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Information on EC 1.14.13.59 - L-lysine N6-monooxygenase (NADPH)
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EC Tree
1.14.13.59 L-lysine N6-monooxygenase (NADPH)IUBMB Comments
A flavoprotein (FAD). The enzyme from strain EN 222 of Escherichia coli is highly specific for L-lysine; L-ornithine and L-homolysine are, for example, not substrates.
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Word Map
- 1.14.13.59
- fad
-
siderophore
- ornithine
- flavoproteins
-
c4a-hydroperoxyflavin
- nicotinamide
- hydroxamate
- nadp+
- iodoacetate
- aerobactin
- glutarate
- 5-aminovalerate
- fumigatus
-
flavin-containing
- semialdehyde
-
oxygen-dependent
-
hydroxamate-containing
The enzyme appears in viruses and cellular organisms
Synonyms
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 13.12.10
-
-
-
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flavin-dependent N6-lysine monooxygenase
IucD
LH
Lysine N(6)-hydroxylase
-
-
-
-
Lysine N6-hydroxylase
lysine N6-monooxygenase
Lysine:N6-hydroxylase
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-
-
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MbsG
N-hydroxylating monooxygenase
NbtG
Oxygenase, lysine N6-mono-
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-
-
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IucD
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-
-
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Lysine N6-hydroxylase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
reaction mechanism, Cys51 is involved, while Cys31, Cys146, Cys158, and Cys166 are not
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L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O
unique mechanism where a rate-limiting and pH-sensitive conformational change occurs in the reductive half-reaction, which affects the efficiency of lysine hydroxylation
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L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O
via C4a-hydroperoxyflavin intermediate
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L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O
unique mechanism where a rate-limiting and pH-sensitive conformational change occurs in the reductive half-reaction, which affects the efficiency of lysine hydroxylation
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
L-lysine,NADPH:oxygen oxidoreductase (6-hydroxylating)
A flavoprotein (FAD). The enzyme from strain EN 222 of Escherichia coli is highly specific for L-lysine; L-ornithine and L-homolysine are, for example, not substrates.
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CAS REGISTRY NUMBER
COMMENTARY
64295-82-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Lys + NADPH + O2
?
-
enzyme catalyzes the first step in aerobactin biosynthesis
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-
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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
?
-
with lower efficiency than NADPH, recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus
-
-
-
L-Lys + NADPH + O2
N6-Hydroxy-L-Lys + NADP+ + H2O
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specific for NADPH
-
-
L-Lys + NADPH + O2
N6-Hydroxy-L-Lys + NADP+ + H2O
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specific for NADPH
-
-
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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-
?
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
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-
-
-
?
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
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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
-
-
?
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
-
the hydride transfer is rate-limiting
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-
?
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
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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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-
?
additional information
?
-
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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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-
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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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Lys + NADPH + O2
?
-
enzyme catalyzes the first step in aerobactin biosynthesis
-
-
-
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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-
-
-
?
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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-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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; requires FAD
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
inhibition of the wild-type and mutant P14G enzymes at very high concentrations
FAD analogs
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complete loss of activity after prolonged incubation with 8-chloro-FAD, 8-fluoro-FAD, 8-mercapto-FAD or 8-methoxy-FAD
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p-chloromercuribenzoate
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0.01 mM, 62% inhibition, reversed by dithiothreitol
additional information
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number of cysteine residues in wild-type and mutant enzymes accessible for modification with DTNB, overview
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additional information
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enzyme is sensitive to deleterious action of endoproteases trypsin, carboxypeptidase Y, and chymotrypsin, FAD and ADP protect, proteolysis of a C-terminal segment results in loss of enzyme activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
NADPH
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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; 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
-
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1.29
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.94
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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
containing the structural gene for the enzyme on a multicopy plasmid
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brenda
recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus
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brenda
strain GR143 and EN222, and strain which produce recombinant enzymes
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brenda
containing the structural gene for the enzyme on a multicopy plasmid
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brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
-
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
physiological function
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Mycobacterium smegmatis G (MbsG) is a flavin-dependent L-lysine monooxygenase involved in the biosynthesis of the siderophore mycobactin, overview
physiological function
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the flavoenzyme catalyzes the NADPH-and oxygen-dependent hydroxylation of lysine, NbtG utilizes NADPH and molecular oxygen to hydroxylate the Nepsilon-atom of L-Lys. NbtG is unable to stabilize the FADOOH intermediate, which results in production of hydrogen peroxide and superoxide. The biosynthesis of the siderophore nocobactin in Nocardia farcinica requires functioning of NbtG
physiological function
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Mycobacterium smegmatis G (MbsG) is a flavin-dependent L-lysine monooxygenase involved in the biosynthesis of the siderophore mycobactin, overview
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Show AA Sequence and Transmembrane Helices (717 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Erwinia amylovora (strain CFBP1430)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
tetramer
-
with time the enzyme aggregates to polytetrameric forms, which is reversible by thiols, the C-terminal segment is important for activity and conformational stability
additional information
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comparison of amino acid sequences of enzyme-encoding genes iucD and aerA
additional information
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comparison of amino acid sequences of enzyme-encoding genes iucD and aerA
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged wild-type and seleno-L-methionine-labeled enzyme mutant K184A, method screening, drop vapor diffusion method, mixing of 0.001 ml of 6 mg/ml protein in 25 mM HEPES/NaOH, pH 7.5, 500 mM NaCl, and 5 mM NADP+ in the presence of either L-Lys or D-Lys, with 0.001 ml of reservoir solution containing 10% w/v PEG 6000, 5% v/v 2,4-methylpentanediol, and 0.1 M HEPES/NaOH, pH 7.5, 3-4 days at 20°C, micro-seeding technique, X-ray diffraction structure determination and analysis at 2.4-2.9 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C146A
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site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C158A
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site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C166A
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site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C31A
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site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C31A/C51A
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site-directed mutagenesis, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
C51A
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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
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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
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site-directed mutagenesis, about 2fold increased activity, unaffected thermal stability, and affinity for L-lysine and FAD compared to the wild-type enzyme
P14G
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
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
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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
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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
-
additional information
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is sensitive to deleterious action of proteases, FAD and ADP protect, while NADPH protects only partially, and L-lysine and L-norleucine are ineffective in protecting the enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, medium of ionic strength 0.25 or higher, recombinant enzyme form IacD398, stable for 1 month
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme form IucD439, in which the sequence encoding the IucD protein is fused in frame to the amino-terminal sequence of beta-galactosidase
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recombinant His-tagged wild-type and P14G mutant enzymes from strain M15-2 to homogeneity by gel filtration, ion exchange and nickel affinity chromatography
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recombinant His8-MBP-tagged wild-type and mutant K184A enzymes, as well as seleno-L-methionine-labeled enzyme from Escherichia coli TOP10 cells by nickel affinity chromatography, dialysis, tag cleavage by TEV protease, followed by a second step of nickel affinity chromatography and by MBP-tracking affinity chromatography, eluting the detagged enzyme, followed by dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aerA, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and P14G mutant enzymes in strain M15-2, comparison of nucleotide sequences of enzyme-encoding genes iucD and aerA
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recombinant expression of His8-MBP-tagged wild-type and mutant K184A enzymes, as well as seleno-L-methionine-labeled enzyme in Escherichia coli TOP10 cells
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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
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
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