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Volumn 39, Issue 34, 2000, Pages 10373-10384

Dihydroorotate dehydrogenase from Clostridium oroticum is a class 1B enzyme and utilizes a concerted mechansim of catalysis

(3) Argyrou, A a,c Washabaugh, M W b Pickart, C M a

a JOHNS HOPKINS UNIVERSITY (United States)

b MERCK RESEARCH LABORATORIES (United States)

c ALBERT EINSTEIN COLLEGE OF MEDICINE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DIHYDROOROTATE DEHYDROGENASE; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; POLYPEPTIDE;

ARTICLE; CATALYSIS; CLOSTRIDIUM; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME KINETICS; IONIZATION; NONHUMAN; OXIDATION REDUCTION REACTION; PH; PRIORITY JOURNAL; PROTON TRANSPORT; SEQUENCE ANALYSIS; STEADY STATE;

ANIMALS; CATALYSIS; CATALYTIC DOMAIN; CATTLE; CLOSTRIDIUM; DEUTERIUM; ELECTRON TRANSPORT; HYDROGEN-ION CONCENTRATION; KINETICS; LACTOCOCCUS LACTIS; MODELS, MOLECULAR; MOLECULAR WEIGHT; OROTIC ACID; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PROTEIN STRUCTURE, QUATERNARY;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM OROTICUM; FELIS CATUS;

EID: 0034730083 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi001111d Document Type: Article

Times cited : (33)

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