Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.4.3.20 - L-lysine 6-oxidase and Organism(s) Marinomonas mediterranea and UniProt Accession F2JXJ3

for references in articles please use BRENDA:EC1.4.3.20
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.20 L-lysine 6-oxidase
IUBMB 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 .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Marinomonas mediterranea
UNIPROT: F2JXJ3
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Marinomonas mediterranea
The enzyme appears in selected viruses and cellular organisms
Synonyms
marinocine, l-lysine epsilon-oxidase, lysine-epsilon oxidase, lysine-epsilon-oxidase, l-lysine-epsilon-oxidase, marinocine antimicrobial protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epsilon-lysine oxidase
-
L-lysine epsilon-oxidase
-
L-lysine-epsilon-oxidase
-
lysine-epsilon-oxidase
-
marinocine antimicrobial protein
-
L-lysine epsilon-oxidase
-
-
L-lysine-epsilon oxidase
-
-
lysine-epsilon oxidase
-
-
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
-
SUBSTRATE
PRODUCT                       
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
? + H2O2 + NH3
show the reaction diagram
15.1% activity compared to L-lysine
-
-
?
alpha-N-acetyl-L-lysine + H2O
N-acetyl-6-oxo-L-norleucine + H2O2 + NH3
show the reaction diagram
-
91.9% of the activity with L-lysine
-
-
?
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 + 2 H2O
(2S)-2-hydroxy-5-oxopentanoate + 2 NH3 + H2O2
show the reaction diagram
-
3.2% activity compared to L-lysine
-
-
?
L-ornithine + O2 + H2O
5-oxo-L-norvaline + H2O2 + NH3
show the reaction diagram
-
15.1% of activity with L-lysine
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
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-lysine + O2 + H2O
2-aminoadipate 6-semialdehyde + H2O2 + NH3
show the reaction diagram
L-ornithine + O2 + 2 H2O
(2S)-2-hydroxy-5-oxopentanoate + 2 NH3 + H2O2
show the reaction diagram
-
3.2% activity compared to L-lysine
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine tryptophylquinone
lysyl-tyrosyl quinone
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-aminopropanenitrile
-
0.2 mM, 91% inhibition
6-aminocaproic acid
-
0.2 mM, 72% inhibition
aminoguanidine
-
-
cadaverine
-
0.2 mM, 74% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018 - 0.142
L-lysine
0.0372 - 1.043
O2
0.0018
L-lysine
-
in 15 mM potassium phosphate buffer (pH 7.0), at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 1.2
L-lysine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36.9
-
in 15 mM potassium phosphate buffer (pH 7.0), at 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
at death phase of growth
Manually annotated by BRENDA team
additional information
-
from blood plasma and serum
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
gel filtration
80880
calculated from amino acid sequence
160000
-
gel filtration, non-denaturing
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
97000
-
x * 97000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 80880, dimeric in solution
homodimer
2 * 97000, SDS-PAGE
tetramer
4 * 80880, tetrameric in crystal state
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with L-lysine
sitting drop vapor diffusion method, crystal structure resolved to 1.98 A resolution, Protein Data Bank codes 3WEU and 3WEV
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
pH 5 and 7, 1 h, antibacterial activity is stable up to 70
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
quite resistant to hydrolytic enzymes
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration on Sephacryl S-300, subsequent column chromatograpyh on DEAE-Toyopearl
Ni-NTA column chromatography and DEAE cellulose column chromatography
Ni-NTA resin column chromatography
High Q strong anion-exchange chromatography
-
Mono Q column chromatography
-
Ni-NTA agarose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta cells
expressed in Escherichia coli Rosetta(DE3) cells
expressed in Escherichia coli S17-1 (lambdapir) cells
-
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
-
L-lysine epsilon-oxidase can be used for diagnosis based on plasma L-lysine concentration
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team