The Enzyme Database

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Accepted name: L-lysine N6-monooxygenase (NADPH)
Reaction: L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O
For diagram of aerobactin biosynthesis, click here
Other name(s): lysine N6-hydroxylase; L-lysine 6-monooxygenase (NADPH) (ambiguous)
Systematic name: L-lysine,NADPH:oxygen oxidoreductase (6-hydroxylating)
Comments: A flavoprotein (FAD). The enzyme from strain EN 222 of Escherichia coli is highly specific for L-lysine; L-ornithine and L-homolysine are, for example, not substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64295-82-5
1.  Plattner, H.J., Pfefferle, P., Romaguera, A., Waschutza, S. and Diekmann, H. Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222. Biol. Met. 2 (1989) 1–5. [PMID: 2518519]
2.  Macheroux, P., Plattner, H.J., Romaguera, A. and Diekmann, H. FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EN 222. Eur. J. Biochem. 213 (1993) 995–1002. [PMID: 8504838]
3.  Thariath, A.M., Fatum, K.L., Valvano, M.A. and Viswanatha, T. Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase. Biochim. Biophys. Acta 1203 (1993) 27–35. [PMID: 8218389]
4.  de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570–578. [PMID: 2935523]
5.  Marrone, L., Siemann, S., Beecroft, M. and Viswanatha, T. Specificity of lysine:N-6-hydroxylase: A hypothesis for a reactive substrate intermediate in the catalytic mechanism. Bioorg. Chem. 24 (1996) 401–406.
6.  Goh, C.J., Szczepan, E.W., Menhart, N. and Viswanatha, T. Studies on lysine: N6-hydroxylation by cell-free system of Aerobacter aerogenes 62-1. Biochim. Biophys. Acta 990 (1989) 240–245. [PMID: 2493814]
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