The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis

Biochemistry

Volumn 38, Issue 10, 1999, Pages 2899-2908

  Björnberg, Olof ^a   Grüner, Anne Charlotte ^a,c   Roepstorff, Peter ^b   Jensen, Kaj Frank ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

^c INSTITUT PASTEUR   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CYSTEINE; DIHYDROOROTATE DEHYDROGENASE; OROTIC ACID; SERINE; TRYPSIN;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME STRUCTURE; ESCHERICHIA COLI; MUTAGENESIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

BINDING SITES; CHROMATOGRAPHY, GEL; CONSERVED SEQUENCE; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; HYDROLYSIS; ISOENZYMES; KINETICS; MUTAGENESIS, SITE-DIRECTED; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SERINE; SPECTROMETRY, FLUORESCENCE; TRYPSIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; LACTOCOCCUS LACTIS;

EID: 0039021706     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982352c     Document Type: Article

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