Information on EC 1.5.3.4 - N6-methyl-lysine oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.3.4
-
RECOMMENDED NAME
GeneOntology No.
N6-methyl-lysine oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N6-methyl-L-lysine + H2O + O2 = L-lysine + formaldehyde + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
demethylation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
N6-methyl-L-lysine:oxygen oxidoreductase (demethylating)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37256-28-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-(methylamino)-2-oxohexanoic acid + H2O + O2
6-amino-2-oxohexanoic acid + formaldehyde + H2O2
show the reaction diagram
epsilon-N-methyl groups in protein-bound methyllysine residues + O2 + H2O
demethylated lysine residues + formaldehyde + H2O2
show the reaction diagram
N6,N6-dimethyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
show the reaction diagram
N6-ethyl-L-lysine + H2O + O2
L-lysine + acetaldehyde + H2O2
show the reaction diagram
-
about 50% of the activity with N6-methyl-L-lysine
-
-
?
N6-methyl-D-lysine + H2O + O2
D-lysine + formaldehyde + H2O2
show the reaction diagram
-
11% of the activity with epsilon-N-methyl-L-lysine
-
-
?
N6-methyl-L-lysine + O2 + H2O
L-lysine + formaldehyde + H2O2
show the reaction diagram
N6-methyl-L-lysyl-histone + O2 + H2O
histone + formaldehyde + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
epsilon-N-methyl groups in protein-bound methyllysine residues + O2 + H2O
demethylated lysine residues + formaldehyde + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6-dichlorophenolindophenol
ascorbic acid
-
moderate inhibition
FAD
-
moderate inhibition
FMN
-
moderate inhibition
KCN
-
1.3 mM, about 40% inhibition
Mn2+
-
moderate inhibition
NADH
-
moderate inhibition
phosphate
-
inhibits activity in crude homogenate, but stimulates enzyme in prepared mitochondrial fraction
additional information
-
not inhibited by semicarbazide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
-
stimulates enzyme in prepared mitochondrial fraction, but inhibits activity in crude homogenate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.87
N6,N6-dimethyl-L-lysine
-
-
5.95
N6-ethyl-L-lysine
-
-
1.05 - 1.9
N6-methyl-L-lysine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00106
-
N6-methyl-L-lysyl-histone
0.0283
0.0433
-
16fold purified enzyme
additional information
-
values in dependence of different incubation mixtures
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
partially purified enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.8
-
pH 6: about 10% of activity maximum, pH 7.8: about 15% of activity maximum
6 - 8
-
pH 6: about 35% of activity maximum, pH 8: about 50% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000 - 200000
-
gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
4 min: 70% loss of activity, 10 min: complete loss of activity
additional information
-
enzyme is resistant to heat, far more stable in presence of substrates
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10% glycerol protects enzyme from inactivation during Sephadex G-200 column chromatography
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
16fold partial purification; enzyme from kidney
-
2.78fold partial purification; enzyme from kidney
-