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(S)-2-Aminoethyl-L-Cys + NADPH + O2
?
1,5-Diaminopentane + NADPH + O2
?
-
-
-
-
?
D-lysine + NADH + H+ + O2
N6-hydroxy-D-lysine + NAD+ + H2O
-
-
-
-
?
D-lysine + NADPH + H+ + O2
N6-hydroxy-D-lysine + NADP+ + H2O
-
-
-
-
?
DL-4-Selenalysine + NADPH + O2
?
DL-Homocysteine + NADPH + O2
?
DL/DL-Allo-delta-hydroxylysine + NADPH + O2
?
-
-
-
-
?
L-Lys + NADPH + O2
?
-
enzyme catalyzes the first step in aerobactin biosynthesis
-
-
?
L-Lys + NADPH + O2
N6-Hydroxy-L-Lys + NADP+ + H2O
L-lysine + iodine + O2
N6-hydroxy-L-lysine + iodate + H2O
L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
L-lysine + NADPH + O2
N6-hydroxy-L-lysine + NADP+ + H2O
additional information
?
-
(S)-2-Aminoethyl-L-Cys + NADPH + O2
?
-
-
-
-
?
(S)-2-Aminoethyl-L-Cys + NADPH + O2
?
-
i.e. L-aminoethylcysteine
-
-
?
(S)-2-Aminoethyl-L-Cys + NADPH + O2
?
-
i.e. L-aminoethylcysteine
-
-
?
DL-4-Selenalysine + NADPH + O2
?
-
-
-
-
?
DL-4-Selenalysine + NADPH + O2
?
-
-
-
-
?
DL-Homocysteine + NADPH + O2
?
-
-
-
-
?
DL-Homocysteine + NADPH + O2
?
-
-
-
-
?
L-Lys + NADH + O2
?
-
-
-
-
?
L-Lys + NADH + O2
?
-
with lower efficiency than NADPH, recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus
-
-
?
L-Lys + NADH + O2
?
-
-
-
-
?
L-Lys + NADPH + O2
N6-Hydroxy-L-Lys + NADP+ + H2O
-
-
-
?
L-Lys + NADPH + O2
N6-Hydroxy-L-Lys + NADP+ + H2O
-
-
-
-
?
L-Lys + NADPH + O2
N6-Hydroxy-L-Lys + NADP+ + H2O
-
specific for NADPH
-
?
L-Lys + NADPH + O2
N6-Hydroxy-L-Lys + NADP+ + H2O
-
specific for NADPH
-
?
L-lysine + iodine + O2
N6-hydroxy-L-lysine + iodate + H2O
-
iodine less effective than NADPH for the wild-type enzyme
-
-
?
L-lysine + iodine + O2
N6-hydroxy-L-lysine + iodate + H2O
-
iodine less effective than NADPH for the wild-type enzyme
-
-
?
L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
-
-
-
-
?
L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
-
the hydride transfer is rate-limiting
-
-
?
L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
-
-
-
-
?
L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
-
the hydride transfer is rate-limiting
-
-
?
L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
-
-
-
-
?
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
-
-
?
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
-
-
?
L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
-
-
-
-
?
L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
-
the hydride transfer is rate-limiting
-
-
?
L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
-
-
-
-
?
L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
-
the hydride transfer is rate-limiting
-
-
?
L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
-
-
-
-
?
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
-
-
?
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
-
-
?
L-lysine + NADPH + O2
N6-hydroxy-L-lysine + NADP+ + H2O
-
-
-
-
?
L-lysine + NADPH + O2
N6-hydroxy-L-lysine + NADP+ + H2O
-
NADPH preferred compared to iodine for the wild-type enzyme
-
-
?
L-lysine + NADPH + O2
N6-hydroxy-L-lysine + NADP+ + H2O
-
NADPH preferred compared to iodine for the wild-type enzyme
-
-
?
additional information
?
-
-
in absence of substrate, the enzyme has an NADPH oxidase activity which results in generation of H2O2
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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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additional information
additional information
-
49
D-Lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADPH
62
D-Lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADH
0.0016
FAD
-
mutant C51A, pH 7.0, 37°C
0.0019
FAD
-
mutant C146A, pH 7.0, 37°C
0.0021
FAD
-
mutant C51A/C158A, pH 7.0, 37°C
0.0022
FAD
-
mutant C166A, pH 7.0, 37°C
0.0025
FAD
-
mutant C31A, pH 7.0, 37°C
0.0033
FAD
-
wild-type enzyme, pH 7.0, 37°C
0.0047
FAD
-
mutant C51A/C166A, pH 7.0, 37°C
0.0056
FAD
-
mutant C31A/C51A, pH 7.0, 37°C
0.0057
FAD
-
mutant C158A, pH 7.0, 37°C
0.2 - 1
L-lysine
-
pH 7.5, 25°C
2.4
L-lysine
-
pH 7.5, 25°C, with NADH
12
L-lysine
-
pH 7.5, 25°C, with NADPH
13
L-lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADPH
40
L-lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADH
0.018
NADH
-
-
0.4
NADH
-
pH 7.5, 25°C, recombinant wild-type enzyme, with L-Lys
1.6
NADH
-
pH 7.5, 25°C, recombinant wild-type enzyme, with D-Lys
0.07
NADPH
-
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
-
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
0.14
NADPH
-
pH 7.5, 25°C, recombinant wild-type enzyme, with L-Lys
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
0.51
NADPH
-
pH 7.5, 25°C, recombinant wild-type enzyme, with D-Lys
0.7
NADPH
-
pH 7.5, 25°C, recombinant mutant P238R, L-lysine hydroxylation
0.8
NADPH
-
pH 7.5, 25°C, recombinant mutant P238R, O2 consumption
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
-
kinetics
-
additional information
additional information
-
analysis of steady-state and rapid reaction conditions using primary and solvent kinetic isotope effects, stopped-flow and steady-state kinetics, overview
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics, determined by oxygen consumption assay or L-lysine hydroxylation assay
-
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0.6
O2
-
pH 7.5, 25°C, recombinant mutant P238R, with NADPH
0.021
D-Lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADH
0.13
D-Lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADPH
0.243
FAD
-
mutant C146A, pH 7.0, 37°C
0.305
FAD
-
mutant C166A, pH 7.0, 37°C
0.351
FAD
-
mutant C31A, pH 7.0, 37°C
0.405
FAD
-
wild-type enzyme, pH 7.0, 37°C
0.425
FAD
-
mutant C158A, pH 7.0, 37°C
0.543
FAD
-
mutant C51A/C158A, pH 7.0, 37°C
0.614
FAD
-
mutant C31A/C51A, pH 7.0, 37°C
0.667
FAD
-
mutant C51A, pH 7.0, 37°C
0.731
FAD
-
mutant C51A/C166A, pH 7.0, 37°C
0.08
L-lysine
-
pH 7.5, 25°C
0.146
L-lysine
-
pH 7.5, 25°C, recombinant mutant P238R, with NADPH
0.18
L-lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADH
0.34
L-lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADPH
0.43
L-lysine
-
pH 7.5, 25°C, with NADH
0.55
L-lysine
-
pH 7.5, 25°C, with NADPH
1.29
NADH
-
pH 7.5, 25°C, recombinant wild-type enzyme, with L-Lys
2.5
NADH
-
pH 7.5, 25°C, recombinant wild-type enzyme, with D-Lys
0.7
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption
0.8
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption
0.98
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption
1.08
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption
1.08
NADPH
-
pH 7.5, 25°C, recombinant wild-type enzyme, with L-Lys
1.29
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption
2.4
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption
2.9
NADPH
-
pH 7.5, 25°C, recombinant wild-type enzyme, with D-Lys
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0.00034
D-Lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADH
0.0027
D-Lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADPH
1.563
D-Lysine
-
pH 7.5, 25°C, recombinant wild-type enzyme, with NADH
5.686
D-Lysine
-
pH 7.5, 25°C, recombinant wild-type enzyme, with NADPH
0.0045
L-lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADH
0.026
L-lysine
-
pH 7.5, 25°C, recombinant mutant K64A, with NADPH
0.046
L-lysine
-
pH 7.5, 25°C, with NADPH
0.179
L-lysine
-
pH 7.5, 25°C, with NADH
3.225
L-lysine
-
pH 7.5, 25°C, recombinant wild-type enzyme, with NADH
7.714
L-lysine
-
pH 7.5, 25°C, recombinant wild-type enzyme, with NADPH
0.026
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption
0.21
NADPH
-
pH 7.5, 25°C, recombinant mutant P238R, L-lysine hydroxylation
0.545
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption
0.79
NADPH
-
pH 7.5, 25°C, recombinant mutant P238R, O2 consumption
0.94
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption
3.3
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption
5.95
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption
7.7
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption
8.9
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption
10.7
NADPH
pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption
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C146A
-
site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C158A
-
site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C166A
-
site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C31A
-
site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C31A/C51A
-
site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C51A
-
site-directed mutagenesis, about 2fold increased activity, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C51A rlucD
-
activity of the genetically engineered enzyme forms C51A rIucD, C51A/C158A eIucD is 1.5times that of the parent rIucD. The activity of C158A rIucD is similar to that of the parent enzyme form
C51A/C158A
-
site-directed mutagenesis, about 2fold increased activity, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C51A/C158A rlucD
-
activity of the genetically engineered enzyme forms C51A rIucD, C51A/C158A eIucD is 1.5times that of the parent rIucD. The activity of C158A rIucD is similar to that of the parent enzyme form
C51A/C166A
-
site-directed mutagenesis, about 2fold increased activity, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
E216Q
mutation increases the Km value for L-Lys by 30fold with very little change on the kcat value or in the binding of NAD(P)H
K184A
-
site-directed mutagenesis
K200A
-
site-directed mutagenesis
K202A
-
site-directed mutagenesis
K64A
-
site-directed mutagenesis, the K64A variant support a conserved amino acid substrate binding site among members of the NMO group of enzymes, crystal structure analysis, overview
M239R
mutation results in high production of hydrogen peroxide and little hydroxylation with no change in coenzyme selectivity
P238R
-
site-directed mutagenesis, substitution of Pro to an Arg at position 238 converts NbtG into a NADPH-specific monooxygenase but increases the Km value for NADPH. The P238R enzyme is as uncoupled as wild-type NbtG
R301A
mutation causes a 300fold decrease on kcat/Km value with NADPH but no change with NADH
E216Q
-
mutation increases the Km value for L-Lys by 30fold with very little change on the kcat value or in the binding of NAD(P)H
-
M239R
-
mutation results in high production of hydrogen peroxide and little hydroxylation with no change in coenzyme selectivity
-
R301A
-
mutation causes a 300fold decrease on kcat/Km value with NADPH but no change with NADH
-
P14G
-
site-directed mutagenesis, requires different reaction conditions for full activity and shows altered cofactor specificity than the wild-type enzyme
P14G
-
site-directed mutagenesis, requires different reaction conditions for full activity and shows altered cofactor specificity than the wild-type enzyme
-
additional information
-
construction of recombinant IucD proteins with modified amino termini by creating three in-frame gene fusions of IucD to the amino-terminal amino acids of the cytoplasmic enzyme beta-galactosidase. Two of these constructs result in the addition of the iucD coding region of a hydrophilic leader sequence of 13 and 30 amino acids. The other construct involves the deletion of the first 47 amino acids of the IucD amino terminus and the addition of 19 amino acids of the amino terminus of beta-galactosidase. Cells expressing any of the three recombinant IucD forms produce soluble N6-hydroxylysine
additional information
-
a covalent C51A-dichloropehno indophenol conjugate accomodates FAD in its catalytic function
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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
brenda
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
brenda
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
brenda
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
brenda
Marrone, L.; Beecroft, M.; Viswanatha, T.
Lysine:N6-hydroxylase: cofactor interactions
Bioorg. Chem.
24
304-317
1996
Escherichia coli
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda