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  • Title: Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase.
    Author: Thariath AM, Fatum KL, Valvano MA, Viswanatha T.
    Journal: Biochim Biophys Acta; 1993 Nov 10; 1203(1):27-35. PubMed ID: 8218389.
    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.
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