Information on EC 1.4.3.14 - L-lysine oxidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.4.3.14
-
RECOMMENDED NAME
GeneOntology No.
L-lysine oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine degradation VII
-
-
Lysine degradation
-
-
Metabolic pathways
-
-
Tropane, piperidine and pyridine alkaloid biosynthesis
-
-
lysine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-lysine:oxygen 2-oxidoreductase (deaminating)
Also acts, more slowly, on L-ornithine, L-phenylalanine, L-arginine and L-histidine.
CAS REGISTRY NUMBER
COMMENTARY hide
70132-14-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fasted
-
-
Manually annotated by BRENDA team
no activity in Aspergillus
-
-
-
Manually annotated by BRENDA team
no activity in Fusarium
-
-
-
Manually annotated by BRENDA team
no activity in Mucor
-
-
-
Manually annotated by BRENDA team
no activity in Penicillium
-
-
-
Manually annotated by BRENDA team
no activity in Rhizopus
-
-
-
Manually annotated by BRENDA team
Phylogenetic tree based on 16S rRNA gene sequences, overview
-
-
Manually annotated by BRENDA team
Phylogenetic tree based on 16S rRNA gene sequences, overview
-
-
Manually annotated by BRENDA team
Trichoderma cf. aureoviride
-
-
-
Manually annotated by BRENDA team
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
-
-
Manually annotated by BRENDA team
wheat bran culture of Ts75-2
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginine + O2 + H2O
5-carbamidamido-2-oxopentanoate + NH3 + H2O2
show the reaction diagram
L-arginine + O2 + H2O
5-guanidino-2-oxopentanoate + NH3 + H2O2
show the reaction diagram
L-histidine + O2 + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
show the reaction diagram
L-leucine + O2 + H2O
4-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
show the reaction diagram
L-lysine + semicarbazide + ?
4-methyl-2-oxopentanoate + ?
show the reaction diagram
-
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoate + NH3 + H2O2
show the reaction diagram
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram
L-phenylalanine + O2 + H2O
phenylpyruvate + NH3 + H2O2
show the reaction diagram
L-tyrosine + O2 + H2O
3-(4-hydroxyphenyl)pyruvate + NH3 + 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
L-arginine + O2 + H2O
5-carbamidamido-2-oxopentanoate + NH3 + H2O2
show the reaction diagram
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
show the reaction diagram
L-ornithine + O2 + H2O
5-amino-2-oxopentanoate + NH3 + H2O2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-diaminobutane
-
20% inhibition
1,5-Diaminopentane
-
24% inhibition
1,6-diaminohexane
-
43% inhibition
6-aminocaproic acid
-
30% inhibition
p-chloromercuribenzoate
-
-
Semicarbazide
-
weak competitive, reversible inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenine
-
increases enzyme production
glycine
-
increases enzyme production
L-glutamine
-
increases enzyme production
L-histidine
-
increases enzyme production
NaNO3
-
stimulation of enzyme production
NH4NO3
-
stimulation of enzyme production
purine
-
increases enzyme production
additional information
-
no significant effect of sugars and vitamines
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.46 - 0.68
L-arginine
0.026 - 0.4
L-lysine
0.044 - 0.75
L-ornithine
14 - 25.5
L-phenylalanine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
56
Semicarbazide
-
500 mM, 10 mM L-lysine, 3% inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.29
Trichoderma cf. aureoviride
-
culture liquid, at pH 8.0 and 25C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.8
-
membrane-immobilized enzyme
7 - 7.8
-
membrane-immobilized enzyme
7 - 8
-
Tris- and phosphate buffer
7.4
-
assay at
7.4 - 9.2
-
for L-lysine, reaction rate declines markedly below pH 7.0
7.8 - 8.2
Trichoderma cf. aureoviride
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
-
enzyme activity does not fall below 60%, at pH 3.0 the activity is still 30%
6 - 9.5
Trichoderma cf. aureoviride
-
about 50% activity at pH 6.0, about 80% activity at pH 7.0, 100% activity at pH 8.0, about 85% activity at pH 9.0, about 78% activity at pH 9.5
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
-
82% relative activity at 30C, 103% at 50C and 58C at 70C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.68
-
isoelectric focusing
4.35
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
-
2 * 55000, SDS-PAGE
56000
-
2 * 56000, SDS-PAGE
71000
-
native PAGE
110000
-
gel filtration
112000 - 119000
-
gel filtration, sedimentation equilibrium centrifugation
115000 - 116000
Trichoderma cf. aureoviride
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
stable at extreme pH values
391751
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
30 min, 0.1 M potassium phosphate buffer, reaction rate is between 85% at pH 3.0 and 90% at pH 11.0
45
-
stable for 30 min in the pH range from pH 5.0 or pH 7.0 to pH 10.0
55
-
0.1 M potassium phosphate buffer, pH 7.4, 30 min, 100% of original activity
60
-
0.1 M potassium phosphate buffer, pH 7.4, 30 min, 92% of original activity
65
-
0.1 M potassium phosphate buffer, pH 7.4, 30 min, 42% of original activity
75
-
30 min, complete loss of activity
additional information
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
Ethanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.05 M potassium phosphate buffer of Tris-HCl buffer pH 8.0, at least 14 months stable without any loss of activity
-
-20C, 0.1 M potassium phosphate buffer, pH 7.4, at least 3 months, with little loss of activity
-
-4C, practically no loss of activity over several months
4-37C, 0.05 M potassium phosphate buffer of Tris-HCl buffer pH 8.0, stable for 4-5 days
-
4C, activity preserved
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetone precipitation, ion-exchange
-
ammonium sulfate precipitation
-
ammonium sulfate precipitation, ion-exchange
-
ammonium sulfate precipitation, ion-exchange, gel-filtration
-
gel-filtration
-
lectin affinity column chromatography, anion-exchange HPLC, and hydroxyapatite column chromatography
octyl Sepharose column chromatography, DEAE ToyoPearl column chromatography, and gel filtration
Trichoderma cf. aureoviride
-
rapid loss of activity during isolation and purification
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sequence comparisons, the enzyme shows 100% sequence identitiy with gene alpP of Pseudoalteromonas tunicata D2 encoding an autolytic and antibacterial protein
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced in submerged culture on wheat bran under salt stress conditions (6% (w/v) NaCl)
Trichoderma cf. aureoviride
-
enzyme expression is induced in submerged culture on wheat bran under salt stress conditions (6% (w/v) NaCl); the synthesis of extracellular enzyme is induced during submerged cultivation on wheat bran under salt stress (maximum after 5-7 days at 6% (w/v) NaCl)
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
-
the synthesis of extracellular enzyme is induced during submerged cultivation on wheat bran under salt stress (maximum after 5-7 days at 6% (w/v) NaCl)
Trichoderma cf. aureoviride
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
nutrition