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Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase
A M Thariath1, K L Fatum, M A Valvano
1Guelph Waterloo Centre for Graduate Work in Chemistry, Department of Chemistry, University of Waterloo, Ontario, Canada.
Biochimica Et Biophysica Acta
|November 10, 1993
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.