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Information on EC 1.4.3.2 - L-amino-acid oxidase and Organism(s) Ophiophagus hannah and UniProt Accession P81383
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1.4.3.2 L-amino-acid oxidaseIUBMB Comments
A flavoprotein (FAD).
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- 1.4.3.2
- atrial
- appendage
-
occlusion
- fibrillation
- stroke
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anticoagulation
-
bleeding
- venom
- snake
-
percutaneous
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thromboembolic
-
amplatzer
-
watchman
-
transesophageal
-
echocardiography
-
amulet
- thrombus
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has-bled
- embolism
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cha2ds2-vasc
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contraindication
-
periprocedural
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non-valvular
-
device-related
- medicine
- tamponade
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transcatheter
- bothrops
- crotalus
-
noacs
-
procedure-related
- rhodostoma
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post-procedural
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lariat
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chads2
- calloselasma
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fluoroscopy
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transseptal
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pre-procedural
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cardioembolic
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non-vitamin
- antivenoms
- atrox
- hare
- agkistrodon
- analysis
- moojeni
- synthesis
- drug development
The taxonomic range for the selected organisms is: Ophiophagus hannah
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
laao, il4i1, l-amino-acid oxidase, l-aao, escapin, head kidney and gill, dolabellanin, l-phenylalanine oxidase, akbu-laao, m-lao, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aromatic L-amino acid oxidase
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-
-
-
L-amino acid oxidase
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-
-
-
L-amino acid:O2 oxidoreductase
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-
-
-
L-aminooxidase
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-
-
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LAAO
LAO
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-
-
-
ophio-amino-acid oxidase
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-
-
-
LAAO
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidative deamination
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Alanine, aspartate and glutamate metabolism, Biosynthesis of secondary metabolites, Cysteine and methionine metabolism, Isoquinoline alkaloid biosynthesis, Phenylalanine metabolism, Phenylalanine, tyrosine and tryptophan biosynthesis, Tryptophan metabolism, Tyrosine metabolism, Valine, leucine and isoleucine degradation
SYSTEMATIC NAME
IUBMB Comments
L-amino-acid:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY
9000-89-9
-
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
L-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
-
-
-
?
L-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
L-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
L-lysine + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
-
-
-
?
L-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
-
-
-
?
additional information
?
-
-
cytotoxic to different cell lines, resulting in loss of ability in attachment and inhibition of cell proliferation
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
venom LAAO is very effective in inhibiting the two Gram-positive bacteria Staphylococcus aureus and Staphylococcus epidermidis with MICs of 0.000006 mM and 0.000012 mM, respetively. LAAO is only moderately effective against three Gram-negative bacteria tested, Pseudomonas aeruginosa, Klebsiella pneumoniae, and Escherichia coli, overview. Binding to bacteria is important for the potent antibacterial activity of the enzyme
physiological function
-
the enzyme exhibits cytotoxic, bactericidal, leishmanicidal, and antiviral effects
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). OXLA_OPHHA
491
0
55977
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53686
1 * 64000, SDS-PAGE under non-reducing conditions, 1 * 67000, SDS-PAGE under reducing conditions, 1 * 53686, sequence analysis
64000
1 * 64000, SDS-PAGE under non-reducing conditions, 1 * 67000, SDS-PAGE under reducing conditions, 1 * 53686, sequence analysis
67000
1 * 64000, SDS-PAGE under non-reducing conditions, 1 * 67000, SDS-PAGE under reducing conditions, 1 * 53686, sequence analysis
135000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
1 * 64000, SDS-PAGE under non-reducing conditions, 1 * 67000, SDS-PAGE under reducing conditions, 1 * 53686, sequence analysis
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
25°C, 5 min, 47% loss of activity, complete loss of activity after 30 min
391772
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing, quick freezing with dry ice/acetone mixture and storage at -15°C for 60 h, enzyme is stable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration, ion-exchange and heparin chromatography, to homogeneity
Sephadex G-100 gel filtration, Q column chromatography, and HiTrap heparin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
LAAO does not induce platelet aggregation, but it has potent inhibitory activity on platelet aggregation induced by ADP and U46619. It shows no effect on platelet aggregation induced by thrombin, mucetin, ristocetin and stejnulxin
medicine
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coadministering adipose-derived mesenchymal stromal cells and Ophiophagus hannah L-amino acid oxidase in a mouse model of methicillin-resistant Staphylococcus aureus-infected wounds results in reduction of MRSA load by one order of magnitude to the approximate range of 6 log10 colony-forming units compared to untreated controls (7.3 log10 CFU). Similar wound healing and improvements in histological parameters are observed between the two groups. Coadministration of adipose-derived mesenchymal stromal cells and L-amino acid oxidase reduces bacterial burden by approximately two orders of magnitude to 5.1 log10 CFU and leads to a significant enhancement in the wound healing process
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tan, N.H.; Saifuddin, M.N.
Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom
Biochem. Int.
19
937-944
1989
Ophiophagus hannah
Du, X.Y.; Clemetson, K.J.
Snake venom L-amino acid oxidases
Toxicon
40
659-665
2002
Agkistrodon contortrix laticinctus, Gloydius blomhoffii, Calloselasma rhodostoma, Bothrops moojeni, Crotalus adamanteus, Crotalus atrox, Eristicophis macmahoni, Ophiophagus hannah, snake, Protobothrops flavoviridis, Protobothrops mucrosquamatus, Naja kaouthia, Pseudechis australis
Li, Z.Y.; Yu, T.F.; Lian, C.Y.
Purification and characterization of L-amino acid oxidase from king cobra (Ophiophagus hannah) venom and its effects on human platelet aggregation
Toxicon
32
1349-1358
1994
Ophiophagus hannah
Ahn, M.Y.; Lee, B.M.; Kim, Y.S.
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)
Int. J. Biochem. Cell Biol.
29
911-919
1997
Ophiophagus hannah
Jin, Y.; Lee, W.H.; Zeng, L.; Zhang, Y.
Molecular characterization of L-amino acid oxidase from king cobra venom
Toxicon
50
479-489
2007
Bungarus fasciatus (A8QL52), Bungarus fasciatus, Bungarus multicinctus (A8QL51), Bungarus multicinctus, Naja atra (A8QL58), Naja atra, Ophiophagus hannah (P81383), Ophiophagus hannah
Lee, M.L.; Tan, N.H.; Fung, S.Y.; Sekaran, S.D.
Antibacterial action of a heat-stable form of l-amino acid oxidase isolated from king cobra (Ophiophagus hannah) venom
Comp. Biochem. Physiol. C
153
237-242
2010
Ophiophagus hannah
Izidoro, L.F.; Sobrinho, J.C.; Mendes, M.M.; Costa, T.R.; Grabner, A.N.; Rodrigues, V.M.; da Silva, S.L.; Zanchi, F.B.; Zuliani, J.P.; Fernandes, C.F.; Calderon, L.A.; Stabeli, R.G.; Soares, A.M.
Snake venom L-amino acid oxidases trends in pharmacology and biochemistry
BioMed Res. Int.
2014
196754
2014
Deinagkistrodon acutus, Calloselasma rhodostoma, Bothrops atrox, Bothrops jararaca, Bothrops marajoensis, Bungarus fasciatus, Lachesis muta, Naja oxiana, Ophiophagus hannah, Daboia russelii, Macrovipera lebetina, Bothrops alternatus, Bothrops pirajai, Gloydius ussuriensis, Bungarus caeruleus, Aplysia punctata, Bothrops insularis, Bothrops pauloensis, Crotalus durissus cumanensis, Bothrops leucurus, Vipera berus berus
Mot, Y.Y.; Othman, I.; Sharifah, S.H.
Synergistic antibacterial effect of co-administering adipose-derived mesenchymal stromal cells and Ophiophagus hannah L-amino acid oxidase in a mouse model of methicillin-resistant Staphylococcus aureus-infected wounds
Stem Cell Res. Ther.
8
005
2017
Ophiophagus hannah
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