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1.14.13.59: L-lysine N6-monooxygenase (NADPH)

This is an abbreviated version!
For detailed information about L-lysine N6-monooxygenase (NADPH), go to the full flat file.

Word Map on EC 1.14.13.59

Reaction

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

Synonyms

EC 1.13.12.10, EC 13.12.10, flavin-dependent lysine monooxygenase, flavin-dependent N6-lysine monooxygenase, IucD, LH, lysine monooxygenase, Lysine N(6)-hydroxylase, Lysine N6-hydroxylase, lysine N6-monooxygenase, lysine: N6-hydroxylase, lysine:N(6)-hydroxylase, Lysine:N6-hydroxylase, MbsG, N-hydroxylating monooxygenase, NbtG, Oxygenase, lysine N6-mono-

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.59 L-lysine N6-monooxygenase (NADPH)

Reference

Reference on EC 1.14.13.59 - L-lysine N6-monooxygenase (NADPH)

Please use the Reference Search for a specific query.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Plattner, H.J.; Pfefferle, P.; Romaguera, A.; Waschutza, S.; Dieckman, H.
Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222
Biol. Met.
2
1-5
1989
Escherichia coli, Escherichia coli EN222
Manually annotated by BRENDA team
Macheroux, P.; Plattner, H.J.; Romaguera, A.; Diekmann, H.
FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EC 222
Eur. J. Biochem.
213
995-1002
1993
Escherichia coli
Manually annotated by BRENDA team
Thariath, A.; Socha, D.; Valvano, M.A.; Viswanatha, T.
Construction and biochemical characterization of recombinant cytoplasmic forms of IucD protein (lysine:N6-hydroxylase) encoded by the pColV-K30 aerobactin gene cluster
J. Bacteriol.
175
589-596
1993
Escherichia coli
Manually annotated by BRENDA team
Thariath, A.M.; Fatum, K.L.; Valvano, M.A.; Viswanatha, T.
Physico-chemical characterization of a recombinant cytoplasmic form of lysine:N6-hydroxylase
Biochim. Biophys. Acta
1203
27-35
1993
Escherichia coli
Manually annotated by BRENDA team
Marrone, L.; Beecroft, M.; Viswanatha, T.
Lysine:N6-hydroxylase: cofactor interactions
Bioorg. Chem.
24
304-317
1996
Escherichia coli
-
Manually annotated by BRENDA team
Marrone, L.; Viswanatha, T.
Effect of selective cysteine --> alanine replacements on the catalytic functions of lysine:N6-hydroxylase
Biochim. Biophys. Acta
1343
263-277
1997
Escherichia coli
Manually annotated by BRENDA team
Dick, S.; Siemann, S.; Frey, H.E.; Lepock, J.R.; Viswanatha, T.
Recombinant lysine:N(6)-hydroxylase: effect of cysteine-->alanine replacements on structural integrity and catalytic competence
Biochim. Biophys. Acta
1594
219-233
2002
Escherichia coli
Manually annotated by BRENDA team
Stehr, M.; Smau, L.; Singh, M.; Seth, O.; Macheroux, P.; Ghisla, S.; Diekmann, H.
Studies with lysine N6-hydroxylase. Effect of a mutation in the assumed FAD binding site on coenzyme affinities and on lysine hydroxylating activity
Biol. Chem.
380
47-54
1999
Escherichia coli, Escherichia coli EN222
Manually annotated by BRENDA team
Dick, S.; Marrone, L.; Duewel, H.; Beecroft, M.; McCourt, J.; Viswanatha, T.
Lysine: N6-hydroxylase: stability and interaction with ligands
J. Protein Chem.
18
893-903
1999
Escherichia coli
Manually annotated by BRENDA team
Robinson, R.; Sobrado, P.
Substrate binding modulates the activity of Mycobacterium smegmatis G, a flavin-dependent monooxygenase involved in the biosynthesis of hydroxamate-containing siderophores
Biochemistry
50
8489-8496
2011
Mycolicibacterium smegmatis
Manually annotated by BRENDA team
Robinson, R.M.; Rodriguez, P.J.; Sobrado, P.
Mechanistic studies on the flavin-dependent N6-lysine monooxygenase MbsG reveal an unusual control for catalysis
Arch. Biochem. Biophys.
550-551
58-66
2014
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis G
Manually annotated by BRENDA team
Abdelwahab, H.; Robinson, R.; Rodriguez, P.; Adly, C.; El-Sohaimy, S.; Sobrado, P.
Identification of structural determinants of NAD(P)H selectivity and lysine binding in lysine N(6)-monooxygenase
Arch. Biochem. Biophys.
606
180-188
2016
Nocardia farcinica (Q5Z1T5), Nocardia farcinica IFM 10152 (Q5Z1T5)
Manually annotated by BRENDA team
Binda, C.; Robinson, R.M.; Martin Del Campo, J.S.; Keul, N.D.; Rodriguez, P.J.; Robinson, H.H.; Mattevi, A.; Sobrado, P.
An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation
J. Biol. Chem.
290
12676-12688
2015
Nocardia farcinica
Manually annotated by BRENDA team