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+
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hydroxamate-containing
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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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Substrates Products
Substrates Products on EC 1.14.13.59 - L-lysine N6-monooxygenase (NADPH)
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REACTION DIAGRAM
L-Lys + NADPH + O2
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enzyme catalyzes the first step in aerobactin biosynthesis
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(S)-2-Aminoethyl-L-Cys + NADPH + O2
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i.e. L-aminoethylcysteine
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L-Lys + NADH + O2
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with lower efficiency than NADPH, recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus
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L-Lys + NADPH + O2
N6-Hydroxy-L-Lys + NADP+ + H2O
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specific for NADPH
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L-Lys + NADPH + O2
N6-Hydroxy-L-Lys + NADP+ + H2O
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specific for NADPH
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N6-hydroxy-L-lysine + iodate + H2O
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iodine less effective than NADPH for the wild-type enzyme
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L-lysine + iodine + O2
N6-hydroxy-L-lysine + iodate + H2O
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iodine less effective than NADPH for the wild-type enzyme
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N6-hydroxy-L-lysine + NAD+ + H2O
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L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
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the hydride transfer is rate-limiting
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L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
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L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
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the hydride transfer is rate-limiting
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L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
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, while E216 plays a role in L-Lys binding and FAD reduction
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L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
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, while E216 plays a role in L-Lys binding and FAD reduction
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N6-hydroxy-L-lysine + NADP+ + H2O
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L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
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the hydride transfer is rate-limiting
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L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
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L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
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the hydride transfer is rate-limiting
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L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
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, while E216 plays a role in L-Lys binding and FAD reduction
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L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
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, while E216 plays a role in L-Lys binding and FAD reduction
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L-lysine + NADPH + O2
N6-hydroxy-L-lysine + NADP+ + H2O
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NADPH preferred compared to iodine for the wild-type enzyme
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L-lysine + NADPH + O2
N6-hydroxy-L-lysine + NADP+ + H2O
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NADPH preferred compared to iodine for the wild-type enzyme
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in absence of substrate, the enzyme has an NADPH oxidase activity which results in generation of H2O2
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additional information
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enzyme functions as an oxidase when the activity of MbsG is measured by monitoring oxygen consumption in the absence of L-lysine, oxidizing NADH and NADPH with kcat values of 59 and 49 per min, respectively. Under these conditions, both hydrogen peroxide and superoxide are produced
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additional information
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MbsG is non-specific for reduced pyridine dinucleotide, as it can utilize both NADH and NADPH with similar catalytic efficiency. But MbsG is specific for L-lysine and shows no activity with L-ornithine, 6-amino-1-hexanol, L-arginine, putrescine, and cadaverine
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additional information
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MbsG is non-specific for reduced pyridine dinucleotide, as it can utilize both NADH and NADPH with similar catalytic efficiency. But MbsG is specific for L-lysine and shows no activity with L-ornithine, 6-amino-1-hexanol, L-arginine, putrescine, and cadaverine
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additional information
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NbtG is unable to stabilize the FADOOH intermediate, which results in production of hydrogen peroxide and superoxide. NbtG is also active on D-Lys, although it binds L-Lys with a higher affinity. NbtG can use both NADH and NADPH and is highly uncoupled, producing more superoxide and hydrogen peroxide than hydroxylated Lys. NbtG is highly active in the absence of L-Lys, having about 2fold higher activity with NADPH as compared with NADH. Under these conditions, NbtG functions as an oxidase, as no hydroxylation occurs, overview
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