PHYSICOCHEMICAL CHARACTERIZATION OF A RECOMBINANT CYTOPLASMIC FORM OF LYSINE-N6-HYDROXYLASE

被引：17
|
作者：
THARIATH, AM
FATUM, KL
VALVANO, MA
VISWANATHA, T
机构：
[1] UNIV WATERLOO, GUELPH WATERLOO CTR GRAD WORK CHEM, DEPT CHEM, WATERLOO N2L 3G1, ONTARIO, CANADA
[2] UNIV WESTERN ONTARIO, DEPT MICROBIOL & IMMUNOL, LONDON N6A 3K7, ONTARIO, CANADA
来源：
BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1203卷 / 01期
关键词：
LYSINE-N6-HYDROXYLATION; FLAVOPROTEIN; OXYGEN ACTIVATION; SIDEROPHORE;
D O I：
10.1016/0167-4838(93)90032-M
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：27 / 35
页数：9
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