Kinetic and structural analysis of mutant Escherichia coli dihydroorotases: A flexible loop stabilizes the transition state

Biochemistry

Volumn 46, Issue 37, 2007, Pages 10538-10550

  Lee, Mihwa ^a   Maher, Megan J ^b   Christopherson, Richard I ^a   Guss, J Mitchell ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES; ESCHERICHIA COLI DIHYDROOROTASES; TRANSITION STATE;

BINDING SITES; CRYSTALLIZATION KINETICS; ELECTRON ENERGY LEVELS; ESCHERICHIA COLI; MOLECULAR STRUCTURE; NUCLEOTIDES;

ENZYME KINETICS;

ASPARTIC ACID DERIVATIVE; BACTERIAL ENZYME; CARBAMIC ACID DERIVATIVE; DIHYDROOROTASE;

ARTICLE; BACTERIUM MUTANT; CATALYSIS; CRYSTALLIZATION; CYCLIZATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; CYCLIZATION; DIHYDROOROTASE; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PORPHYROMONAS GINGIVALIS; PROTEIN STRUCTURE, SECONDARY; SEQUENCE DELETION; STATIC ELECTRICITY; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI;

EID: 34548687217     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701098e     Document Type: Article

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