Dioxygenases Without Requirement for Cofactors: Identification of Amino Acid Residues Involved in Substrate Binding and Catalysis, and Testing for Rate-Limiting Steps in the Reaction of 1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase

Current Microbiology

Volumn 51, Issue 5, 2005, Pages 344-352

  Frerichs Deeken, Ursula ^a,b   Fetzner, Susanne ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

^b UNIVERSITY OF OLDENBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

1H 3 HYDROXY 4 OXOQUINALDINE 2,4 DIOXYGENASE; AMINO ACID; HYDROLASE; ISOTOPE; OXYGEN; PROTON; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID ANALYSIS; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; NONHUMAN; NUCLEOTIDE SEQUENCE; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; VISCOSITY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO ACIDS; BINDING SITES; CATALYTIC DOMAIN; COENZYMES; DIOXYGENASES; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; MUTAGENESIS, SITE-DIRECTED; SEQUENCE ALIGNMENT; VISCOSITY;

EID: 27744471646     PISSN: 03438651     EISSN: 14320991     Source Type: Journal    
DOI: 10.1007/s00284-005-0065-3     Document Type: Article

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