title: Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase.
abstract: A recombinant cytoplasmic preparation of lysine: N6-hydroxylase, IucD398, with a deletion of 47 amino acids at the N-terminus, was purified to homogeneity. IucD398 is capable of N-hydroxylation of L-lysine upon supplementation with FAD and NADPH. The enzyme is stringently specific with L-lysine and (S)-2-aminoethyl-L-cysteine serving as substrates. Protonophores, FCCP and CCCP, as well as cinnamylidene, have been found to serve as potent inhibitors of lysine: N6-hydroxylation by virtue of their ability to interfere in the reduction of the flavin cofactor.
authors.affiliation: Guelph Waterloo Centre for Graduate Work in Chemistry, Department of Chemistry, University of Waterloo, Ontario, Canada.
authors.forename: A M
authors.initials: AM
authors.lastname: Thariath
authors.forename: K L
authors.initials: KL
authors.lastname: Fatum
authors.forename: M A
authors.initials: MA
authors.lastname: Valvano
authors.forename: T
authors.initials: T
authors.lastname: Viswanatha
mesh_terms: D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone / Q000494:pharmacology; D003593:Cytoplasm / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology; D005182:Flavin-Adenine Dinucleotide; D006861:Hydrogen Peroxide / Q000737:chemistry; D006899:Mixed Function Oxygenases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification*; D009249:NADP; D011994:Recombinant Proteins / Q000737:chemistry; D013379:Substrate Specificity
chemical_list: D011994:Recombinant Proteins; D005182:Flavin-Adenine Dinucleotide; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; D009249:NADP; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D006861:Hydrogen Peroxide; D006899:Mixed Function Oxygenases; C047196:lysine N-epsilon hydroxylase