1.
Trends Biochem Sci
; 23(11): 414-5, 1998 Nov.
Article
in English
| MEDLINE
| ID: mdl-9852757
Subject(s)
Flavin-Adenine Dinucleotide/metabolism , Mixed Function Oxygenases/metabolism , Alkaline Phosphatase , Binding Sites/genetics , Cyclin-Dependent Kinases/metabolism , Escherichia coli , Escherichia coli Proteins , Lac Operon , Mixed Function Oxygenases/genetics , NADP/metabolism , Protein Conformation , Recombinant Fusion Proteins/metabolism , Sequence Analysis, DNA , beta-Galactosidase/genetics , beta-Galactosidase/metabolism
2.
Biochim Biophys Acta
; 1203(1): 27-35, 1993 Nov 10.
Article
in English
| MEDLINE
| ID: mdl-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.