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
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1.14.13.59
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fad
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siderophore
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flavoproteins
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ornithine
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nicotinamide
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c4a-hydroperoxyflavin
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hydroxamate
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nadp+
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hydroxamate-containing
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oxygen-dependent
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5-aminovalerate
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aerobactin
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glutarate
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semialdehyde
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flavin-containing
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iodoacetate
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fumigatus
- 1.14.13.59
- fad
-
siderophore
- flavoproteins
- ornithine
- nicotinamide
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c4a-hydroperoxyflavin
- hydroxamate
- nadp+
-
hydroxamate-containing
-
oxygen-dependent
- 5-aminovalerate
- aerobactin
- glutarate
- semialdehyde
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flavin-containing
- iodoacetate
- fumigatus
Reaction
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
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Cofactor
Cofactor on EC 1.14.13.59 - L-lysine N6-monooxygenase (NADPH)
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FAD
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Km: 0.005 mM, parent enzyme protein rIucD and genetically engineered forms C51A rIucD, C51A/C158A rIucD and C158A rIucD
NADH
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recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus
NADH
the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH
NADPH
the enzyme displays a 3fold preference for NADPH over NADH. R301 plays a major role in NADPH selectivity by interacting with the 2'-phosphate of the adenine-ribose moiety of NADPH
additional information
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activity measurements with isotopes of NAD(P)H, kinetic isotope effects, overview
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additional information
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an unexpected protein conformation with a 30° rotation of the NAD(P)H domain with respect to the flavin adenine dinucleotide (FAD) domain precludes binding of the nicotinamide cofactor
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