Information on EC 1.14.13.59 - L-lysine N6-monooxygenase (NADPH)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.59
-
RECOMMENDED NAME
GeneOntology No.
L-lysine N6-monooxygenase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-lysine + NADPH + H+ + O2 = N6-hydroxy-L-lysine + NADP+ + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aerobactin biosynthesis
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Lysine degradation
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Microbial metabolism in diverse environments
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
64295-82-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-2-Aminoethyl-L-Cys + NADPH + O2
?
show the reaction diagram
1,5-Diaminopentane + NADPH + O2
?
show the reaction diagram
-
-
-
-
-
DL-4-Selenalysine + NADPH + O2
?
show the reaction diagram
DL-Homocysteine + NADPH + O2
?
show the reaction diagram
DL/DL-Allo-delta-hydroxylysine + NADPH + O2
?
show the reaction diagram
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-
-
-
-
L-Lys + NADH + O2
?
show the reaction diagram
L-Lys + NADPH + O2
?
show the reaction diagram
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enzyme catalyzes the first step in aerobactin biosynthesis
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-
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L-Lys + NADPH + O2
N6-Hydroxy-L-Lys + NADP+ + H2O
show the reaction diagram
L-lysine + iodine + O2
N6-hydroxy-L-lysine + iodate + H2O
show the reaction diagram
L-lysine + NADH + H+ + O2
N6-hydroxy-L-lysine + NAD+ + H2O
show the reaction diagram
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-
-
-
?
L-lysine + NADPH + H+ + O2
N6-hydroxy-L-lysine + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-lysine + NADPH + O2
N6-hydroxy-L-lysine + NADP+ + H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Lys + NADPH + O2
?
show the reaction diagram
-
enzyme catalyzes the first step in aerobactin biosynthesis
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-
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L-lysine + NADPH + O2
N6-hydroxy-L-lysine + NADP+ + H2O
show the reaction diagram
-
-
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
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cofactor interactions
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Carbonylcyanide-m-chlorophenylhydrazone
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Carbonylcyanide-p-fluoromethoxyphenylhydrazone
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Cinnamylidene
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Cl-
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above 600 mM, enzyme exists in a reversible inactive conformation
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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L-lysine
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substrate inhibition of the wild-type and mutant P14G enzymes
p-chloromercuribenzoate
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0.01 mM, 62% inhibition, reversed by dithiothreitol
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DL-2,3-Diaminopropionic acid
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stimulates, but remains unchanged
DL-2,6-diaminopimelic acid
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stimulates, but remains unchanged
L-Orn
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stimulates, but remains unchanged
N6-Acetyl-L-Lys
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stimulates, but remains unchanged
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016 - 0.0057
FAD
0.105
L-Lys
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0.2 - 1
L-lysine
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pH 7.5, 25C
0.018 - 1.1
NADH
0.07 - 2.4
NADPH
additional information
additional information
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kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.243 - 0.731
FAD
0.08
L-lysine
Mycobacterium smegmatis
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pH 7.5, 25C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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inhibition kinetics
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00016
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recombinant mutant P14G, with 0.005 mM FAD, and NADPH
0.0011
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recombinant mutant P14G, with 0.005 mM FAD, and iodine
0.0039
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recombinant mutant P14G, with 0.3 mM FAD, and NADPH
0.028
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recombinant mutant P14G, with 0.3 mM FAD, and iodine
0.3
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recombinant wild-type enzyme, with 0.005 mM FAD, and iodine
0.444
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recombinant wild-type enzyme, with 0.005 mM FAD, and NADPH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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assay at
8
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wild-type enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH-profile of wild-type and mutant P14G enzymes
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at with NADPH as cofactor
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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enzyme from strain EN222 and strain GR143
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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4 * 50000, SDS-PAGE
200000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
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
4C, 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 wild-type and mutants from strain DH5alpha
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression of wild-type and mutants in strain DH5alpha
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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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gene iucD, expression of wild-type and mutants in strain DH5alpha
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
Show AA Sequence (501 entries)
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