Mutations of glutamate-84 at the putative potassium-binding site affect camphor binding and oxidation by cytochrome P450(cam)

European Journal of Biochemistry

Volumn 265, Issue 3, 1999, Pages 929-935

  Westlake, Andrew C G ^a,b   Harford Cross, Charles F ^a   Donovan, Jacqueline ^a   Wong, Luet Lok ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

Cations; Co operativity; Cytochrome P450(cam); Electron transfer; Potassium

Indexed keywords

CAMPHOR; CYTOCHROME P450; GLUTAMIC ACID; POTASSIUM;

ARTICLE; BINDING AFFINITY; BINDING SITE; DISSOCIATION CONSTANT; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS PUTIDA;

AMINO ACID SUBSTITUTION; BINDING SITES; CAMPHOR; CAMPHOR 5-MONOOXYGENASE; ESCHERICHIA COLI; GLUTAMIC ACID; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; POINT MUTATION; POTASSIUM; PSEUDOMONAS PUTIDA; RECOMBINANT PROTEINS;

EID: 0033230093     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00793.x     Document Type: Article

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