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
-
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
Advanced search results
KM Value
KM Value on EC 1.14.13.59 - L-lysine N6-monooxygenase (NADPH)
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0.07
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parent enzyme protein rIucD and genetically engineered forms C51A rIucD, C51A/C158A rIucD and C158A rIucD
0.08
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption
0.09
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption
0.1
NADPH
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recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus
0.14
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption
0.4
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption
0.4
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption
0.7
NADPH
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pH 7.5, 25°C, recombinant mutant P238R, L-lysine hydroxylation
1.5
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption
2.6
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption
additional information
additional information
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analysis of steady-state and rapid reaction conditions using primary and solvent kinetic isotope effects, stopped-flow and steady-state kinetics, overview
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additional information
additional information
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Michaelis-Menten steady-state kinetics, determined by oxygen consumption assay or L-lysine hydroxylation assay
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