Phenylalanine dehydrogenase from Rhodococcus sp. M4: High-resolution X- ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism

Biochemistry

Volumn 38, Issue 8, 1999, Pages 2326-2339

  Vanhooke, Janeen L ^a   Thoden, James B ^a   Brunhuber, Norbert M W ^b   Blanchard, John S ^c   Holden, Hazel M ^b  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b SCIENCE APPLICATIONS INTERNATIONAL CORPORATION   (United States)

^c ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DIMER; HYDROCINNAMIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; PHENYLALANINE DEHYDROGENASE; PHENYLPYRUVIC ACID; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DEAMINATION; ENZYME ACTIVE SITE; ENZYME ASSAY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; REACTION ANALYSIS; RHODOCOCCUS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

AMINO ACID OXIDOREDUCTASES; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DEAMINATION; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; NAD; OXIDATION-REDUCTION; PHENYLPROPIONATES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RHODOCOCCUS;

ACTINOBACTERIA (CLASS); BACTERIA (MICROORGANISMS); RHODOCOCCUS; RHODOCOCCUS SP.; UNCULTURED ACTINOMYCETE;

EID: 0033596724     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982244q     Document Type: Article

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