Information on EC 1.4.3.20 - L-lysine 6-oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.4.3.20
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RECOMMENDED NAME
GeneOntology No.
L-lysine 6-oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-lysine + O2 + H2O = (S)-2-amino-6-oxohexanoate + H2O2 + NH3
show the reaction diagram
Differs from EC 1.4.3.13, protein-lysine 6-oxidase, by using free L-lysine rather than the protein-bound form. 2-N-Acetyl-L-lysine is also a substrate, but 6-N-acetyl-L-lysine, which has an acetyl group at position 6, is not a substrate. Also acts on L-ornithine, D-lysine and 4-hydroxy-L-lysine, but more slowly. The amines cadaverine and putrescine are not substrates
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SYSTEMATIC NAME
IUBMB Comments
L-lysine:oxygen 6-oxidoreductase (deaminating)
Differs from EC 1.4.3.13, protein-lysine 6-oxidase, by using free L-lysine rather than the protein-bound form. N2-Acetyl-L-lysine is also a substrate, but N6-acetyl-L-lysine, which has an acetyl group at position 6, is not a substrate. Also acts on L-ornithine, D-lysine and 4-hydroxy-L-lysine, but more slowly. The amines cadaverine and putrescine are not substrates [2].
CAS REGISTRY NUMBER
COMMENTARY hide
860791-20-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-N-acetyl-L-lysine + H2O
N-acetyl-6-oxo-L-norleucine + H2O2 + NH3
show the reaction diagram
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91.9% of the activity with L-lysine
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?
D-lysine + O2 + H2O2
?
show the reaction diagram
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?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
show the reaction diagram
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
show the reaction diagram
L-lysine + O2 + H2O2
2-aminoadipate 6-semialdehyde + NH3 + H2O2
show the reaction diagram
L-ornithine + O2 + H2O
(2S)-2-hydroxy-5-oxopentanoate + NH3 + H2O2
show the reaction diagram
L-ornithine + O2 + H2O
5-oxo-L-norvaline + H2O2 + NH3
show the reaction diagram
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15.1% of activity with L-lysine
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?
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-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
show the reaction diagram
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
show the reaction diagram
L-ornithine + O2 + H2O
(2S)-2-hydroxy-5-oxopentanoate + NH3 + H2O2
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine tryptophylquinone
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lysyl-tyrosyl quinone
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-aminopropanenitrile
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0.2 mM, 91% inhibition
6-aminocaproic acid
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0.2 mM, 72% inhibition
aminoguanidine
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cadaverine
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0.2 mM, 74% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018 - 0.02491
L-lysine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36.9
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in 15 mM potassium phosphate buffer (pH 7.0), at 25C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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at pH 7, the incubation of the samples at temperatures below inactivation produces a characteristic and reliable increase in activity. This activation is already noticeable at 50C for treatments longer than 1 h
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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at pH 7, the incubation of the samples at temperatures below inactivation produces a characteristic and reliable increase in activity. This activation is already noticeable at 50C for treatments longer than 1 h
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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at death phase of growth
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1)
Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1)
Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80880
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calculated from amino acid sequence
95000
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x * 95000, SDS-PAGE, intracellular enzyme is detected as two bands of approximately 95000 and 200000 Da
97000
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x * 97000, SDS-PAGE
160000
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gel filtration, non-denaturing
200000
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x * 200000, SDS-PAGE, intracellular enzyme is detected as two bands of approximately 95000 and 200000 Da
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, crystal structure resolved to 1.98 A resolution, Protein Data Bank codes 3WEU and 3WEV
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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pH 5 and 7, 1 h, antibacterial activity is stable up to 70
75
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heat exposure at temperatures up to 75C and pH 7 cause a conformational change in the marinocine structure leading to this rare strong activation, but temperatures above 75C cause the denaturation in marinocine clearly observed in the electrophoresis experiments, with appearance of the two bands of 97000 Da and 185000Da
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
quite resistant to hydrolytic enzymes
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration on Sephacryl S-300, subsequent column chromatograpyh on DEAE-Toyopearl
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High Q strong anion-exchange chromatography
Mono Q column chromatography
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Ni-NTA agarose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli S17-1 (lambdapir) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme activity is induced at the posttranscriptional level by L-lysine as well as by L-arginine and meso-2,6-diaminopimelic acid
the expression of the lysine-epsilon oxidase activity requires functional copies of both genes lodA and lodB since mutants lacking either lodA or lodB do not show any enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine