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Enzyme Nomenclature
Information on EC 1.14.13.59 - L-lysine N6-monooxygenase (NADPH)
for references in articles please use BRENDA:EC1.14.13.59
Word Map on EC 1.14.13.59
- 1.14.13.59
- fad
- iodoacetate
- aerobactin
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tetrameric
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apoenzyme
- thiols
- flavin
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flavoproteins
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.59
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RECOMMENDED NAME
GeneOntology No.
L-lysine N6-monooxygenase (NADPH)
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aerobactin biosynthesis
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus
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containing the structural gene for the enzyme on a multicopy plasmid
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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
?
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enzyme catalyzes the first step in aerobactin biosynthesis
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L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
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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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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
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iodine less effective than NADPH 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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?
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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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
?
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enzyme catalyzes the first step in aerobactin biosynthesis
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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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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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
0.1
NADPH
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recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
tetramer
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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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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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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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ENGINEERING
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
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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
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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
additional information
P14G
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site-directed mutagenesis, requires different reaction conditions for full activity and shows altered cofactor specificity than the wild-type enzyme
P14G
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site-directed mutagenesis, requires different reaction conditions for full activity and shows altered cofactor specificity than the wild-type enzyme
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additional information
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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
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a covalent C51A-dichloropehno indophenol conjugate accomodates FAD in its catalytic function
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