IUBMB Enzyme Nomenclature

EC 1.14.13.59

Accepted name: L-lysine N6-monooxygenase (NADPH)

Reaction: L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O

For diagram of reaction 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

References:

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]

[EC 1.14.13.59 created 1999, modified 2001, modified 2012]


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