X-ray structure of 12-Oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE

Structure

Volumn 9, Issue 5, 2001, Pages 419-429

  Breithaupt, Constanze ^a   Strassner, Jochen ^b   Breitinger, Ulrike ^a   Huber, Robert ^a   Macheroux, Peter ^a   Schaller, Andreas ^b   Clausen, T ^b  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b ETH ZURICH   (Switzerland)

Author keywords

Flavoenzyme; Jasmonic acid; Octadecanoids; OPR; OYE; Plant defense

Indexed keywords

12 OXOPHYTODIENOATE; 12 OXOPHYTODIENOATE REDUCTASE 1; ALKENE DERIVATIVE; CARBONYL DERIVATIVE; CYCLOPENTENONE; FATTY ACID DERIVATIVE; FLAVINE MONONUCLEOTIDE; HISTIDINE DERIVATIVE; MACROGOL 400; MONOMER; OXIDOREDUCTASE; OXYLIPIN; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE; TYROSINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; PLANT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTON TRANSPORT; STEREOCHEMISTRY; STRUCTURE ANALYSIS;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; FATTY ACIDS, UNSATURATED; FLAVIN MONONUCLEOTIDE; LYCOPERSICON ESCULENTUM; MODELS, MOLECULAR; NADPH DEHYDROGENASE; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PROTEIN STRUCTURE, SECONDARY; SUBSTRATE SPECIFICITY;

LYCOPERSICON ESCULENTUM;

EID: 0034980393     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00602-5     Document Type: Article

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