNIVERSITÉ DE STRASBOURG   (France)

Author keywords

Arabidopsis thaliana; Cycloartenol isomerization; Cycloeucalenol isomerase; Cyclopropylsterol cycloisomerase; Ergosterol biosynthesis 7 (erg7) yeast mutant; Mutagenesis; Plant sterol pathway

Indexed keywords

24 DIHYDROCYCLOARTENOL; 24 METHYLENE 24 DIHYDROCYCLOARTENOL; 24 METHYLENEDIHYDROLANOSTEROL; 4ALPHA METHYL CYCLOPROPYLSTEROL CYCLOEUCALENOL; 4BETA METHYL 24 DIHYDROCYCLOEUCALENOL; 4BETA METHYL 24 DIHYDROOBTUSIFOLIOL; 9BETA 19 CYCLOPROPANE; AMINO ACID; ASPARAGINE; CYCLOARTENOL; CYCLOEUCALENOL; CYCLOPROPANE DERIVATIVE; CYCLOPROPYLSTEROL CYCLOISOMERASE ENZYME; DELTA 8 STEROL OBTUSIFOLIOL; ERGOSTEROL; ESSENTIAL AMINO ACID; GLUTAMIC ACID; GLYCINE; ISOMERASE; LANOSTEROL; LANOSTEROL SYNTHASE; PHYTOSTEROL; STEROL 14ALPHA DEMETHYLASE; STEROL DERIVATIVE; TRITERPENE DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARABIDOPSIS; ARABIDOPSIS THALIANA; ARTICLE; AUXOTROPHY; CATALYSIS; CHEMICAL MUTAGENESIS; CHEMICAL STRUCTURE; CONTROLLED STUDY; DNA LIBRARY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; FUNGAL CELL CULTURE; IN VITRO STUDY; IN VIVO STUDY; ISOMERIZATION; LIMIT OF DETECTION; LIMIT OF QUANTITATION; MICHAELIS MENTEN KINETICS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PLASMID; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTON TRANSPORT; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; STEROL ANALYSIS; YEAST CELL;

AMINO ACID SEQUENCE; ARABIDOPSIS PROTEINS; CALCIUM-BINDING PROTEINS; DNA, COMPLEMENTARY; EPITOPES; GENE EXPRESSION REGULATION, PLANT; INTRAMOLECULAR LYASES; ISOMERASES; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; MUTATION; STEROIDS; SUBSTRATE SPECIFICITY; YEASTS;

EID: 84897538071     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20131239     Document Type: Article

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