Identification of a lysine residue in the NADH-binding site of salicylate hydroxylase from Pseudomonas putida S-1

Journal of Biochemistry

Volumn 117, Issue 3, 1995, Pages 579-585

  Suzuki, Kenzi ^a   Mizuguchi, Mitsuo ^a   Gomi, Tomoharu ^b   Itagaki, Eiji ^a  

^a KANAZAWA UNIVERSITY   (Japan)

^b Toyama Medical and Pharmaceutical University   (Japan)

Author keywords

Chemical modification; Lysine residue; NADH binding site; Pseudomonas putida S 1; Salicylate hydroxylase

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; APOPROTEIN; BACTERIAL ENZYME; FLAVINE ADENINE NUCLEOTIDE; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXYGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SALICYLIC ACID; TRINITROBENZENESULFONIC ACID;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING KINETICS; BINDING SITE; CHROMATOGRAPHY; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME ISOLATION; ENZYME KINETICS; ENZYME MODIFICATION; ENZYME STRUCTURE; NONHUMAN; OXIDATION; PSEUDOMONAS PUTIDA; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BINDING SITES; CHYMOTRYPSIN; LYSINE; MIXED FUNCTION OXYGENASES; MOLECULAR SEQUENCE DATA; NAD; PSEUDOMONAS PUTIDA; PYRIDOXAL PHOSPHATE; TRINITROBENZENESULFONIC ACID;

EID: 0028958976     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a124747     Document Type: Article

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