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Information on EC 1.5.3.4 - N6-methyl-lysine oxidase
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1.5.3.4 N6-methyl-lysine oxidaseSpecify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
epsilon-alkyllysinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
epsilon-alkyl-L-lysine:oxygen oxidoreductase
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epsilon-alkyllysinase
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epsilon-N-methyllysine demethylase
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N6-methyllysine oxidase
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oxidase, N6-methyllysine
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additional information
additional information
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same enzyme is responsible for the demethylation of epsilon-N-methyl-L-lysine and of methylated histone
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N6-methyl-L-lysine + H2O + O2 = L-lysine + formaldehyde + H2O2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
demethylation
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oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
N6-methyl-L-lysine:oxygen oxidoreductase (demethylating)
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CAS REGISTRY NUMBER
COMMENTARY
37256-28-3
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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
6-(methylamino)-2-oxohexanoic acid + H2O + O2
6-amino-2-oxohexanoic acid + formaldehyde + H2O2
epsilon-N-methyl groups in protein-bound methyllysine residues + O2 + H2O
demethylated lysine residues + formaldehyde + H2O2
N6-ethyl-L-lysine + H2O + O2
L-lysine + acetaldehyde + H2O2
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about 50% of the activity with N6-methyl-L-lysine
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?
N6-methyl-D-lysine + H2O + O2
D-lysine + formaldehyde + H2O2
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11% of the activity with epsilon-N-methyl-L-lysine
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?
N6-methyl-L-lysyl-histone + O2 + H2O
histone + formaldehyde + H2O2
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?
6-(methylamino)-2-oxohexanoic acid + H2O + O2
6-amino-2-oxohexanoic acid + formaldehyde + H2O2
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?
6-(methylamino)-2-oxohexanoic acid + H2O + O2
6-amino-2-oxohexanoic acid + formaldehyde + H2O2
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15% of the activity with N6-methyl-L-lysine
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?
6-(methylamino)-2-oxohexanoic acid + H2O + O2
6-amino-2-oxohexanoic acid + formaldehyde + H2O2
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free alpha-amino group is not required for susceptibility
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?
epsilon-N-methyl groups in protein-bound methyllysine residues + O2 + H2O
demethylated lysine residues + formaldehyde + H2O2
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methylation of lysyl residues is catalyzed by S-adenosylmethionine:protein (lysine) N-methyltransferase
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ir
epsilon-N-methyl groups in protein-bound methyllysine residues + O2 + H2O
demethylated lysine residues + formaldehyde + H2O2
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protein: e.g. histones
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ir
N6,N6-dimethyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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?
N6,N6-dimethyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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46% of the activity with N6-methyl-L-lysine, it may be oxidized by a different enzyme
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?
N6,N6-dimethyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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enzyme consumes per molecule N6,N6-dimethyl-L-lysine one molecule of oxygen
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?
N6-methyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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?
N6-methyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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?
N6-methyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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?
N6-methyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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ir
N6-methyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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reaction in reverse direction, i.e. methylation of L-lysine, is probably catalyzed by protein methylase III
equimolar amounts of L-lysine and formaldehyde
ir
N6-methyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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highest enzyme activity
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?
N6-methyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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enzyme consumes per mol N6-methyl-L-lysine half a mol of oxygen
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?
N6-methyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
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enzyme consumes per mol N6-methyl-L-lysine half a mol of oxygen
equimolar amounts of L-lysine and formaldehyde
ir
additional information
?
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demethylation involves an electron transport system: FAD is the physiological electron acceptor, phenazine methosulfate as artificial and more efficient electron acceptor than FAD, final electron acceptor is oxygen or 2,6-dichlorophenolindophenol
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?
additional information
?
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not: several acyl derivatives, alpha-N-methyl-L-lysine
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?
additional information
?
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activity restricted to epsilon-N-alkyllysine derivatives
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?
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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
epsilon-N-methyl groups in protein-bound methyllysine residues + O2 + H2O
demethylated lysine residues + formaldehyde + H2O2
epsilon-N-methyl groups in protein-bound methyllysine residues + O2 + H2O
demethylated lysine residues + formaldehyde + H2O2
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methylation of lysyl residues is catalyzed by S-adenosylmethionine:protein (lysine) N-methyltransferase
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ir
epsilon-N-methyl groups in protein-bound methyllysine residues + O2 + H2O
demethylated lysine residues + formaldehyde + H2O2
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protein: e.g. histones
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ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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physiological electron acceptor, not required with whole homogenate, but required for partially purified enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
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inhibits activity in crude homogenate, but stimulates enzyme in prepared mitochondrial fraction
2,6-dichlorophenolindophenol
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inhibitory toward the partially purified enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
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stimulates enzyme in prepared mitochondrial fraction, but inhibits activity in crude homogenate
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0283
additional information
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values in dependence of different incubation mixtures
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.8
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pH 6: about 10% of activity maximum, pH 7.8: about 15% of activity maximum
6 - 8
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pH 6: about 35% of activity maximum, pH 8: about 50% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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low enzyme activity in young rat, increases to the adult level, highest level of demethylation activity
brenda
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low enzyme activity in young rat, increases to the adult level, after kidney next highest level of demethylation activity
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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60% of the activity in rat kidney is present in the mitochondrial fraction
brenda
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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). Q1LRF8_CUPMC
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
169
0
18576
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme is resistant to heat, far more stable in presence of substrates
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10% glycerol protects enzyme from inactivation during Sephadex G-200 column chromatography
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Paik, W.K.; Kim, S.
epsilon-Alkyllysinase. New assay method, purification, and biological significance
Arch. Biochem. Biophys.
165
369-378
1974
Rattus norvegicus
brenda
Kim, S.; Benoiton, L.; Woon Ki Paik
Epsilon-alkyllysinase. Purification and properties of the enzyme
J. Biol. Chem.
239
3790-3796
1964
Canis lupus familiaris, Cavia porcellus, Columba sp., Felis catus, Gallus gallus, Mesocricetus auratus, Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
brenda
Paik, W.K.; DiMaria, P.
Enzymatic methylation and demethylation of protein-bound lysine residues
Methods Enzymol.
106
274-287
1984
Rattus norvegicus
brenda
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