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.

Cite this paper

@article{Thariath1993PhysicochemicalCO, title={Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase.}, author={Abraham Thariath and K L Fatum and Miguel A Valvano and Thammaiah Viswanatha}, journal={Biochimica et biophysica acta}, year={1993}, volume={1203 1}, pages={27-35} }