Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: The catalytic mechanism of a complex oxidation involved in NAD biosynthesis

Biochemistry

Volumn 44, Issue 21, 2005, Pages 7632-7643

  Zhang, Yang ^a   Colabroy, Keri L ^a   Begley, Tadhg P ^a   Ealick, Steven E ^a  

^a Department of Obstetrics Gynecology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3-HYDROXYANTHRAILATE-3,4-DIOXYGENASE (HAD); NICOTINAMIDE ADENINE DINUCLEOTIDES; PYRIDINE; QUINOLATE;

BIOSYNTHESIS; CATALYSIS; DIMERS; ENZYME INHIBITION; IRON; MUTAGENESIS; POSITIVE IONS; STRUCTURE (COMPOSITION); SULFUR;

ENZYMES;

3 HYDROXYANTHRANILATE 3,4 DIOXYGENASE; DIMER; FERROUS ION; HYDROGEN; IRON; MONOMER; NICOTINAMIDE ADENINE DINUCLEOTIDE; NITRIC OXIDE; QUINOLINIC ACID; TRYPTOPHAN;

ARTICLE; BINDING SITE; BIOSYNTHESIS; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME STRUCTURE; HYDROGEN BOND; ISOMERIZATION; LIGAND BINDING; MUTAGENESIS; OXIDATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; RALSTONIA;

3-HYDROXYANTHRANILATE 3,4-DIOXYGENASE; 3-HYDROXYANTHRANILIC ACID; BINDING SITES; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIOXYGENASES; ENZYME INHIBITORS; FERRIC COMPOUNDS; LIGANDS; MUTAGENESIS, SITE-DIRECTED; NAD; OXIDATION-REDUCTION; PROTEIN CONFORMATION; RALSTONIA; SUBSTRATE SPECIFICITY;

RALSTONIA; WAUTERSIA METALLIDURANS;

EID: 19644363211     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047353l     Document Type: Article

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