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

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

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

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

School of Medicine, Dentistry and Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

18 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 language	English
Pages (from-to)	27-35
Number of pages	9
Journal	Biochimica et biophysica acta
Volume	1203
Issue number	1
Publication status	Published - 1993

Cite this

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title = "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.",

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year = "1993",

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pages = "27--35",

journal = "Biochimica et biophysica acta",

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T1 - Physico-chemical characterization of a recombinant cytoplasmic form of lysine

T2 - N6-hydroxylase

AU - Thariath, A M

AU - Fatum, K L

AU - Valvano, M A

AU - Viswanatha, T

PY - 1993

Y1 - 1993

N2 - 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.

AB - 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.

M3 - Article

C2 - 8218389

SN - 0006-3002

VL - 1203

SP - 27

EP - 35

JO - Biochimica et biophysica acta

JF - Biochimica et biophysica acta

IS - 1

ER -

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

Abstract

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