Two pockets in the active site of maize sesquiterpene synthase TPS4 carry out sequential parts of the reaction scheme resulting in multiple products

Archives of Biochemistry and Biophysics

Volumn 448, Issue 1-2, 2006, Pages 83-92

  Köllner, Tobias G ^a   O'Maille, Paul E ^b   Gatto, Nathalie ^a   Boland, Wilhelm ^a   Gershenzon, Jonathan ^a   Degenhardt, Jörg ^a  

^a MAX PLANCK INSTITUTE FOR CHEMICAL ECOLOGY   (Germany)

^b SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

Author keywords

Multiproduct enzyme; Sesquiterpene biosynthesis; Terpene synthase; Terpene synthase reaction mechanism

Indexed keywords

AMINO ACID; BICYCLO COMPOUND; CATION; FARNESYL DIPHOSPHATE; SESQUITERPENE DERIVATIVE; SYNTHETASE;

ARTICLE; CATALYSIS; COMPLEX FORMATION; CYCLIZATION; ENZYME ACTIVE SITE; MAIZE; MEASUREMENT; MUTATION; NONHUMAN; PRIORITY JOURNAL; REACTION ANALYSIS; SEQUENTIAL ANALYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BINDING SITES; CARBON-CARBON LYASES; COMPUTER SIMULATION; ENZYME ACTIVATION; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; RECOMBINANT PROTEINS; SESQUITERPENES; ZEA MAYS;

ZEA MAYS;

EID: 33646138480     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2005.10.011     Document Type: Article

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