Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme

Biochemistry

Volumn 48, Issue 23, 2009, Pages 5239-5245

  Luo, Qianyi ^a   Olucha, Jose ^a   Lamb, Audrey L ^a  

^a UNIVERSITY OF KANSAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE ARCHITECTURE; BIFUNCTIONAL ENZYMES; CATALYTIC MECHANISMS; CHEMICAL NATURE; CHORISMATE; CHORISMATE MUTASE; CIRCULAR DICHROISM; CONFORMATIONAL PLASTICITY; LOOP CONFORMATION; LOOP DYNAMICS; MOLECULAR BASIS; MUTATIONAL EFFECTS; PERICYCLIC REACTION; PSEUDOMONAS AERUGINOSA; PYRUVATE; REACTIVE SUBSTRATES; SECONDARY STRUCTURES; SIDEROPHORE; SITE DIRECTED MUTAGENESIS; STRUCTURAL CHANGE; STRUCTURAL HOMOLOGY; STRUCTURE-FUNCTION ANALYSIS; TRANSITION STATE STABILIZATION; X-RAY CRYSTALLOGRAPHIC STRUCTURES;

CONFORMATIONS; DICHROISM; DYNAMICS; ELECTROSTATICS; STABILIZATION;

CATALYSIS;

ISOCHORISMATE PYRUVATE LYASE; LYASE; MUTANT PROTEIN; PYRUVIC ACID; SALICYLIC ACID; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHEMICAL REACTION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STRUCTURE; MOLECULAR DYNAMICS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PSEUDOMONAS AERUGINOSA; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

BACTERIAL PROTEINS; CARBON-OXYGEN LYASES; CATALYSIS; CATALYTIC DOMAIN; CHORISMIC ACID; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PSEUDOMONAS AERUGINOSA; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI; PSEUDOMONAS AERUGINOSA;

EID: 67049134258     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900456e     Document Type: Article

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