Site-directed mutagenesis of potential catalytic residues in 1H-3- hydroxy-4-oxoquinoline 2,4-dioxygenase, and hypothesis on the catalytic mechanism of 2,4-dioxygenolytic ring cleavage

FEMS Microbiology Letters

Volumn 190, Issue 1, 2000, Pages 21-27

  Fischer, Frank ^a   Fetzner, Susanne ^a  

^a UNIVERSITY OF OLDENBURG   (Germany)

Author keywords

Hydrolase fold; 1H 3 Hydroxy 4 oxoquinoline; Base catalysis; Cofactor free dioxygenase; Flavin; Radical pair

Indexed keywords

1H 3 HYDROXY 4 OXOQUINOLINE 2,4 DIOXYGENASE; AMINO ACID; BACTERIAL ENZYME; FLAVINE MONONUCLEOTIDE; HYDROLASE; LUCIFERASE; OXYGENASE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PSEUDOMONAS PUTIDA; REACTION ANALYSIS; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

CATALYSIS; CATALYTIC DOMAIN; DIOXYGENASES; ESCHERICHIA COLI; FLAVINS; KINETICS; MUTAGENESIS, SITE-DIRECTED; OXYGENASES; PSEUDOMONAS PUTIDA; QUINOLONES;

EID: 0034284245     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(00)00309-8     Document Type: Article

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