Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase

A M Thariath, K L Fatum, M A Valvano, T Viswanatha

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17 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)27-35
Number of pages9
JournalBiochimica et biophysica acta
Volume1203
Issue number1
Publication statusPublished - 1993

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