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Information on EC 1.4.3.20 - L-lysine 6-oxidase
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EC Tree
1.4.3.20 L-lysine 6-oxidaseIUBMB Comments
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 .
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Word Map
- 1.4.3.20
- marinomonas
- mediterranea
-
melanogenic
-
broad-spectrum
- oxidases
- tunicata
-
pseudoalteromonas
- flavoproteins
-
draft
- quinone
-
multicopper
- melanin
- rheinheimera
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
marinocine, l-lysine epsilon-oxidase, lysine-epsilon-oxidase, lysine-epsilon oxidase, marinocine antimicrobial protein, l-lysine-epsilon-oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
epsilon-lysine oxidase
L-lysine epsilon-oxidase
L-lysine-epsilon-oxidase
Lod
LodA
lysine-epsilon oxidase
lysine-epsilon-oxidase
marinocine
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-lysine + O2 + H2O = (S)-2-amino-6-oxohexanoate + H2O2 + NH3
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].
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CAS REGISTRY NUMBER
COMMENTARY
860791-20-4
-
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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
alpha-N-acetyl-L-lysine + H2O
N-acetyl-6-oxo-L-norleucine + H2O2 + NH3
-
91.9% of the activity with L-lysine
-
-
?
L-ornithine + O2 + H2O
5-oxo-L-norvaline + H2O2 + NH3
-
15.1% of activity with L-lysine
-
-
?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
-
-
?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
-
-
-
?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
-
-
?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
100% activity
-
-
?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
-
-
?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
100% activity
-
-
?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
-
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
100% activity
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
100% activity
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
the enzyme shows antibacterial activity
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
high stereospecificity for L-lysine
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
-
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
100% activity
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
100% activity
-
-
?
L-lysine + O2 + H2O2
2-aminoadipate 6-semialdehyde + NH3 + H2O2
-
-
-
-
?
L-lysine + O2 + H2O2
2-aminoadipate 6-semialdehyde + NH3 + H2O2
-
-
-
-
?
L-lysine + O2 + H2O2
2-aminoadipate 6-semialdehyde + NH3 + H2O2
-
-
-
-
?
L-lysine + O2 + H2O2
2-aminoadipate 6-semialdehyde + NH3 + H2O2
-
-
-
-
?
L-ornithine + O2 + 2 H2O
(2S)-2-hydroxy-5-oxopentanoate + 2 NH3 + H2O2
-
3.2% activity compared to L-lysine
-
-
?
L-ornithine + O2 + 2 H2O
(2S)-2-hydroxy-5-oxopentanoate + 2 NH3 + H2O2
-
3.2% activity compared to L-lysine
-
-
?
L-ornithine + O2 + H2O
? + H2O2 + NH3
15.1% activity compared to L-lysine
-
-
?
L-ornithine + O2 + H2O
? + H2O2 + NH3
15.1% activity compared to L-lysine
-
-
?
additional information
?
-
-
no activity with morpholinepropanesulfonic acid, trehalose, and tricine
-
-
?
additional information
?
-
-
no activity with morpholinepropanesulfonic acid, trehalose, and tricine
-
-
?
additional information
?
-
-
the enzyme shows antibacterial activity
-
-
?
additional information
?
-
-
no activity with morpholinepropanesulfonic acid, trehalose, and tricine
-
-
?
additional information
?
-
no activity with L-arginine and meso-2,6-diaminopimelic acid
-
-
?
additional information
?
-
-
no activity with L-arginine and meso-2,6-diaminopimelic acid
-
-
?
additional information
?
-
-
no activity with L-phenylalanine, L-arginine, L-tyrosine, L-histidine, and L-leucine
-
-
?
additional information
?
-
alternative electron acceptors like 2,6-dichloroinophenol, ferricyanide, NAD+, amicyanin or cytochrome C-550 cannot effectively substitute for O2 in the reaction
-
-
?
additional information
?
-
no activity with L-arginine and meso-2,6-diaminopimelic acid
-
-
?
additional information
?
-
alternative electron acceptors like 2,6-dichloroinophenol, ferricyanide, NAD+, amicyanin or cytochrome C-550 cannot effectively substitute for O2 in the reaction
-
-
?
additional information
?
-
-
no activity with L-phenylalanine, L-arginine, L-tyrosine, L-histidine, and L-leucine
-
-
?
additional information
?
-
-
no activity with morpholinepropanesulfonic acid, trehalose, and tricine
-
-
?
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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-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
-
-
?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
-
-
-
?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
-
-
?
L-lysine + O2 + H2O
(S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
-
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
100% activity
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
100% activity
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
the enzyme shows antibacterial activity
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
-
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
100% activity
-
-
?
L-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
-
100% activity
-
-
?
L-ornithine + O2 + 2 H2O
(2S)-2-hydroxy-5-oxopentanoate + 2 NH3 + H2O2
-
3.2% activity compared to L-lysine
-
-
?
L-ornithine + O2 + 2 H2O
(2S)-2-hydroxy-5-oxopentanoate + 2 NH3 + H2O2
-
3.2% activity compared to L-lysine
-
-
?
additional information
?
-
no activity with L-arginine and meso-2,6-diaminopimelic acid
-
-
?
additional information
?
-
-
no activity with L-arginine and meso-2,6-diaminopimelic acid
-
-
?
additional information
?
-
-
no activity with L-phenylalanine, L-arginine, L-tyrosine, L-histidine, and L-leucine
-
-
?
additional information
?
-
no activity with L-arginine and meso-2,6-diaminopimelic acid
-
-
?
additional information
?
-
-
no activity with L-phenylalanine, L-arginine, L-tyrosine, L-histidine, and L-leucine
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
highest enzyme activity is obtained by incubation with 1.6 M NaCl, which is approximately 1.5fold higher than that of the untreated enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0018
L-lysine
-
in 15 mM potassium phosphate buffer (pH 7.0), at 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
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
additional information
-
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 50°C for treatments longer than 1 h
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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 50°C for treatments longer than 1 h
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LODA_MARM1
Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1)
726
0
80880
Swiss-Prot
-
A0A6P2UE33_BURL3
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
687
0
75304
TrEMBL
-
A0A6P3CBE3_BURL3
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
666
0
73771
TrEMBL
-
A0A7G1Q7N6_9GAMM
457
0
52471
TrEMBL
-
A0A2R8BGL2_9RHOB
621
0
67978
TrEMBL
-
A0A3B0XIW5_9ZZZZ
483
0
53044
TrEMBL
other Location (Reliability: 3)
A0A7G1Q848_9GAMM
229
0
25328
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
200000
-
x * 200000, SDS-PAGE, intracellular enzyme is detected as two bands of approximately 95000 and 200000 Da
95000
-
x * 95000, SDS-PAGE, intracellular enzyme is detected as two bands of approximately 95000 and 200000 Da
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
?
-
two major bands of 97000 Da and 185000 Da appear in denaturing SDS-PAGE
?
-
x * 200000, SDS-PAGE, intracellular enzyme is detected as two bands of approximately 95000 and 200000 Da
?
-
x * 95000, SDS-PAGE, intracellular enzyme is detected as two bands of approximately 95000 and 200000 Da
?
-
x * 200000, SDS-PAGE, intracellular enzyme is detected as two bands of approximately 95000 and 200000 Da
-
?
-
x * 95000, SDS-PAGE, intracellular enzyme is detected as two bands of approximately 95000 and 200000 Da
-
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C448A
the mutation causes large increases in the Km values for L-lysine
C448D
the mutation causes large increases in the Km values for L-lysine
K530A
the variant exhibits diminished levels of cysteine tryptophylquinone but significantly increased kcat value. The mutation causes large increases in the Km values for L-lysine
K530R
the variant exhibits diminished levels of cysteine tryptophylquinone but significantly increased kcat value. The mutation causes large increases in the Km values for L-lysine
Y211A
the variant the highest level of cysteine tryptophylquinone but exhibits no activity
Y211E
the variant the highest level of cysteine tryptophylquinone but exhibits no activity
Y211F
the mutant has reduced levels of cysteine tryptophylquinone but near normal levels of kcat. The mutation causes large increases in the Km values for L-lysine
C448A
-
the mutation causes large increases in the Km values for L-lysine
-
K530A
-
the variant exhibits diminished levels of cysteine tryptophylquinone but significantly increased kcat value. The mutation causes large increases in the Km values for L-lysine
-
K530R
-
the variant exhibits diminished levels of cysteine tryptophylquinone but significantly increased kcat value. The mutation causes large increases in the Km values for L-lysine
-
Y211A
-
the variant the highest level of cysteine tryptophylquinone but exhibits no activity
-
Y211F
-
the mutant has reduced levels of cysteine tryptophylquinone but near normal levels of kcat. The mutation causes large increases in the Km values for L-lysine
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
-
heat exposure at temperatures up to 75°C and pH 7 cause a conformational change in the marinocine structure leading to this rare strong activation, but temperatures above 75°C cause the denaturation in marinocine clearly observed in the electrophoresis experiments, with appearance of the two bands of 97000 Da and 185000Da
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration on Sephacryl S-300, subsequent column chromatograpyh on DEAE-Toyopearl
High Q strong anion-exchange chromatography
Ni-NTA column chromatography and DEAE cellulose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
enzyme activity is induced at the posttranscriptional level by L-lysine as well as by L-arginine and meso-2,6-diaminopimelic acid
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
-
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
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
L-lysine epsilon-oxidase can be used for diagnosis based on plasma L-lysine concentration
medicine
-
L-lysine epsilon-oxidase can be used for diagnosis based on plasma L-lysine concentration
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lucas-Elio, P.; Hernandez, P.; Sanchez-Amat, A.; Solano, F.
Purification and partial characterization of marinocine, a new broad-spectrum antibacterial protein produced by Marinomonas mediterranea
Biochim. Biophys. Acta
1721
193-203
2005
Marinomonas mediterranea
brenda
Gomez, D.; Lucas-Elio, P.; Sanchez-Amat, A.; Solano, F.
A novel type of lysine oxidase: L-lysine-epsilon-oxidase
Biochim. Biophys. Acta
247; 1764
1577-1585
2006
Marinomonas mediterranea
brenda
Lucas-Elio, P.; Gomez, D.; Solano, F.; Sanchez-Amat, A.
The antimicrobial activity of marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity
J. Bacteriol.
188
2493-2501
2006
Marinomonas mediterranea (F2JXJ3), Marinomonas mediterranea
brenda
Mai-Prochnow, A.; Lucas-Elio, P.; Egan, S.; Thomas, T.; Webb, J.S.; Sanchez-Amat, A.; Kjelleberg, S.
Hydrogen peroxide linked to lysine oxidase activity facilitates biofilm differentiation and dispersal in several gram-negative bacteria
J. Bacteriol.
190
5493-5501
2008
Caulobacter vibrioides, Chromobacterium violaceum, Marinomonas mediterranea, Pseudoalteromonas tunicata
brenda
Okazaki, S.; Nakano, S.; Matsui, D.; Akaji, S.; Inagaki, K
Asano, Y.: X-Ray crystallographic evidence for the presence of the cysteine tryptophylquinone cofactor in L-lysine {varepsilon}-oxidase from Marinomonas mediterranea
J. Biochem.
154
233-236
2013
Marinomonas mediterranea (F2JXJ3), Marinomonas mediterranea NBRC 103028 (F2JXJ3)
brenda
Matsuda, M.; Asano, Y.
Determination of plasma and serum L-lysine using L-lysine epsilon-oxidase from Marinomonas mediterranea NBRC 103028T
Anal. Biochem.
406
19-23
2010
Marinomonas mediterranea, Marinomonas mediterranea NBRC 103028T
brenda
Molina-Quintero, L.R.; Lucas-Elio, P.; Sanchez-Amat, A.
Regulation of the Marinomonas mediterranea antimicrobial protein lysine oxidase by L-lysine and the sensor histidine kinase PpoS
Appl. Environ. Microbiol.
76
6141-6149
2010
Marinomonas mediterranea (F2JXJ3), Marinomonas mediterranea, Marinomonas mediterranea MMB-1 (F2JXJ3)
brenda
Gomez, D.; Lucas-Elio, P.; Solano, F.; Sanchez-Amat, A.
Both genes in the Marinomonas mediterranea lodAB operon are required for the expression of the antimicrobial protein lysine oxidase
Mol. Microbiol.
75
462-473
2010
Marinomonas mediterranea, Marinomonas mediterranea MMB-1
brenda
Sehanobish, E.; Chacon-Verdu, M.D.; Sanchez-Amat, A.; Davidson, V.L.
Roles of active site residues in LodA, a cysteine tryptophylquinone dependent epsilon-lysine oxidase
Arch. Biochem. Biophys.
579
26-32
2015
Marinomonas mediterranea (F2JXJ3), Marinomonas mediterranea NBRC 103028 (F2JXJ3)
brenda
Chacon-Verdu, M.D.; Campillo-Brocal, J.C.; Lucas-Elio, P.; Davidson, V.L.; Sanchez-Amat, A.
Characterization of recombinant biosynthetic precursors of the cysteine tryptophylquinone cofactors of l-lysine-epsilon-oxidase and glycine oxidase from Marinomonas mediterranea
Biochim. Biophys. Acta
1854
1123-1131
2015
Marinomonas mediterranea (F2JXJ3), Marinomonas mediterranea, Marinomonas mediterranea NBRC 103028 (F2JXJ3)
brenda
Matsui, D.; Asano, Y.
Heterologous production of L-lysine epsilon-oxidase by directed evolution using a fusion reporter method
Biosci. Biotechnol. Biochem.
79
1473-1480
2015
Marinomonas mediterranea (F2JXJ3), Marinomonas mediterranea NBRC 103028 (F2JXJ3)
brenda
Sehanobish, E.; Shin, S.; Sanchez-Amat, A.; Davidson, V.L.
Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidase
FEBS Lett.
588
752-756
2014
Marinomonas mediterranea (F2JXJ3), Marinomonas mediterranea NBRC 103028 (F2JXJ3)
brenda
Okazaki, S.; Nakano, S.; Matsui, D.; Akaji, S.; Inagaki, K.; Asano, Y.
X-ray crystallographic evidence for the presence of the cysteine tryptophylquinone cofactor in L-lysine alpha-oxidase from Marinomonas mediterranea
J. Biochem.
154
233-236
2013
Marinomonas mediterranea (F2JXJ3), Marinomonas mediterranea NBRC 103028 (F2JXJ3)
brenda
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