E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases

Structure

Volumn 10, Issue 9, 2002, Pages 1211-1223

  Norager, Sofie ^a   Jensen, Kaj Frank ^a   Björnberg, Olof ^a   Larsen, Sine ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Flavoproteins; Hydride transfer; Orotate binding; Pyrimidine nucleotide biosynthesis; Reaction mechanism; Structural comparisons

Indexed keywords

CYSTEINE; DIHYDROOROTATE DEHYDROGENASE; ISOENZYME; SERINE; URIDINE PHOSPHATE; OXIDOREDUCTASE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BIOSYNTHESIS; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; ESCHERICHIA COLI; HUMAN VERSUS ANIMAL COMPARISON; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FUNCTION; SPECIES COMPARISON; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CLASSIFICATION; ENZYMOLOGY; HUMAN; HYDROGEN BOND; METABOLISM; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ANIMALIA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0041433824     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00831-6     Document Type: Article

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