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Biochemistry

Volumn 39, Issue 31, 2000, Pages 9174-9187

Rhodococcus L-phenylalanine dehydrogenase: Kinetics, mechanism, and structural basis for catalytic specifity

(4) Brunhuber, N M W a,d Thoden, J B b Blanchard, J S a Vanhooke, J L c

a ALBERT EINSTEIN COLLEGE OF MEDICINE (United States)

b UNIVERSITY OF WISCONSIN (United States)

c UNIVERSITY OF WISCONSIN MADISON (United States)

d Medical Action Communications (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; PHENYLALANINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

AMINO ACID METABOLISM; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME PURIFICATION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; RHODOCOCCUS;

AMINO ACID OXIDOREDUCTASES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; HYDROGEN; HYDROGEN-ION CONCENTRATION; KINETICS; LACTATES; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NAD; NADP; PHENYLALANINE; PHENYLPROPIONATES; PROTEIN CONFORMATION; RHODOCOCCUS; STEREOISOMERISM; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); RHODOCOCCUS; RHODOCOCCUS SP.;

EID: 0034622509 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi000494c Document Type: Article

Times cited : (107)

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