Information on EC 1.4.3.2 - L-amino-acid oxidase:
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EC NUMBERCOMMENTARY
1.4.3.2-

RECOMMENDED NAMEGeneOntology No.
L-amino-acid oxidaseGO:0001716

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
an L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2
show the reaction diagram		----
an L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2
show the reaction diagram		mechanismCrotalus adamanteus-389803, 391766, 391778, 391790, 391795
an L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2
show the reaction diagram		mechanismAgkistrodon piscivorus piscivorus-389803, 391766
an L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2
show the reaction diagram		mechanismRattus norvegicus-391766
an L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2
show the reaction diagram		ping-pong mechanism with binary complexes, derived from kinetic dataNeurospora crassa-391788
an L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2
show the reaction diagram		allosteric effects, activation energyCrotalus adamanteus-391800
an L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2
show the reaction diagram		mechanismSynechococcus sp.-391811
an L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2
show the reaction diagram		reaction mechanism. Catalytic amino acids are H223 in two conformations, G464 and R322Calloselasma rhodostoma-669893
an L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2
show the reaction diagram		hydride transfer mechanismRhodococcus opacus-669894

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidative deamination----
redox reaction----

PATHWAYKEGG LinkMetaCyc Link
arginine degradation VIII (arginine oxidase pathway)-ARGDEG-IV-PWY

SYSTEMATIC NAMEIUBMB Comments
L-amino-acid:oxygen oxidoreductase (deaminating)A flavoprotein (FAD).

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
ACTX-6Deinagkistrodon acutus--694317
ACTX-8Deinagkistrodon acutus--693949
Akbu-LAAOAgkistrodon blomhoffi ussuriensis--711329
APITAplysia punctataQ6T277-670963
aromatic L-amino acid oxidase----
Balt-LAAO-IBothrops alternatus--654954
Bpir-LAOO-1Bothrops pirajai--667933
DAADolabella auricularia--655316
DolabellaninDolabella auricularia--655316
escapinAplysia californica--669658, 695637, 697333
IL4I1Mus musculus--656435
Il4i1 proteinMus musculus--656435
Il4i1 proteinHomo sapiens-secreted L-phenylalanine oxidase, physiologically expressed by myeloid cells, gene expression in primary mediastinal B-cell lymphoma699933
ink toxin 1Aplysia punctataQ6T277-670963
Interleukin Four Induced Gene 1 proteinHomo sapiens-first described in the mouse, characterized in human B cells, expression is restricted to lymphoid tissues and induced by interleukin-4699933
L-AAORhodococcus opacus--651026, 653762
L-AAOAplysia californicaQ6IWZ0-695637
L-AAOPseudoalteromonas flavipulchra--711872
L-AAORhodococcus sp.--711874
L-AAOBothrops jararaca--713559
L-amino acid oxidase----
L-amino acid: O2 oxidoreductaseBothrops marajoensis--713558
L-amino acid:O2 oxidoreductase----
L-amino acid:O2 oxidoreductase (deaminating)Rhodococcus opacusQ8VPD4-651026
L-aminooxidase----
L-AoxGloeobacter violaceus PCC 7421, Nostoc punctiforme PCC 73102, Nostoc sp. PCC 7120, Synechococcus cedrorum PCC 6908--695281
L-AoxSynechococcus elongatus PCC 6301P72346-695281
L-AoxSynechococcus elongatus PCC 7942, Synechococcus sp. CC9605, Synechococcus sp. WH 5701, Synechococcus sp. WH 7805, Synechocystis sp. PCC 6803, Trichodesmium erythraeum IMS101--695281
L-phenylalanine oxidaseHomo sapiens--699933
LAAO----
LAAORhodococcus opacus--669894
LAAOCalloselasma rhodostoma--670798, 695276
LAAONaja atra--690221, 695209
LAAONaja oxiana--691918
LAAODaboia russellii russellii--692288
LAAOStreptococcus oligofermentans--692863
LAAODeinagkistrodon acutus--694317
LAAOBungarus fasciatus--695209, 701332
LAAOOphiophagus hannah--695209, 711791
LAAOBungarus multicinctusA8QL51-695209
LAAOVipera ammodytes ammodytes--695361, 712998
LAAOBothropoides pauloensisB5AR80-696493
LAAOAplysia californicaQ6IWZ0-697333
LAAOBothrops atrox--697450
LAAOBothrops jararaca--701330
LAAODaboia russellii siamensisQ4F867-701333
LAAOPlatichthys stellatusD2KWB6-711987
LAAOCrotalus atrox--713525
LAAOBothrops marajoensis--713558
LAAO-IBothrops jararaca--690684, 690856
LAAO-IBothrops moojeni--690693, 692650
LAAO-IBothrops jararacussuQ6TGQ9-690693
LAO----
LAOSebastes schlegelii--668580, 691917, 692408, 711786
LAOPseudoalteromonas luteoviolacea--690575
LAOCrotalus atrox, Hebeloma cylindrosporum, Hebeloma sp., Laccaria bicolor--694300
LAOAgkistrodon blomhoffi ussuriensis--695208
LAOBothrops insularis--695212
LAOMyoxocephalus polyacanthocephalusB5U982-697466
LAOMus musculus--697859
M-LAOGloydius blomhoffi--654872, 698669
ophio-amino-acid oxidase----
RoLAAORhodococcus opacus--667079
sarAEmericella nidulans--667254
Sebastes schlegeli antibacterial proteinSebastes schlegeliiA1IGW6-668580
Sebastes schlegelii antibacterial proteinSebastes schlegelii--691917
SSAPSebastes schlegeliiA1IGW6; 668580
SSAPSebastes schlegelii--691917, 692408
TJ-LAOProtobothrops jerdonii--656581
toxophallinAmanita phalloides--711980
TSV-LAOViridovipera stejnegeriQ6WP39-654441

CAS REGISTRY NUMBERCOMMENTARY
9000-89-9-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Agkistrodon blomhoffi ussuriensis-695208, 711329--Manually annotated by BRENDA team
Agkistrodon contortrix laticinctus-391781--Manually annotated by BRENDA team
Agkistrodon contortrix laticinctusvenom391821--Manually annotated by BRENDA team
Agkistrodon piscivorus piscivorus-389803--Manually annotated by BRENDA team
Agkistrodon piscivorus piscivoruscottonmouth moccasin391766--Manually annotated by BRENDA team
Amanita phalloides-711980--Manually annotated by BRENDA team
Aplysia californica-669658Q6IWZ0SwissprotManually annotated by BRENDA team
Aplysia californicasea hare, strain Cooper 1863 collected in California695637Q6IWZ0SwissprotManually annotated by BRENDA team
Aplysia californicastrain Cooper 1863 collected in California697333Q6IWZ0SwissprotManually annotated by BRENDA team
Aplysia californica Cooper 1863strain Cooper 1863 collected in California697333Q6IWZ0SwissprotManually annotated by BRENDA team
Aplysia punctata-670963Q6T277SwissProtManually annotated by BRENDA team
Bacillus carotarum2Pfa391824--Manually annotated by BRENDA team
Bacillus carotarum 2Pfa2Pfa391824--Manually annotated by BRENDA team
Bothropoides pauloensis-696493B5AR80UniProtManually annotated by BRENDA team
Bothrops alternatus-654954--Manually annotated by BRENDA team
Bothrops atrox-697450--Manually annotated by BRENDA team
Bothrops insularis-695212--Manually annotated by BRENDA team
Bothrops jararaca-690684Q6TGQ9UniprotManually annotated by BRENDA team
Bothrops jararaca-690856, 701330, 713559--Manually annotated by BRENDA team
Bothrops jararacussu-690693Q6TGQ9UniProtManually annotated by BRENDA team
Bothrops marajoensis-713558--Manually annotated by BRENDA team
Bothrops moojeni-391781, 692650--Manually annotated by BRENDA team
Bothrops moojeni-690693Q6TGQ8UniProtManually annotated by BRENDA team
Bothrops pirajai-667933--Manually annotated by BRENDA team
Bothrops sp.venom391823--Manually annotated by BRENDA team
Bungarus fasciatus-695209A8QL52UniProtManually annotated by BRENDA team
Bungarus fasciatusllected from Guangxi Province, P.R. China701332--Manually annotated by BRENDA team
Bungarus multicinctus-695209A8QL51UniProtManually annotated by BRENDA team
Calloselasma rhodostoma-391781, 391815, 391816, 391818, 391819, 667235, 669893, 695276--Manually annotated by BRENDA team
Calloselasma rhodostoma; expression in Pichia pastoris670798--Manually annotated by BRENDA team
Chlamydomonas reinhardtii-391814--Manually annotated by BRENDA team
Corynebacterium sp.A20391784--Manually annotated by BRENDA team
Corynebacterium sp. A20A20391784--Manually annotated by BRENDA team
Crotalus adamanteus-389803, 391766, 391770, 391774, 391776, 391777, 391778, 391779, 391781, 391782, 391783, 391790, 391791, 391793, 391795, 391797, 391799, 391800, 391804, 661038, 667368--Manually annotated by BRENDA team
Crotalus adamanteuseastern diamondback rattlesnake, multiple electrophoretic components391792--Manually annotated by BRENDA team
Crotalus atrox-391781, 694300, 713525--Manually annotated by BRENDA team
Crotalus durissus cascavella-670964--Manually annotated by BRENDA team
Crotalus terrificus terrificus-391775--Manually annotated by BRENDA team
Daboia russellii russellii-692288--Manually annotated by BRENDA team
Daboia russellii siamensis-701333Q4F867UniProtManually annotated by BRENDA team
Deinagkistrodon acutus-693949, 694317--Manually annotated by BRENDA team
Dolabella auricularia-655316--Manually annotated by BRENDA team
Emericella nidulans-667254--Manually annotated by BRENDA team
Eristicophis macmahoni-391781--Manually annotated by BRENDA team
Eristocophis macmahonii-391820--Manually annotated by BRENDA team
Gallus gallus-391801--Manually annotated by BRENDA team
Gloeobacter violaceus PCC 7421-695281--Manually annotated by BRENDA team
Gloydius blomhoffi-391781, 654872--Manually annotated by BRENDA team
Gloydius blomhoffi-698669Q90W54UniProtManually annotated by BRENDA team
Gloydius halys-654119--Manually annotated by BRENDA team
Hebeloma cylindrosporumstrain CBS 558.96694300--Manually annotated by BRENDA team
Hebeloma cylindrosporum CBS 558.96strain CBS 558.96694300--Manually annotated by BRENDA team
Hebeloma sp.strains SE5, F-NB01 , F-RS01, R-RS01 and SIV694300--Manually annotated by BRENDA team
Homo sapienslymphoid and non lymphoid malignancies, lymphoma cell lines L428, KM-H2, and SU-DHL-4699933--Manually annotated by BRENDA team
Laccaria bicolorstrain S238N694300--Manually annotated by BRENDA team
Macrovipera lebetina-670968--Manually annotated by BRENDA team
Meleagris gallopavoturkey391789--Manually annotated by BRENDA team
Mus musculus-656435, 697859--Manually annotated by BRENDA team
Mus musculusmilk391817O09046UniprotManually annotated by BRENDA team
Myoxocephalus polyacanthocephalusisozymes MPLAO1, MPLAO2, and MPLAO3697466B5U982UniProtManually annotated by BRENDA team
Naja atra-690221--Manually annotated by BRENDA team
Naja atra-695209A8QL58UniProtManually annotated by BRENDA team
Naja kaouthia-391781--Manually annotated by BRENDA team
Naja oxiana-691918--Manually annotated by BRENDA team
Neurospora crassa-391787, 391788, 391822--Manually annotated by BRENDA team
Neurospora crassainducible, expression in cells derepressed for nitrogen in presence of an amino acid, intracellular and extracellular location391803--Manually annotated by BRENDA team
no activity in Acinetobacter anitratum-391768--Manually annotated by BRENDA team
no activity in Alcaligenes faecalis-391768--Manually annotated by BRENDA team
no activity in Anabaena variabilis ATCC 29413-695281--Manually annotated by BRENDA team
no activity in Bacillus subtilis-391768--Manually annotated by BRENDA team
no activity in Bacillus subtilis subsp. subtilis-391784--Manually annotated by BRENDA team
no activity in Bacillus subtilis subsp. subtilis NCIB 3610-391784--Manually annotated by BRENDA team
no activity in Diplococcus pneumoniae-391768--Manually annotated by BRENDA team
no activity in Enterobacter aerogenes-391768--Manually annotated by BRENDA team
no activity in Escherichia coli-391784--Manually annotated by BRENDA team
no activity in Klebsiella pneumoniae-391768--Manually annotated by BRENDA team
no activity in Micrococcus tetragenus-391768--Manually annotated by BRENDA team
no activity in Moraxella catarrhalis-391768--Manually annotated by BRENDA team
no activity in Mycobacterium phlei-391768--Manually annotated by BRENDA team
no activity in Prochlorococcus marinus-695281--Manually annotated by BRENDA team
no activity in Pseudomonas aeruginosa-391768--Manually annotated by BRENDA team
no activity in Pseudomonas putida-391784--Manually annotated by BRENDA team
no activity in Serratia marcescens-391768--Manually annotated by BRENDA team
no activity in Shigella flexneri-391768--Manually annotated by BRENDA team
no activity in Staphylococcus aureus-391768--Manually annotated by BRENDA team
no activity in Staphylococcus epidermidis-391768--Manually annotated by BRENDA team
no activity in Streptococcus viridans-391768--Manually annotated by BRENDA team
no activity in Synechococcus sp.-695281--Manually annotated by BRENDA team
no activity in Synechococcus sp. CC9902-695281--Manually annotated by BRENDA team
no activity in Synechococcus sp. WH 8102-695281--Manually annotated by BRENDA team
no activity in Thermosynechococcus elongatus BP-1-695281--Manually annotated by BRENDA team
Nostoc punctiforme PCC 73102-695281--Manually annotated by BRENDA team
Nostoc sp. PCC 7120-695281--Manually annotated by BRENDA team
Ophiophagus hannah-391781, 391825, 391826, 711791--Manually annotated by BRENDA team
Ophiophagus hannah-695209A8QL50UniProtManually annotated by BRENDA team
Ophiophagus hannahking cobra391772--Manually annotated by BRENDA team
Platichthys stellatus-711987D2KWB6UniProtManually annotated by BRENDA team
Proteus mirabilis-391786--Manually annotated by BRENDA team
Proteus sp.30 different strains391768--Manually annotated by BRENDA team
Protobothrops jerdonii-656581--Manually annotated by BRENDA team
Protobothrops mucrosquamatus-391781--Manually annotated by BRENDA team
Protobothrops mucrosquamatusTaiwan habu snake391773--Manually annotated by BRENDA team
Providencia rettgeri-391775, 391785--Manually annotated by BRENDA team
Providencia sp.10 different strains391768--Manually annotated by BRENDA team
Providencia sp.PCM 1298391780--Manually annotated by BRENDA team
Providencia sp. PCM 1298PCM 1298391780--Manually annotated by BRENDA team
Pseudechis australis-391781--Manually annotated by BRENDA team
Pseudoalteromonas flavipulchraisolated from the encrusting pore coral Montipora aequituberculata from the Kenting coast of Southern Taiwan711872--Manually annotated by BRENDA team
Pseudoalteromonas flavipulchra C2isolated from the encrusting pore coral Montipora aequituberculata from the Kenting coast of Southern Taiwan711872--Manually annotated by BRENDA team
Pseudoalteromonas luteoviolaceastrain CPMOR-1; strain CPMOR-2; strain NCIMB 1893T690575--Manually annotated by BRENDA team
Pseudoalteromonas luteoviolacea CPMOR-1strain CPMOR-1690575--Manually annotated by BRENDA team
Pseudoalteromonas luteoviolacea CPMOR-2strain CPMOR-2690575--Manually annotated by BRENDA team
Pseudoalteromonas luteoviolacea NCIMB 1893Tstrain NCIMB 1893T690575--Manually annotated by BRENDA team
Ralstonia pickettii T1-391784--Manually annotated by BRENDA team
Rattus norvegicus-391766, 391769, 391794, 391796, 391798, 391802--Manually annotated by BRENDA team
Rhodococcus opacus-653762, 667079, 669894--Manually annotated by BRENDA team
Rhodococcus opacusDSM 43250; DSM 43250, one of the best L-AAO producer651026Q8VPD4SwissProtManually annotated by BRENDA team
Rhodococcus opacuslao-gene; DSM 43250 strain653762Q8VPD4SwissProtManually annotated by BRENDA team
Rhodococcus sp.-711874--Manually annotated by BRENDA team
Sebastes schlegelii-668580A1IGW6SwissProtManually annotated by BRENDA team
Sebastes schlegelii-668580, 691917, 692408, 711786--Manually annotated by BRENDA team
snake-391771, 391781, 391812, 391813--Manually annotated by BRENDA team
Streptococcus oligofermentans-692863--Manually annotated by BRENDA team
Synechococcus cedrorum PCC 6908-695281--Manually annotated by BRENDA team
Synechococcus elongatus PCC 6301-695281P72346UniProtManually annotated by BRENDA team
Synechococcus elongatus PCC 7942-695281--Manually annotated by BRENDA team
Synechococcus elongatus PCC 7942Synechococcus leopoliensis (blue-green algae)391805, 391806, 391807, 391808, 391809, 391810--Manually annotated by BRENDA team
Synechococcus sp.-391811--Manually annotated by BRENDA team
Synechococcus sp. CC9605-695281--Manually annotated by BRENDA team
Synechococcus sp. WH 5701-695281--Manually annotated by BRENDA team
Synechococcus sp. WH 7805-695281--Manually annotated by BRENDA team
Synechocystis sp. PCC 6803-695281--Manually annotated by BRENDA team
Trichodesmium erythraeum IMS101-695281--Manually annotated by BRENDA team
Trimeresurus flavoviridis-391781--Manually annotated by BRENDA team
Vipera ammodytes ammodytes-712998--Manually annotated by BRENDA team
Vipera ammodytes ammodytescaptured in northwest Bulgaria, five LAAO isozymes695361--Manually annotated by BRENDA team
Viridovipera stejnegeri-654441Q6WP39UniprotManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionBothrops atrox-the enzyme induces in vitro platelet aggregation, which may be due to H2O2 production, the addition of catalase completely inhibits the aggregation effect. It also shows cytotoxicity towards several cancer cell lines: HL60, Jurkat, B16F10 and PC12 causing apoptosis. The cytotoxicity activity is abolished by catalase697450
physiological functionMyoxocephalus polyacanthocephalusB5U982the antibacterial LAO isozymes may be involved in the innate immunity of the great sculpin Myoxocephalus polyacanthocephalus skin697466
physiological functionAgkistrodon blomhoffi ussuriensis-Akbu-LAAO shows apparent anti-aggregation effects on human and rabbit platelets and exhibits a strong bacteriostasis effect on Staphylococcus aureus, 18fold that of cephalosporin C711329
physiological functionSebastes schlegelii-serum LAO is involved in innate immunity in the rockfish body, it exhibits a broad antibacterial activity against Gram positive and negative bacteria, most potently against Aeromonas hydrophila and Aeromonas salmonicida with a minimum inhibitory concentration of 0.000078 mg/ml711786
physiological functionOphiophagus hannah-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 enzyme711791
physiological functionPseudoalteromonas flavipulchra-the enzyme shows from strain C2 shows potent antibacterial activity against several methicillin-resistant Staphylococcus aureus strains, antibacterial spectrum, overview711872
physiological functionAmanita phalloides-toxophallin induces chromatin condensation, as well as DNA and nucleus fragmentation, which are typical for apoptosis. Toxophallin uses a caspase-independent pathway of apoptosis induction711980
additional informationAmanita phalloides-toxophallin is a highly cytotoxic protein, but differs distinctly from the other death cap toxic protein phallolysin. The interaction of toxophallin with target cells is not mediated by a specific cell surface receptor711980

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
(1,1,2,2-tetrafluoroethyl)-L-cysteine + H2O + O22-oxo-3-[(1,1,2,2-tetrafluoroethyl)sulfanyl]propanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-80% of the activity with L-methionine661038--?
3,4-dihydroxyphenyl-L-Ala + H2O + O23-(3,4-dihydroxyphenyl)-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus--667368--?
alpha-hydroxyisocaproic acid + H2O + O22-oxo-4-methylpentanoic acid + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391802--?
alpha-hydroxyvaleric acid + H2O + O22-oxopentanoic acid + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391802--?
an L-amino acid + H2O + O2a 2-oxo-acid + NH3 + H2O2
show the reaction diagram		Vipera ammodytes ammodytes-L-amino-acid oxidase catalyzes the oxidative deamination of a number of L-amino acids to their respective imino acids with concomitant hydrolysis to alpha-keto acids, together with the production of ammonia and hydrogen peroxide695361--?
DL-3-(1-pyridyl)-alanine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD424% of the activity compared to L-alanine651026-651026?
DL-3-(1-pyridyl)alanine + H2O + O23-(1-pyridyl)pyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD424% of the activity with L-Ala651026--?
DL-4-fluorophenylalanine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD425% of the activity compared to L-alanine651026-651026?
DL-4-fluorophenylalanine + H2O + O2(4-fluorophenyl)pyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD425% of the activity with L-Ala651026--?
DL-asparagine + H2O + O22-oxosuccinamic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--?
DL-beta-phenylserine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD48% of the activity with L-Ala651026--?
DL-homophenylalanine + H2O + O22-oxo-4-phenylbutanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD450% of the activity compared to L-alanine651026-651026?
DL-homophenylalanine + H2O + O22-oxo-4-phenylbutyric acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD450% of the activity with L-Ala651026--?
DL-leucine + H2O + O22-oxo-4-methylpentanoate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--?
DL-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--?
DL-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--?
DL-norleucine + H2O + O2alpha-ketocaproate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD473% of the activity compared to L-alanine651026-651026?
DL-norleucine + H2O + O2alpha-ketocaproate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD473% of the activity with L-Ala651026--?
DL-norleucine + H2O + O22-oxocaproate + NH3 + H2O2
show the reaction diagram		Gloydius blomhoffiQ90W54-698669--?
DL-norleucine + H2O + O22-oxocaproate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--?
DL-O-methylserine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD499% of the activity compared to L-alanine651026-651026?
DL-O-methylserine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD499% of the activity with L-Ala651026--?
DL-phenylseine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD48% of the activity compared to L-alanine651026-651026?
DL-threonine + H2O + O22-oxo-3-hydroxybutanoic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--?
DL-tryptophan + H2O + O23-(1H-indol-3-yl)-2-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--?
DL-valine + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--?
glycine + H2O + O2glyoxylate + NH3 + H2O2
show the reaction diagram		Rattus norvegicus-not391769, 391802--?
glycine + H2O + O2glyoxylate + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.-not391784--?
glycine + H2O + O2glyoxylate + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-not391773---
glycine + H2O + O2glyoxylate + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-low activity391770---
glycine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Bothrops moojeni--692650--?
hydroxyisovaleric acid + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391802--?
L-2,3-diaminopropionic acid + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD471% of the activity compared to L-alanine651026-651026?
L-2,3-diaminopropionic acid + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD471% of the activity with L-Ala651026--?
L-2,4-diaminobutyric acid + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4100% of the activity compared to L-alanine651026-651026?
L-2,4-diaminobutyric acid + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4as active as L-Ala651026--?
L-2-4,4,dimethylvaleric acid + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD446% of the activity compared to L-alanine651026-651026?
L-2-amino-4,4-dimethylhexanoic acid + H2O + O24,4-dimethyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD444% of the activity with L-Ala651026--?
L-2-amino-4,4-dimethylvaleric acid + H2O + O24,4-dimethyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD446% of the activity with L-Ala651026--?
L-2-amino-5,5-dimethylhexanoic acid + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD444% of the activity compared to L-alanine651026-651026?
L-2-chlorophenylalanine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD424% of the activity compared to L-alanine651026-651026?
L-2-chlorophenylalanine + H2O + O2(2-chlorophenyl)pyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD424% of the activity with L-Ala651026--?
L-3-(1-naphthyl)alanine + H2O + O23-(1-naphthyl)pyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4109% of the activity with L-Ala651026--?
L-3-(naphthyl)alanine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4109% of the activity compared to L-alanine651026-651026?
L-4-aminophenylalanine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD416% of the activity compared to L-alanine651026-651026?
L-4-aminophenylalanine + H2O + O2(4-aminophenyl)pyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD416% of the activity with L-Ala651026--?
L-4-chlorophenylalanine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD49% of the activity compared to L-alanine651026-651026?
L-4-chlorophenylalanine + H2O + O2(4-chlorophenyl)pyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD49% of the activity with L-Ala651026--?
L-4-nitrophenylalanine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD430% of the activity compared to L-alanine651026-651026?
L-4-nitrophenylalanine + H2O + O2(4-nitrophenyl)pyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD430% of the activity with L-Ala651026--?
L-Ala + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4-651026--?
L-Ala + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Ala + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80-696493--?
L-alanine + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-alanine + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4-653762--?
L-alanine + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacus--669894--?
L-alanine + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops moojeni--692650--?
L-alanine + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-alanine + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-not391773---
L-alanine + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4highly enantioselective enzyme with a broad substrate specificity651026-651026?
L-alanine + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4highly enantioselective enzyme with a broad substrate specificity653762-653762?
L-albizziin + H2O + O2alpha-keto-beta-ureidopropionic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-L-alpha-amino-beta-ureidopropionic acid391804--?
L-alpha-aminobutyric acid + H2O + O2alpha-ketobutyrate + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-alpha-aminobutyric acid + H2O + O2alpha-ketobutyrate + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.-low reaction rate391768--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Gallus gallus--391801--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Meleagris gallopavo--391789--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942--391805, 391806, 391807, 391808, 391809, 391810--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Mus musculusO09046-391817--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391769, 391794, 391796, 391798, 391802--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Neurospora crassa--391787, 391788, 391803, 391822--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Proteus mirabilis--391786--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Providencia sp.--391768, 391780--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus sp.--391811--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Proteus sp.--391768--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma--391815, 391816--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus--389803, 391766, 391770, 391774, 391776, 391777, 391778, 391779, 391782, 391783, 391790, 391791, 391792, 391793, 391795, 391797, 391799, 391800, 391804--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Ophiophagus hannah--391772, 391825--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus--391773--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Providencia rettgeri--391775, 391785--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Eristocophis macmahonii--391820--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Crotalus terrificus terrificus--391775--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Agkistrodon piscivorus piscivorus--389803, 391766--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		snake--391771, 391781, 391812, 391813--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Agkistrodon contortrix laticinctus--391821--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Bothrops sp.--391823--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Bacillus carotarum--391824--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Chlamydomonas reinhardtii-all amino acids except cysteine391814--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Rattus norvegicus-other electron acceptors: methylene blue391766--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942-first step in reaction sequence of formation of phenylacetic acid from L-phenylalanine391809--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942-functional in photosynthetic and respiratory activities as well as in L-arginine degradation391806---
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942-functional in photosynthetic and respiratory activities as well as in L-arginine degradation391810--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.-utilization of amino acids as nitrogen source391784--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Chlamydomonas reinhardtii-operates as scavanger of ammonium from extracellular amino acids391814--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-bactericidal action of L-amino acid oxidase391791--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942-involved in the water-splitting reaction of photosystem II391805, 391807---
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus sp.-involved in the water-splitting reaction of photosystem II391811--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Mus musculusO09046responsible for killing bacteria in the mammary gland391817--?
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		snake-biological functions of snake venom enzymes391781---
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Dolabella auricularia-cell death induced by the enzyme is of two types, one non-apoptotic and the other apoptotic. The effect is not dependent on the acute toxicity of H2O2655316--?
L-Arg + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Arg + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80-696493--?
L-Arg + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD470% of the activity with L-Ala651026--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Meleagris gallopavo--391789--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942--391808--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Bothrops moojeni--692650--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Bacillus carotarum--391824--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Aplysia punctataQ6T277-670963--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Aplysia californicaQ6IWZ0-669658--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Streptococcus oligofermentans--692863--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.-low reaction rate391768--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-low reaction rate391773--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Naja oxiana-good substrate691918--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD470% of the activity compared to L-alanine651026-651026?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas luteoviolacea-low enzyme activity690575--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Macrovipera lebetina-substrate affinity in decreasing order: L-methionine, L-tryptophan, L-leucine, L-histidine, L-phenylalanine, L-arginine, L-isoleucine670968--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942, Synechococcus cedrorum PCC 6908-best substrate, 100% substrate specificity695281--?
L-arginine + H2O + O22-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 6301P72346best substrate, 100% substrate specificity695281--?
L-arginine + H2O + O22-oxo-5-guanidinopentanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--?
L-arginine + H2O + O22-oxo-5-guanidinopentanoic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--?
L-Asn + H2O + O22-oxosuccinamic acid + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Asp + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD411% of the activity with L-Ala651026--?
L-Asp + H2O + O2alpha-ketosuccinamic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD497% of the activity with L-Ala651026--?
L-Asp + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-asparagine + H2O + O2alpha-ketosuccinamic acid + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-asparagine + H2O + O2alpha-ketosuccinamic acid + NH3 + H2O2
show the reaction diagram		Streptococcus oligofermentans--692863--?
L-asparagine + H2O + O2alpha-ketosuccinamic acid + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-very low activity391773--?
L-asparagine + H2O + O2alpha-ketosuccinamic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD497% of the activity compared to L-alanine651026-651026?
L-aspartic acid + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Streptococcus oligofermentans--692863--?
L-aspartic acid + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Rattus norvegicus-not391769---
L-aspartic acid + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.-not391784---
L-aspartic acid + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-low activity391770--?
L-aspartic acid + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-low activity391773--?
L-aspartic acid + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD411% of the activity compared to L-alanine651026-651026?
L-citrulline + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD474% of the activity compared to L-alanine651026-651026?
L-citrulline + H2O + O2N5-carbamoyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD474% of the activity with L-Ala651026--?
L-citrulline + H2O + O22-oxo-5-ureidovaleric acid + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--?
L-cysteic acid + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD434% of the activity compared to L-alanine651026-651026?
L-cysteic acid + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD434% of the activity with L-Ala651026--?
L-cysteine + H2O + O22-oxo-3-mercaptopropanoic acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-cysteine + H2O + O22-oxo-3-mercaptopropanoic acid + NH3 + H2O2
show the reaction diagram		Providencia rettgeri, Crotalus terrificus terrificus--391775---
L-cysteine + H2O + O22-oxo-3-mercaptopropanoic acid + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-not391773---
L-cysteine + H2O + O22-oxo-3-mercaptopropanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-40% of the activity with L-methionine661038--?
L-cystine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-very low activity391773--?
L-cystine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4104% of the activity with L-Ala651026--?
L-cystine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-35% of the activity with L-methionine661038--?
L-cystine + H2O + O22-oxo-3-mercaptopropanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4104% of the activity compared to L-alanine651026-651026?
L-Dopa + H2O + O2? + NH3 + H2O2
show the reaction diagram		Mus musculus-about 10% of the activity with L-Phe656435--?
L-Gln + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Gln + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD452% of the activity with L-Ala651026--?
L-Glu + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Glu + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80-696493--?
L-Glu + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD452% of the activity with L-Ala651026--?
L-glutamate + H2O + O22-oxoglutaric acid + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--?
L-glutamic acid + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Bothrops moojeni--692650--?
L-glutamic acid + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--?
L-glutamic acid + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Rattus norvegicus-not391769---
L-glutamic acid + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-low activity391770--?
L-glutamic acid + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-low activity391773--?
L-glutamic acid + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--?
L-glutamic acid + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD452% of the activity compared to L-alanine651026-651026?
L-glutamic acid + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas luteoviolacea-high enzyme activity690575--?
L-glutamine + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-very low activity391773--?
L-glutamine + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-10% of the activity with L-methionine661038--?
L-glutamine + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas luteoviolacea-high enzyme activity690575--?
L-glutamine + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Streptococcus oligofermentans--692863--?
L-glutamine + H2O + O22-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD452% of the activity compared to L-alanine651026-651026?
L-glutamine + H2O + O22-oxo-4-carbamoylbutanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--?
L-glutamine + H2O + O22-oxo-4-carbamoylbutanoic acid + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--?
L-His + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-His + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80-696493--?
L-His + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD436% of the activity with L-Ala651026--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Meleagris gallopavo--391789--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942--391808--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Bothrops moojeni--692650--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Hebeloma sp.--694300--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Ophiophagus hannahA8QL50-695209--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.-low reaction rate391768--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-low reaction rate391773--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD436% of the activity compared to L-alanine651026-651026?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas luteoviolacea-low enzyme activity690575--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Macrovipera lebetina-substrate affinity in decreasing order: L-methionine, L-tryptophan, L-leucine, L-histidine, L-phenylalanine, L-arginine, L-isoleucine670968--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Bothrops pirajai-substrate affinity in decreasing order: L-phenylalanine, L-tyrosine, L-tryptophan, L-leucine, L-methionine, L-isoleucine, L-valine, L-histidine667933--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942, Synechococcus cedrorum PCC 6908-poor substrate, less than 2% substrate specificity695281--?
L-histidine + H2O + O23-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 6301P72346poor substrate, less than 2% substrate specificity695281--?
L-histidine + H2O + O22-oxo-4-imidazolepropionic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--?
L-histidine + H2O + O22-oxo-4-imidazolepropionic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--?
L-homocysteine + H2O + O24-thio-2-ketobutyric acid + NH3 + H2O2
show the reaction diagram		Providencia rettgeri, Crotalus terrificus terrificus--391775---
L-homocysteine + H2O + O24-thio-2-ketobutyric acid + NH3 + H2O2
show the reaction diagram		snake--391812--?
L-homocysteine thiolactone + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD423% of the activity compared to L-alanine651026-651026?
L-homocysteine thiolactone + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD423% of the activity with L-Ala651026--?
L-homoserine + H2O + O22-oxo-4-hydroxybutyric acid + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--?
L-homoserine lactone + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD466% of the activity compared to L-alanine651026-651026?
L-homoserine lactone + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD466% of the activity with L-Ala651026--?
L-Ile + H2O + O23-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram		Bothrops atrox--697450--?
L-Ile + H2O + O23-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Ile + H2O + O23-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram		Daboia russellii siamensisQ4F867-701333--?
L-Ile + H2O + O23-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80-696493--?
L-Ile + H2O + O23-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD445% of the activity with L-Ala651026--?
L-isoleucine + H2O + O2alpha-keto-beta-methyl-pentanoic acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-isoleucine + H2O + O2alpha-keto-beta-methyl-pentanoic acid + NH3 + H2O2
show the reaction diagram		Streptococcus oligofermentans--692863--?
L-isoleucine + H2O + O2alpha-keto-beta-methyl-pentanoic acid + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.-low reaction rate391768--?
L-isoleucine + H2O + O2alpha-keto-beta-methyl-pentanoic acid + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-low reaction rate391773--?
L-isoleucine + H2O + O2alpha-keto-beta-methyl-pentanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD445% of the activity compared to L-alanine651026-651026?
L-isoleucine + H2O + O23-methyl-2-oxo-pentanoate + NH3 + H2O2
show the reaction diagram		Macrovipera lebetina-substrate affinity in decreasing order: L-methionine, L-tryptophan, L-leucine, L-histidine, L-phenylalanine, L-arginine, L-isoleucine670968--?
L-isoleucine + H2O + O23-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas luteoviolacea-low enzyme activity690575--?
L-isoleucine + H2O + O23-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops pirajai-substrate affinity in decreasing order: L-phenylalanine, L-tyrosine, L-tryptophan, L-leucine, L-methionine, L-isoleucine, L-valine, L-histidine667933--?
L-isoleucine + H2O + O23-methyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-isoleucine + H2O + O23-methyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram		Daboia russellii russellii--692288--?
L-isoleucine + H2O + O23-methyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram		Ophiophagus hannahA8QL50-695209--?
L-isoleucine + H2O + O23-methyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops moojeni-high catalytic activity692650--?
L-isoleucine + H2O + O23-methyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops jararacaQ6TGQ9high substrate activity690684--?
L-isoleucine + H2O + O23-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram		Crotalus atrox--713525--?
L-isoleucine + H2O + O23-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--?
L-lactic acid + H2O + O2pyruvate + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391766, 391769, 391802--?
L-Leu + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Mus musculus--697859--?
L-Leu + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops atrox--697450--?
L-Leu + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Gloydius halys--654119--?
L-Leu + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Leu + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Daboia russellii siamensisQ4F867-701333--?
L-Leu + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80-696493--?
L-Leu + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD468% of the activity with L-Ala651026--?
L-Leu + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops jararaca-LAAOs are flavoenzymes catalyzing the stereospecifically oxidative deamination of a wide range of L-amino acids701330--?
L-Leu + H2O + O22-oxo-4-methylvaleric acid + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--711329--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Meleagris gallopavo--391789--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391769---
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391802--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma--391815, 391819---
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma--695276--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus atrox--694300--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Naja atra--690221--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Eristocophis macmahonii--391820--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Laccaria bicolor--694300--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Bacillus carotarum--391824--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus durissus cascavella--670964--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Hebeloma cylindrosporum--694300--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Daboia russellii russellii--692288--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Hebeloma sp.--694300--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Ophiophagus hannahA8QL50-695209--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Naja oxiana-good substrate691918--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.-high reaction rate391768--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-high reaction rate391770--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-high reaction rate391773--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops sp.-high reaction rate391823--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Agkistrodon contortrix laticinctus-no reaction with D-leucine391821---
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD468% of the activity compared to L-alanine651026-651026?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma-substrate affinity in decreasing order: L-methionine, L-leucine, L-phenylalanine, L-tyrosine, L-tryptophan670798--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Macrovipera lebetina-substrate affinity in decreasing order: L-methionine, L-tryptophan, L-leucine, L-histidine, L-phenylalanine, L-arginine, L-isoleucine670968--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops pirajai-substrate affinity in decreasing order: L-phenylalanine, L-tyrosine, L-tryptophan, L-leucine, L-methionine, L-isoleucine, L-valine, L-histidine667933--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops moojeni-high affinity for the substrate692650--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas luteoviolacea-high enzyme activity690575--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops jararacaQ6TGQ9high substrate activity, most specific substrate690684--?
L-leucine + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Deinagkistrodon acutus-one of the best substrates694317--?
L-leucine + H2O + O22-oxo-4-methylpentanoate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--?
L-leucine + H2O + O22-oxo-4-methylvaleric acid + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--?
L-leucine + H2O + O22-oxo-4-methylvaleric acid + NH3 + H2O2
show the reaction diagram		Bothrops marajoensis--713558--?
L-leucine + H2O + O22-oxo-4-methylvaleric acid + NH3 + H2O2
show the reaction diagram		Bothrops jararaca--713559--?
L-leucine + H2O + O22-oxo-4-methylpentanoate acid + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--?
L-Lys + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Lys + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Aplysia californicaQ6IWZ0-695637--?
L-Lys + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Aplysia californicaQ6IWZ0-697333--?
L-Lys + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Aplysia californicaQ6IWZ0-697333the enzymatic reaction likely forms an equilibrium mixture containing the linear form 6-amino-2-oxohexanoic acid, the cyclic imine D1-piperidine-2-carboxylic acid, the cyclic enamine D2-piperidine-2-carboxylic acid, possibly the linear enol 6-amino-2-hydroxy-hex-2-enoic acid, the alpha-dihydroxyacid 6-amino-2,2-dihydroxy-hexanoic acid, and the cyclic aminol 2-hydroxy-piperidine-2-carboxylic acid, identification and quantification by mass spectrometry and NMR, overview-?
L-Lys + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD455% of the activity with L-Ala651026--?
L-Lys + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Aplysia californicaQ6IWZ0the ink of sea hares contains escapin, an L-amino acid oxidase that metabolizes L-lysine, thereby producing a mixture that kills microbes and deters attacking predators. This secretion contains H2O2, ammonia, and an equilibrium mixture of socalled escapin intermediate product, EIP-K, that includes 6-amino-2-oxohexanoic acid and several other molecules. Components of the equilibrium mixture react nonenzymatically with H2O2 to form escapin end product, i.e. EEP-K, which contains 2-aminovaleric acid and 2-valerolactam. The proportions of the components in this equilibrium mixture change with pH, and this is biologically important because the secretion has pH 5 when released but becomes pH 8 when fully diluted in seawater, overview695637--?
L-Lys + H2O + O26-amino-2-oxo-hexanoic acid + NH3 + H2O2
show the reaction diagram		Myoxocephalus polyacanthocephalusB5U982-697466--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Meleagris gallopavo--391789--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942--391808--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops moojeni--692650--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Laccaria bicolor--694300--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Bacillus carotarum--391824--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Aplysia punctataQ6T277-670963--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Sebastes schlegeliiA1IGW6-668580--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Sebastes schlegelii--692408--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Hebeloma sp.--694300--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Streptococcus oligofermentans--692863--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Ophiophagus hannahA8QL50-695209--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Rattus norvegicus-not391769---
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Synechococcus sp.-not391811---
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-not391773---
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-low activity391770--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Sebastes schlegelii-strictly specific for711786--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD455% of the activity compared to L-alanine651026-651026?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 6301P7234673% substrate specificity695281--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Synechococcus cedrorum PCC 6908-81% substrate specificity695281--?
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942-82% substrate specificity695281--?
L-Met + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Met + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Bothrops atrox-best substrate697450--?
L-Met + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80best substrate696493--?
L-Met + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD472% of the activity with L-Ala651026--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391802--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma--391819---
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus--661038--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Crotalus atrox--713525--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Laccaria bicolor--694300--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Bacillus carotarum--391824--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Daboia russellii russellii--692288--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Hebeloma sp.--694300--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Ophiophagus hannahA8QL50-695209--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Amanita phalloides-preferred substrate711980--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Naja oxiana-good substrate691918--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.-high reaction rate391768--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-high reaction rate391770--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-high reaction rate391773--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Bothrops sp.-high reaction rate391823--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD472% of the activity compared to L-alanine651026-651026?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma-substrate affinity in decreasing order: L-methionine, L-leucine, L-phenylalanine, L-tyrosine, L-tryptophan670798--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Macrovipera lebetina-substrate affinity in decreasing order: L-methionine, L-tryptophan, L-leucine, L-histidine, L-phenylalanine, L-arginine, L-isoleucine670968--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Bothrops pirajai-substrate affinity in decreasing order: L-phenylalanine, L-tyrosine, L-tryptophan, L-leucine, L-methionine, L-isoleucine, L-valine, L-histidine667933--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Bothrops moojeni-high affinity for the substrate692650--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas luteoviolacea-high enzyme activity690575--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Bothrops jararacaQ6TGQ9high substrate activity690684--?
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Deinagkistrodon acutus-one of the best substrates694317--?
L-norleucine + H2O + O2alpha-ketocaproate + NH3 + H2O2
show the reaction diagram		Providencia sp.--391768--?
L-norleucine + H2O + O2alpha-ketocaproate + NH3 + H2O2
show the reaction diagram		Proteus sp.-high reaction rate391768--?
L-norleucine + H2O + O22-oxohexanoate + NH3 + H2O2
show the reaction diagram		Bothrops moojeni-high catalytic activity692650--?
L-norvaline + H2O + O22-oxo-valeric acid + NH3 + NADH + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma--391819---
L-norvaline + H2O + O22-oxo-valeric acid + NH3 + NADH + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.-high reaction rate391768--?
L-Orn + H2O + O22-oxo-5-aminopentanoate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4117% of the activity with L-Ala651026--?
L-ornithine + H2O + O22-oxo-5-aminopentanoate + NH3 + H2O2
show the reaction diagram		Meleagris gallopavo--391789--?
L-ornithine + H2O + O22-oxo-5-aminopentanoate + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942--391808--?
L-ornithine + H2O + O22-oxo-5-aminopentanoate + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-ornithine + H2O + O22-oxo-5-aminopentanoate + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-not391773---
L-ornithine + H2O + O22-oxo-5-aminopentanoate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD4117% of the activity compared to L-alanine651026-651026?
L-ornithine + H2O + O22-oxo-5-aminopentanoate + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942-28% substrate specificity695281--?
L-ornithine + H2O + O22-oxo-5-aminopentanoate + NH3 + H2O2
show the reaction diagram		Synechococcus cedrorum PCC 6908-35% substrate specificity695281--?
L-ornithine + H2O + O22-oxo-5-aminopentanoate + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 6301P7234646% substrate specificity695281--?
L-Phe + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Bothrops atrox--697450--?
L-Phe + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Phe + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Daboia russellii siamensisQ4F867-701333--?
L-Phe + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80-696493--?
L-Phe + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Mus musculus-best substrate656435--?
L-Phe + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD453% of the activity with L-Ala651026--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Meleagris gallopavo--391789--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391802--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacus--669894--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma--391819---
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma--669893--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Crotalus atrox, Laccaria bicolor--694300--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Bacillus carotarum--391824--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Hebeloma cylindrosporum, Hebeloma sp.--694300--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Naja oxiana-good substrate691918--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.-high reaction rate391768--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-high reaction rate391770--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-high reaction rate391773--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Bothrops sp.-high reaction rate391823--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD453% of the activity compared to L-alanine651026-651026?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma-substrate affinity in decreasing order: L-methionine, L-leucine, L-phenylalanine, L-tyrosine, L-tryptophan670798--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Macrovipera lebetina-substrate affinity in decreasing order: L-methionine, L-tryptophan, L-leucine, L-histidine, L-phenylalanine, L-arginine, L-isoleucine670968--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Bothrops pirajai-substrate affinity in decreasing order: L-phenylalanine, L-tyrosine, L-tryptophan, L-leucine, L-methionine, L-isoleucine, L-valine, L-histidine667933--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Bothrops moojeni-high affinity for the substrate692650--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas luteoviolacea-high enzyme activity690575--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Bothrops jararacaQ6TGQ9high substrate activity, most specific substrate690684--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacus-hydride transfer as the mechanism of dehydrogenation. The substrate-binding domain of LAAO is made up of residues 52-128, 230-238 and 315-422. The substrate-binding domain has almost the same topology as the snake venom LAAO669894--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Daboia russellii russellii-maximum catalytic efficiency for both isoforms692288--?
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Deinagkistrodon acutus-one of the best substrates694317--?
L-phenylalanine + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Homo sapiens-inhibition of T cell proliferation through phenylalanine degradation699933activity measurement by measuring H2O2 production-?
L-phenylglycine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD45% of the activity compared to L-alanine651026-651026?
L-phenylglycine + H2O + O2phenylacetate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD45% of the activity with L-Ala651026--?
L-Pro + H2O + O2? + NH3 + H2O2
show the reaction diagram		Mus musculus-less than 10% of the activity with L-Phe656435--?
L-proline + H2O + O2? + NH3 + H2O2
show the reaction diagram		Bothrops moojeni--692650--?
L-propargylglycine + H2O + O22-oxopent-4-ynoic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus--391783--?
L-Ser + H2O + O22-oxo-3-hydroxypropionic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD472% of the activity with L-Ala651026--?
L-serine + H2O + O22-oxo-3-hydroxypropionic acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-serine + H2O + O22-oxo-3-hydroxypropionic acid + NH3 + H2O2
show the reaction diagram		Bothrops moojeni--692650--?
L-serine + H2O + O22-oxo-3-hydroxypropionic acid + NH3 + H2O2
show the reaction diagram		Rattus norvegicus-not391769---
L-serine + H2O + O22-oxo-3-hydroxypropionic acid + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-not391773---
L-serine + H2O + O22-oxo-3-hydroxypropionic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-low activity391770--?
L-serine + H2O + O22-oxo-3-hydroxypropionic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD472% of the activity compared to L-alanine651026-651026?
L-threonine + H2O + O22-oxo-3-hydroxybutanoic acid + NH3 + H2O2
show the reaction diagram		Bothrops moojeni--692650--?
L-threonine + H2O + O22-oxo-3-hydroxybutanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-low activity391770--?
L-Trp + H2O + O2indole-3-pyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD412% of the activity with L-Ala651026--?
L-Trp + H2O + O2indol-3-pyruvate + NH3 + H2O2
show the reaction diagram		Bothrops atrox--697450--?
L-Trp + H2O + O2indol-3-pyruvate + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Trp + H2O + O2indol-3-pyruvate + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80-696493--?
L-tryptophan + H2O + O2? + NH3 + H2O2
show the reaction diagram		Meleagris gallopavo--391789--?
L-tryptophan + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391802--?
L-tryptophan + H2O + O2? + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-tryptophan + H2O + O2? + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-low reaction rate391773--?
L-tryptophan + H2O + O2? + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.-high reaction rate391768--?
L-tryptophan + H2O + O2? + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-high reaction rate391770--?
L-tryptophan + H2O + O2? + NH3 + H2O2
show the reaction diagram		Bothrops sp.-high reaction rate391823--?
L-tryptophan + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD412% of the activity compared to L-alanine651026-651026?
L-tryptophan + H2O + O2? + NH3 + H2O2
show the reaction diagram		Mus musculus-about 30% of the activity with L-Phe656435--?
L-tryptophan + H2O + O2? + NH3 + H2O2
show the reaction diagram		Bothrops pirajai-substrate affinity in decreasing order: L-phenylalanine, L-tyrosine, L-tryptophan, L-leucine, L-methionine, L-isoleucine, L-valine, L-histidine667933--?
L-tryptophan + H2O + O23-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma--391819---
L-tryptophan + H2O + O23-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-tryptophan + H2O + O23-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Daboia russellii russellii--692288--?
L-tryptophan + H2O + O23-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Streptococcus oligofermentans--692863--?
L-tryptophan + H2O + O23-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Naja oxiana-good substrate691918--?
L-tryptophan + H2O + O23-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma-substrate affinity in decreasing order: L-methionine, L-leucine, L-phenylalanine, L-tyrosine, L-tryptophan670798--?
L-tryptophan + H2O + O23-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Macrovipera lebetina-substrate affinity in decreasing order: L-methionine, L-tryptophan, L-leucine, L-histidine, L-phenylalanine, L-arginine, L-isoleucine670968--?
L-tryptophan + H2O + O23-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Bothrops moojeni-high affinity for the substrate692650--?
L-tryptophan + H2O + O23-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas luteoviolacea-high enzyme activity690575--?
L-tryptophan + H2O + O23-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram		Deinagkistrodon acutus-one of the best substrates694317--?
L-tryptophan + H2O + O23-(1H-indol-3-yl)-2-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus atrox--713525--?
L-Tyr + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD454% of the activity with L-Ala651026--?
L-Tyr + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Mus musculus-about 40% of the activity with L-Phe656435--?
L-Tyr + H2O + O24-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Bothrops atrox--697450--?
L-Tyr + H2O + O24-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Bungarus fasciatus--701332--?
L-Tyr + H2O + O24-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80-696493--?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Meleagris gallopavo--391789--?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.--391784--?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.--391768--?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus--391770--?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus--391773--?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Daboia russellii russellii--692288--?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD454% of the activity compared to L-alanine651026-651026?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Calloselasma rhodostoma-substrate affinity in decreasing order: L-methionine, L-leucine, L-phenylalanine, L-tyrosine, L-tryptophan670798--?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Bothrops pirajai-substrate affinity in decreasing order: L-phenylalanine, L-tyrosine, L-tryptophan, L-leucine, L-methionine, L-isoleucine, L-valine, L-histidine667933--?
L-tyrosine + H2O + O2p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Bothrops moojeni-high affinity for the substrate692650--?
L-tyrosine + H2O + O24-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--?
L-tyrosine + H2O + O24-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--?
L-Val + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Bothropoides pauloensisB5AR80-696493--?
L-Val + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD432% of the activity with L-Ala651026--?
L-valine + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Bothrops moojeni--692650--?
L-valine + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Crotalus atrox--713525--?
L-valine + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--695208--?
L-valine + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Protobothrops mucrosquamatus-very low activity391773--?
L-valine + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD432% of the activity compared to L-alanine651026-651026?
L-valine + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas luteoviolacea-low enzyme activity690575--?
L-valine + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Bothrops pirajai-substrate affinity in decreasing order: L-phenylalanine, L-tyrosine, L-tryptophan, L-leucine, L-methionine, L-isoleucine, L-valine, L-histidine667933--?
Nepsilon-acetyl-L-Lys + H2O + O26-acetylamino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD446% of the activity with L-Ala651026--?
Nepsilon-acetyl-L-lysine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Rhodococcus opacusQ8VPD446% of the activity compared to L-alanine651026-651026?
Nepsilon-acetyl-L-lysine + H2O + O22-oxo-6-acetylaminohexanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--?
O-carbamoyl-L-serine + H2O + O23-O-carbamoyl-2-keto-propionic acid + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.--391768--?
O-carbamoyl-L-serine + H2O + O23-O-carbamoyl-2-keto-propionic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus--391804--?
S-adenosyl-L-homocysteine + H2O + O24-thioadenosyl-2-oxobutyrate + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391796--?
S-adenosyl-L-homocysteine + H2O + O24-thioadenosyl-2-oxobutyrate + NH3 + H2O2
show the reaction diagram		Providencia rettgeri--391785---
S-adenosyl-L-homocysteine + H2O + O24-thioadenosyl-2-oxobutyrate + NH3 + H2O2
show the reaction diagram		Crotalus terrificus terrificus--391775---
S-allyl-L-cysteine + H2O + O22-oxo-3-(prop-2-en-1-ylsulfanyl)propanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-94% of the activity with L-methionine661038--?
S-allylmercapto-L-cysteine + H2O + O22-oxo-3-[(2-thioxoethyl)sulfanyl]propanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-26% of the activity with L-methionine661038--?
S-benzothiazolyl-L-cysteine + H2O + O23-(1,3-benzothiazol-3(2H)-ylsulfanyl)-2-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-161% of the activity with L-methionine661038--?
S-carbamoyl-L-cysteine + H2O + O23-thiocarbamoyl-2-keto-propionic acid + NH3 + H2O2
show the reaction diagram		Providencia sp., Proteus sp.--391768--?
S-carbamoyl-L-cysteine + H2O + O23-thiocarbamoyl-2-keto-propionic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus--391804--?
S-methylmercapto-L-cysteine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-66% of the activity with L-methionine661038--?
S-penta-1,3-dienylmercapto-L-cysteine + H2O + O2? + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-7% of the activity with L-methionine661038--?
S-propylmercapto-L-cysteine + H2O + O22-oxo-3-[(3-thioxopropyl)sulfanyl]propanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-16% of the activity with L-methionine661038--?
thyroxine + H2O + O23-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenylpyruvate] + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391769--?
triiodothyronine + H2O + O23-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391769--?
mandelic acid + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Rattus norvegicus--391802--?
additional information?-Bothrops atrox-substrate specificity, overview697450---
additional information?-Providencia rettgeri, Crotalus terrificus terrificus-investigation of oxidative deamination of sulfur amino acids391775---
additional information?-Providencia rettgeri-2 L-amino acid oxidases with different specificity: 1. oxidative deamination of aromatic carboxylic, sulfur containing imino and beta-hydroxy-L-amino acids, no activity to basic L-amino acids or L-citrulline, 2. oxidative deamination of L-arginine, L-histidine, L-ornithine, L-citrulline and L-lysine, with no affinity for any of the other L-amino acids tested391785---
additional information?-Eristocophis macmahonii-shows apoptosis-inducing activity in cell cultures391820---
additional information?-Agkistrodon contortrix laticinctus-shows apoptosis-inducing activity in cell cultures391821---
additional information?-Rattus norvegicus-not: alpha-hydroxyisobutyrate391766, 391769---
additional information?-Ophiophagus hannah-cytotoxic to different cell lines, resulting in loss of ability in attachment and inhibition of cell proliferation391826---
additional information?-snake-enzymatic properties of snake venom enzymes, mechanisms of enzyme-induced platelet aggregation and apoptosis391781---
additional information?-Corynebacterium sp.-not: proline391784---
additional information?-Protobothrops mucrosquamatus-not: proline391773---
additional information?-Mus musculusO09046reacts in decreasing order Phe, Met,Tyr, Cys, Leu, His, other amino acids391817---
additional information?-Ophiophagus hannah-induces human platelet aggregation391825---
additional information?-Crotalus adamanteus-S-carbamoyl-and S-thiocarbamoyl derivatives of L-cysteine391779---
additional information?-snake-overview on assays391771---
additional information?-Rattus norvegicus, Crotalus adamanteus, Agkistrodon piscivorus piscivorus-proline and N-methyl derivatives of leucine, methionine, homocysteine and S-benzylhomocysteine also oxidized391766---
additional information?-Rattus norvegicus-not: L-threonine391769---
additional information?-Corynebacterium sp.-not: L-threonine391784---
additional information?-Protobothrops mucrosquamatus-not: L-threonine391773---
additional information?-Proteus mirabilis-2 distinct L-amino acid oxidases with different specificity, 1. aliphatic or aromatic L-amino acids with non-polar side chains, 2. L-amino acids with positively charged side chains391786---
additional information?-Rattus norvegicus, Crotalus adamanteus, Agkistrodon piscivorus piscivorus-not: D-amino acids, N,N-dimethylleucine, alpha-aminoisobutyric acid391766---
additional information?-Crotalus adamanteus-has bactericidal activity391791---
additional information?-Trimeresurus flavoviridis, Protobothrops mucrosquamatus, Eristicophis macmahoni-induces apoptosis391781---
additional information?-Gloydius blomhoffi, Agkistrodon contortrix laticinctus-induction of apoptosis391781---
additional information?-Gloydius blomhoffi-the enzyme has anticoagulant activity that impairs the intrinsic clotting by inhibiting factor IX654872---
additional information?-Bothrops alternatus-the enzyme induces platelet aggregation and shows bactericidal activity against Escherichia coli and Staphylococcus aureus. The enzyme is slightly hemorrhagic and induces edema in mouse654954---
additional information?-Gloydius blomhoffi-enzyme possesses anticoagulant activity654872---
additional information?-Protobothrops jerdonii-formation of H2O2 is essential for the enzyme to induce platelet aggregation656581---
additional information?-Ophiophagus hannah, Eristicophis macmahoni-induces platelet aggregation391781---
additional information?-Gloydius blomhoffi-inhibits aggregation of platelets391781---
additional information?-Naja kaouthia-inhibits platelet aggregation391781---
additional information?-Mus musculus-the enzyme has a preference for aromatic amin acids, less than 5% of the activity with L-Phe: Gln, Gly, Asn, His, Leu, Glu, Lys656435---
additional information?-Crotalus durissus cascavella-enzyme induces dose-dependent platelet aggregation, which is abolished by catalase, inhibits the growth of Gram-negative and Gram-positive bacteria and has antileishmanic activity670964---
additional information?-Calloselasma rhodostoma-enzyme induces necrosis and apoptosis in Jurkat cells, in presence of catalase that scavenges H2O2 a switch to apoptosis is observed667235---
additional information?-Bothrops pirajai-enzyme induces time-dependent platelet aggregation, mouse paw edema, shows cytotoxic activity against Escherichia coli, Pseudomonas aeruginosa, Leishmania sp., and tumor cells667933---
additional information?-Sebastes schlegeliiA1IGW6enzyme shows potent antibacterial activity against fish pathogens668580---
additional information?-Aplysia punctataQ6T277enzyme shows tumoricidal activity670963---
additional information?-Aplysia californicaQ6IWZ0native enzyme inhibits the growth of Gram-positive and Gram-negative bacteria, including marine bacteria, and also inhibits the growth of yeasts and fungi. In minimal media, enzyme is bacteriostatic and not bactericidal, but becomes bactericidal in media enriched with Tryptone Peptone669658---
additional information?-Sebastes schlegeliiA1IGW6enzyme uses only L-lysine as substrate and is ineffective with other proteinaceous amino acids or with D-lysine668580---
additional information?-Aplysia californicaQ6IWZ0little or no activity with amino acids other than L-Arg, L-Lys669658---
additional information?-Aplysia punctataQ6T277no substrate: D-lysine670963---
additional information?-Vipera ammodytes ammodytes-active site and substrate binding structure, overview712998---
additional information?-Streptococcus oligofermentans-does not catalyze N-acetyL-L-cysteine and cis-4-hydroxyl-L-proline oxidation692863---
additional information?-Agkistrodon blomhoffi ussuriensis-does not hydrolyze casein and synthetic substrates including N-benzoyl-L-arginine ethylester or N-benzoyl-L-arginine p-nitroanilide695208---
additional information?-Synechococcus elongatus PCC 7942, Synechococcus cedrorum PCC 6908-high specificity for basic L-amino acids695281---
additional information?-Synechococcus elongatus PCC 6301P72346high specificity for basic L-amino acids695281---
additional information?-Naja oxiana-L-histidine, L-glutaminic acid, L-tyrosine, L-isoleucine, L-glutamine and L-lysine are poor substrates691918---
additional information?-Bothrops jararacaQ6TGQ9L-serine, L-proline, L-glycine, L-threonine and L-cysteine are not oxidized690684---
additional information?-Crotalus atrox, Laccaria bicolor, Hebeloma cylindrosporum, Hebeloma sp.-no cleavage of D-phenylalanine and L-aspartic acid694300---
additional information?-Sebastes schlegeliiA1IGW6SSAP catalyzes oxidation of only L-lysine and is ineffective with any other proteinaceous amino acids. No LAO activity is detected when L-lysine is replaced with D-lysine668580---
additional information?-Aplysia californicaQ6IWZ0bactericidal activity of the sea hare secretion against Escherichia coli, Vibrio harveyi, Staphylococcus aureus, and Pseudomonas aeruginosa695637---
additional information?-Daboia russellii siamensisQ4F867LAAO dose-dependently inhibits platelet aggregation and exhibits antibactericidal activity701333---
additional information?-Bungarus fasciatus-LAAO exhibits a cytotoxic effect on A549 cells and causes up to 41.2% apoptosis of A549 cells, overview701332---
additional information?-Bothropoides pauloensisB5AR80LAAO shows leishmanicidal, antitumoral and bactericidal activities dose dependently, overview. LAAO induces platelet aggregation in platelet-rich plasma which is inhibited by catalase696493---
additional information?-Mus musculus-mouse milk contains L-amino acid oxidase, a lactating mammary gland-specific protein, that displays antibacterial activity in vitro through the production of hydrogen peroxide from free amino acids697859---
additional information?-Myoxocephalus polyacanthocephalusB5U982MPLAO3 exhibits potent antibacterial activity against both Gram-positive and Gram-negative bacteria, and is most active against Aeromonas salmonicida strain JCM7874, which is attributable to H2O2, because the activity is completely lost in the presence of catalase697466---
additional information?-Gloydius blomhoffiQ90W54the LAO-containing fraction inhibits coagulation factor IX, and it prolongs the APTT, PT and fibrinogen clotting time and cleaves the Aalpha-chain of fibrinogen probably due to the presence of traces of a metalloproteinase in the fraction, overview. The mechanism for the anticoagulant activity of M-LAO fraction is not due to binding to factor IX. The fibrinogenolytic activity of the M-LAO fraction is independent of either LAO enzymatic activity or generated hydrogen peroxide698669---
additional information?-Bothrops jararaca-the venom enzyme from Bothrops jararaca show high antibacterial activity, e.g. against Staphylococcus aureus, via the produced H2O2, overview. The enzyme also shows hemolytic and leishmanicidal activity, overview701330---
additional information?-Aplysia californicaQ6IWZ0effect of pH on conversion of escapin intermediates to escapin end products, overview697333---
additional information?-Gloydius blomhoffiQ90W54L-amino acid oxidase is a dimeric glycosylated flavoenzyme that catalyses the oxidative deamination of an L-amino acid substrate to a 2-oxo acid along with the production of ammonia and hydrogen peroxide698669---
additional information?-Bungarus fasciatus-LAAO is very active against L-Tyr, L-Asp, L-Phe, L-Glu, L-Trp, L-His, L-Gln, L-Ile, L-Met, L-Leu and moderately active against L-Lys, L-Arg, L-Ala and L-Asn, overview701332---
additional information?-Bothropoides pauloensisB5AR80substrate specificity, no activity with L-Pro, L-Thr, L-Ser, and L-Cys, overview. Construction of a LAAO structural model of the stereochemistry of substrate binding by the enzyme, overview696493---
additional information?-Daboia russellii siamensisQ4F867substrate specificity, overview. No activity with L-Pro, L-Asn, Gly, L-Ser, and L-Cys. The enzyme shows no hemorrhagic activity701333---
additional information?-Bothrops jararaca-Bothrops jararaca venom induces programmed cell death in epimastigotes of Trypanosoma cruzi due to its L-AAO activity, L-AAO activity induces parasites cytoplasmic retraction, mitochondrial swelling and DNA fragmentation, overview. L-AAO produces H2O2, which is highly toxic713559---
additional information?-Crotalus atrox-substrate specificity, overview. L-Thr is a poor substrate713525---
additional information?-Pseudoalteromonas flavipulchra-the antibacterial protein is an L-amino acid oxidase with broad substrate specificity711872---
additional information?-Platichthys stellatusD2KWB6the enzyme shows antibacterial activity against Staphylococcus epidermidis, Staphylococcus aureus, and methicillin-resistant Staphylococcus aureus, overview711987---
additional information?-Bothrops marajoensis-the L-amino acid oxidase from Bothrops marajoensis is able to inhibit the growth of several microorganisms, including Staphylococcus aureus, Candida albicans, Pseudomonas aeruginosa,and Leishmania sp.. The enzyme inhibits the growth of promastigote forms of Leishmania amazonensis and Leishmania chagasi with IC50 values of 2.55 mg/mL and 2.86 mg/mL, respectively713558---
additional information?-Amanita phalloides-toxophallin induces chromatin condensation, as well as DNA and nucleus fragmentation, which are typical for apoptosis, effect towards human leukemia CEM-T4 and murine leukemia L1210 cells, overview, L-cysteine, L-glycine, L-proline, L-oxyproline, DL-serine, and DL-aspartic acid are no substrates. Toxophallin is also not active against benzylamine, ethanolamine, diethylamine, meta- and para-phenylendiamine, ortho-, meta- and paraaminophenols, or putrescin711980---
additional information?-Bothrops marajoensis-LAAO catalyzes the stereospecific oxidative deamination of an L-amino acid substrate, releasing the corresponding 2-oxo acid and resulting in the production of hydrogen peroxide and ammonia713558---
additional information?-Rhodococcus sp.-the enzyme from Rhodococcus sp. AIU Z-35-1 shows broad substrate specificity711874---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
an L-amino acid + H2O + O2a 2-oxo-acid + NH3 + H2O2
show the reaction diagram		Vipera ammodytes ammodytes-L-amino-acid oxidase catalyzes the oxidative deamination of a number of L-amino acids to their respective imino acids with concomitant hydrolysis to alpha-keto acids, together with the production of ammonia and hydrogen peroxide695361--
DL-asparagine + H2O + O22-oxosuccinamic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--
DL-leucine + H2O + O22-oxo-4-methylpentanoate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--
DL-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--
DL-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--
DL-norleucine + H2O + O22-oxocaproate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--
DL-threonine + H2O + O22-oxo-3-hydroxybutanoic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--
DL-tryptophan + H2O + O23-(1H-indol-3-yl)-2-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--
DL-valine + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942-first step in reaction sequence of formation of phenylacetic acid from L-phenylalanine391809--
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942-functional in photosynthetic and respiratory activities as well as in L-arginine degradation391806, 391810--
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Corynebacterium sp.-utilization of amino acids as nitrogen source391784--
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Chlamydomonas reinhardtii-operates as scavanger of ammonium from extracellular amino acids391814--
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Crotalus adamanteus-bactericidal action of L-amino acid oxidase391791--
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus elongatus PCC 7942-involved in the water-splitting reaction of photosystem II391805, 391807--
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Synechococcus sp.-involved in the water-splitting reaction of photosystem II391811--
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Mus musculusO09046responsible for killing bacteria in the mammary gland391817--
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		snake-biological functions of snake venom enzymes391781--
L-amino acid + H2O + O22-oxo acid + NH3 + H2O2
show the reaction diagram		Dolabella auricularia-cell death induced by the enzyme is of two types, one non-apoptotic and the other apoptotic. The effect is not dependent on the acute toxicity of H2O2655316--
L-arginine + H2O + O22-oxo-5-guanidinopentanoic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--
L-glutamic acid + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--
L-glutamic acid + H2O + O22-oxoglutarate + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--
L-glutamine + H2O + O22-oxo-4-carbamoylbutanoic acid + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--
L-histidine + H2O + O22-oxo-4-imidazolepropionic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--
L-isoleucine + H2O + O23-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram		Crotalus atrox--713525--
L-isoleucine + H2O + O23-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--
L-Leu + H2O + O24-methyl-2-oxo-pentanoic acid + NH3 + H2O2
show the reaction diagram		Mus musculus--697859--
L-Leu + H2O + O22-oxo-4-methylvaleric acid + NH3 + H2O2
show the reaction diagram		Agkistrodon blomhoffi ussuriensis--711329--
L-leucine + H2O + O22-oxo-4-methylpentanoate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--
L-leucine + H2O + O22-oxo-4-methylvaleric acid + NH3 + H2O2
show the reaction diagram		Bothrops marajoensis--713558--
L-leucine + H2O + O22-oxo-4-methylvaleric acid + NH3 + H2O2
show the reaction diagram		Bothrops jararaca--713559--
L-Lys + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Aplysia californicaQ6IWZ0-697333--
L-Lys + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Aplysia californicaQ6IWZ0the ink of sea hares contains escapin, an L-amino acid oxidase that metabolizes L-lysine, thereby producing a mixture that kills microbes and deters attacking predators. This secretion contains H2O2, ammonia, and an equilibrium mixture of socalled escapin intermediate product, EIP-K, that includes 6-amino-2-oxohexanoic acid and several other molecules. Components of the equilibrium mixture react nonenzymatically with H2O2 to form escapin end product, i.e. EEP-K, which contains 2-aminovaleric acid and 2-valerolactam. The proportions of the components in this equilibrium mixture change with pH, and this is biologically important because the secretion has pH 5 when released but becomes pH 8 when fully diluted in seawater, overview695637--
L-Lys + H2O + O26-amino-2-oxo-hexanoic acid + NH3 + H2O2
show the reaction diagram		Myoxocephalus polyacanthocephalusB5U982-697466--
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Rhodococcus sp.--711874--
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Amanita phalloides-low activity711980--
L-lysine + H2O + O26-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram		Sebastes schlegelii-strictly specific for711786--
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Crotalus atrox--713525--
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--
L-methionine + H2O + O24-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram		Amanita phalloides-preferred substrate711980--
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--
L-phenylalanine + H2O + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--
L-phenylalanine + O2phenylpyruvate + NH3 + H2O2
show the reaction diagram		Homo sapiens-inhibition of T cell proliferation through phenylalanine degradation699933activity measurement by measuring H2O2 production-
L-tryptophan + H2O + O23-(1H-indol-3-yl)-2-oxopropanoic acid + NH3 + H2O2
show the reaction diagram		Crotalus atrox--713525--
L-tyrosine + H2O + O24-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Pseudoalteromonas flavipulchra--711872--
L-tyrosine + H2O + O24-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram		Amanita phalloides--711980--
L-valine + H2O + O22-oxoisovalerate + NH3 + H2O2
show the reaction diagram		Crotalus atrox--713525--
additional information?-Trimeresurus flavoviridis, Protobothrops mucrosquamatus, Eristicophis macmahoni-induces apoptosis391781--
additional information?-Gloydius blomhoffi, Agkistrodon contortrix laticinctus-induction of apoptosis391781--
additional information?-Gloydius blomhoffi-the enzyme has anticoagulant activity that impairs the intrinsic clotting by inhibiting factor IX654872--
additional information?-Bothrops alternatus-the enzyme induces platelet aggregation and shows bactericidal activity against Escherichia coli and Staphylococcus aureus. The enzyme is slightly hemorrhagic and induces edema in mouse654954--
additional information?-Crotalus durissus cascavella-enzyme induces dose-dependent platelet aggregation, which is abolished by catalase, inhibits the growth of Gram-negative and Gram-positive bacteria and has antileishmanic activity670964--
additional information?-Calloselasma rhodostoma-enzyme induces necrosis and apoptosis in Jurkat cells, in presence of catalase that scavenges H2O2 a switch to apoptosis is observed667235--
additional information?-Bothrops pirajai-enzyme induces time-dependent platelet aggregation, mouse paw edema, shows cytotoxic activity against Escherichia coli, Pseudomonas aeruginosa, Leishmania sp., and tumor cells667933--
additional information?-Sebastes schlegeliiA1IGW6enzyme shows potent antibacterial activity against fish pathogens668580--
additional information?-Aplysia punctataQ6T277enzyme shows tumoricidal activity670963--
additional information?-Aplysia californicaQ6IWZ0native enzyme inhibits the growth of Gram-positive and Gram-negative bacteria, including marine bacteria, and also inhibits the growth of yeasts and fungi. In minimal media, enzyme is bacteriostatic and not bactericidal, but becomes bactericidal in media enriched with Tryptone Peptone669658--
additional information?-Aplysia californicaQ6IWZ0bactericidal activity of the sea hare secretion against Escherichia coli, Vibrio harveyi, Staphylococcus aureus, and Pseudomonas aeruginosa695637--
additional information?-Daboia russellii siamensisQ4F867LAAO dose-dependently inhibits platelet aggregation and exhibits antibactericidal activity701333--
additional information?-Bungarus fasciatus-LAAO exhibits a cytotoxic effect on A549 cells and causes up to 41.2% apoptosis of A549 cells, overview701332--
additional information?-Bothropoides pauloensisB5AR80LAAO shows leishmanicidal, antitumoral and bactericidal activities dose dependently, overview. LAAO induces platelet aggregation in platelet-rich plasma which is inhibited by catalase696493--
additional information?-Mus musculus-mouse milk contains L-amino acid oxidase, a lactating mammary gland-specific protein, that displays antibacterial activity in vitro through the production of hydrogen peroxide from free amino acids697859--
additional information?-Myoxocephalus polyacanthocephalusB5U982MPLAO3 exhibits potent antibacterial activity against both Gram-positive and Gram-negative bacteria, and is most active against Aeromonas salmonicida strain JCM7874, which is attributable to H2O2, because the activity is completely lost in the presence of catalase697466--
additional information?-Gloydius blomhoffiQ90W54the LAO-containing fraction inhibits coagulation factor IX, and it prolongs the APTT, PT and fibrinogen clotting time and cleaves the Aalpha-chain of fibrinogen probably due to the presence of traces of a metalloproteinase in the fraction, overview. The mechanism for the anticoagulant activity of M-LAO fraction is not due to binding to factor IX. The fibrinogenolytic activity of the M-LAO fraction is independent of either LAO enzymatic activity or generated hydrogen peroxide698669--
additional information?-Bothrops jararaca-the venom enzyme from Bothrops jararaca show high antibacterial activity, e.g. against Staphylococcus aureus, via the produced H2O2, overview. The enzyme also shows hemolytic and leishmanicidal activity, overview701330--
additional information?-Bothrops jararaca-Bothrops jararaca venom induces programmed cell death in epimastigotes of Trypanosoma cruzi due to its L-AAO activity, L-AAO activity induces parasites cytoplasmic retraction, mitochondrial swelling and DNA fragmentation, overview. L-AAO produces H2O2, which is highly toxic713559--
additional information?-Crotalus atrox-substrate specificity, overview. L-Thr is a poor substrate713525--
additional information?-Pseudoalteromonas flavipulchra-the antibacterial protein is an L-amino acid oxidase with broad substrate specificity711872--
additional information?-Platichthys stellatusD2KWB6the enzyme shows antibacterial activity against Staphylococcus epidermidis, Staphylococcus aureus, and methicillin-resistant Staphylococcus aureus, overview711987--
additional information?-Bothrops marajoensis-the L-amino acid oxidase from Bothrops marajoensis is able to inhibit the growth of several microorganisms, including Staphylococcus aureus, Candida albicans, Pseudomonas aeruginosa,and Leishmania sp.. The enzyme inhibits the growth of promastigote forms of Leishmania amazonensis and Leishmania chagasi with IC50 values of 2.55 mg/mL and 2.86 mg/mL, respectively713558--
additional information?-Amanita phalloides-toxophallin induces chromatin condensation, as well as DNA and nucleus fragmentation, which are typical for apoptosis, effect towards human leukemia CEM-T4 and murine leukemia L1210 cells, overview711980--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
FADCrotalus adamanteus-2 mol of FAD per mol of enzyme389803, 391766, 391770, 391774 2D-image
FADAgkistrodon piscivorus piscivorus-2 mol of FAD per mol of enzyme389803, 391766 2D-image
FADRattus norvegicus--391766 2D-image
FADOphiophagus hannah-2 mol of FAD per mol of enzyme391772 2D-image
FADNeurospora crassa-4 mol of FAD per mol of enzyme391787 2D-image
FADSynechococcus elongatus PCC 7942-1 mol of FAD per mol of enzyme391808 2D-image
FADChlamydomonas reinhardtii-non-covalently bound391814 2D-image
FADCalloselasma rhodostoma--391815 2D-image
FADBothrops sp.--391823 2D-image
FADBacillus carotarum-2 mol of FAD per mol of enzyme391824 2D-image
FADRhodococcus opacusQ8VPD4a homodimer complex containing 2 FAD molecules651026 2D-image
FADRhodococcus opacus-non-covalently bound667079 2D-image
FADSebastes schlegeliiA1IGW6; 668580 2D-image
FADAplysia californicaQ6IWZ0-669658 2D-image
FADRhodococcus opacus-; the whole cofactor is buried inside the protein and is not solvent accessible. The FAD-binding domain consists of three discontinuous regions of the structure: residues 4-51, 239-314 and 423-488. The main structural feature of this domain is a fivestranded beta-pleated sheet sandwiched between three alpha-helices and a four-stranded beta-pleated sheet. The FAD-binding domain corresponds to a general topology throughout the whole GR2-famil669894 2D-image
FADAplysia punctataQ6T277-670963 2D-image
FADBothrops jararacussuQ6TGQ9-690693 2D-image
FADBothrops moojeniQ6TGQ8-690693 2D-image
FADDaboia russellii russellii--692288 2D-image
FADSynechococcus cedrorum PCC 6908--695281 2D-image
FADSynechococcus elongatus PCC 6301P72346-695281 2D-image
FADSynechococcus elongatus PCC 7942--695281 2D-image
FADVipera ammodytes ammodytes-non-covalently bound695361 2D-image
FADBothropoides pauloensisB5AR80a flavoenzyme696493 2D-image
FADAgkistrodon blomhoffi ussuriensis--711329 2D-image
FADSebastes schlegelii--711786 2D-image
FADVipera ammodytes ammodytes-the FAD-binding domain includes residues 35-72, 239-318 and 446-486. The secondary structure elements of this domain are 4 alpha-helices712998 2D-image
FADCrotalus atrox--713525 2D-image
FADBothrops marajoensis--713558 2D-image
FADBothrops jararaca--713559 2D-image
FlavinGloydius blomhoffiQ90W54LAO is a flavoenzyme698669 2D-image
FlavinBothrops jararaca-a flavoenzyme701330 2D-image
FMNRattus norvegicus-6 mol of FMN per mol of enzyme391769, 391798 2D-image
FMNProtobothrops mucrosquamatus-2 mol of FMN per mol of enzyme391773 2D-image
FMNMeleagris gallopavo-FMN firmly bound to enzyme391789 2D-image
FMNRattus norvegicus--391802 2D-image
FMNCalloselasma rhodostoma-2 mol of FMN per mol of enzyme391819 2D-image
FMNProtobothrops jerdonii-contains 2 mol of FMN per mol of enzyme656581 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ca2+Agkistrodon blomhoffi ussuriensis-activates711329
Ce3+Agkistrodon blomhoffi ussuriensis-activates711329
Cl-Crotalus adamanteus-favors reaction391770
Co2+Agkistrodon blomhoffi ussuriensis-activates711329
Mg2+Agkistrodon blomhoffi ussuriensis-activates711329
Mn2+Protobothrops mucrosquamatus-MnCl2 inhibits391773
Mn2+Meleagris gallopavo-powerful activator391789
Nd3+Agkistrodon blomhoffi ussuriensis-activates711329
Tb3+Agkistrodon blomhoffi ussuriensis-activates711329
Zn2+Agkistrodon blomhoffi ussuriensis-Akbu-LAAO contains four Zn2þ per dimer, that are unessential for the hydrolytic activity of the enzyme. The apoenzyme shows 61% of maximal activity. The zinc ions probably help maintain the structural integrity of the enzyme711329
Zn2+Vipera ammodytes ammodytes-one Zn2+ ion is anchored to His75 at the beta-hairpin formed by the segment 73-86, which stabilizes the oligomeric state by bridging His75 and Glu279 of the adjacent protomer712998
Zn2+Crotalus atrox-required713525
Mn2+Agkistrodon blomhoffi ussuriensis-activates711329
additional informationMeleagris gallopavo-magnesium, iron and molybdene are no activators391789

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2-aminobenzoic acidDaboia russellii russellii-three and two binding sites in isoforms L1 and L2, respectively692288 2D-image
2-NaphtholSynechococcus elongatus PCC 7942--391808 2D-image
anthranilateCalloselasma rhodostoma-competitive391815 2D-image
anthranilateRhodococcus opacus--669894 2D-image
aromatic carboxylatesCrotalus adamanteus-competitive391799 2D-image
aspirinCrotalus durissus cascavella--670964 2D-image
AtebrineProteus sp., Providencia sp.--391768 2D-image
Ba2+Synechococcus elongatus PCC 7942--391808 2D-image
bathophenanthroline disulfonic acidSynechococcus elongatus PCC 7942--391808 2D-image
Benzenearsonic acidRattus norvegicus--391802 2D-image
BenzoateCrotalus adamanteus--391799 2D-image
BenzoateCrotalus adamanteus-and derivatives391800 2D-image
Benzoic acidAgkistrodon piscivorus piscivorus, Crotalus adamanteus, Rattus norvegicus--391766 2D-image
Benzoic acidProtobothrops mucrosquamatus--391773 2D-image
Butanedionesnake-good substrates but not poor substrates protect against inactivation391813 2D-image
Ca2+Synechococcus elongatus PCC 7942-CaCl2, Ca(OOCCH3)2391805 2D-image
Ca2+Synechococcus elongatus PCC 7942-inhibition can be relieved by L-arginine391806 2D-image
Ca2+Synechococcus elongatus PCC 7942--391808 2D-image
CaCl2Synechococcus cedrorum PCC 6908--695281 2D-image
CaCl2Synechococcus elongatus PCC 6301P72346-695281 2D-image
CaCl2Synechococcus elongatus PCC 7942--695281 2D-image
Cd2+Protobothrops mucrosquamatus-CdCl2391773 2D-image
Cd2+Synechococcus elongatus PCC 7942--391808 2D-image
ChloropromazineSynechococcus elongatus PCC 7942-inhibition can be relieved by L-arginine391806 2D-image
Co2+Synechococcus elongatus PCC 7942--391808 2D-image
Cu2+Meleagris gallopavo-in presence of the activator Mn2+391789 2D-image
Cu2+Synechococcus elongatus PCC 7942--391808 2D-image
CuSO4Rattus norvegicus--391766 2D-image
D-mandelateCrotalus adamanteus--391799 2D-image
EDTAChlamydomonas reinhardtii-10 mM, 90% inhibition391814 2D-image
EDTANaja atra-inhibits platelet aggregation induced by LAAO690221 2D-image
EMD 132338Naja atra-inhibits platelet aggregation induced by LAAO690221 2D-image
Gd3+Agkistrodon blomhoffi ussuriensis-inhibits 17% at 10 mM711329 2D-image
GlyRhodococcus opacusQ8VPD4competitive inhibition of reaction with L-Ala, does not reduce activity when 10 mM L-Phe is used as substrate651026 2D-image
glycineRhodococcus opacusQ8VPD4activity strongly decreased in glycine/NaOH-buffer, competitive inhibition, no inhibition, when 10 mM L-phenylanalnine is used as substrate651026 2D-image
HgClProteus sp., Providencia sp.--391768 2D-image
HgClProtobothrops mucrosquamatus--391773 2D-image
hydroxylamineChlamydomonas reinhardtii-5 mM, 75% inhibition391814 2D-image
IndomethacinCrotalus durissus cascavella--670964 2D-image
iodoacetamideProtobothrops mucrosquamatus--391773 2D-image
iodoacetic acidAgkistrodon piscivorus piscivorus, Crotalus adamanteus, Rattus norvegicus--391766 2D-image
K+Synechococcus elongatus PCC 7942-KCl, K(OOCH3)391805 2D-image
KCNProteus sp., Providencia sp.--391768 2D-image
KCNProtobothrops mucrosquamatus--391773 2D-image
KCNChlamydomonas reinhardtii-10 mM, complete inhibition391814 2D-image
L-alanineRhodococcus opacusQ8VPD4-653762 2D-image
L-arginineRhodococcus opacusQ8VPD4; pH 7.6, 30°C651026 2D-image
L-citrullineRhodococcus opacusQ8VPD4; pH 7.6, 30°C651026 2D-image
L-leucineRhodococcus opacusQ8VPD4; pH 7.6, 30°C651026 2D-image
L-lysineRhodococcus opacusQ8VPD4; pH 7.6, 30°C651026 2D-image
L-MandelateCrotalus adamanteus--391799 2D-image
L-methionineRhodococcus opacusQ8VPD4; pH 7.6, 30°C651026 2D-image
L-NorleucineRhodococcus opacusQ8VPD4; pH 7.6, 30°C651026 2D-image
L-ornithineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
L-phenylalanineRhodococcus opacusQ8VPD4; pH 7.6, 30°C651026 2D-image
L-serineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
L-tyrosineRhodococcus opacusQ8VPD4; pH 7.6, 30°C651026 2D-image
La3+Synechococcus elongatus PCC 7942-LaCl3, La(OOCCH3)3391805 2D-image
m-AminobenzoateCrotalus adamanteus--391799 2D-image
m-chlorobenzoateCrotalus adamanteus--391799 2D-image
m-chlorobenzoateGloydius blomhoffiQ90W54LAO inhibitor, does not inhibit the degradation of fibrinogen698669 2D-image
m-fluorobenzoateCrotalus adamanteus--391799 2D-image
m-HydroxybenzoateCrotalus adamanteus--391799 2D-image
m-NitrobenzoateCrotalus adamanteus--391799 2D-image
MandelateCrotalus adamanteus--391799 2D-image
Mg2+Synechococcus elongatus PCC 7942-EDTA, ATP and ADP, but not AMP can overcome inhibition391808 2D-image
Mn2+Synechococcus elongatus PCC 7942--391805, 391808 2D-image
N-acetyl-L-tryptophan amideDaboia russellii russellii-inhibition of both isoforms L1 and L2692288 2D-image
N-acetyltryptophanDaboia russellii russellii-inhibition of both isoforms L1 and L2692288 2D-image
Na+Synechococcus elongatus PCC 7942-sodium salts, order of effectiveness: SCN-, NO3-, Cl-, Br-, I-, F-, HCOO-, CH3COO-391805 2D-image
NaFChlamydomonas reinhardtii-10 mM, 85% inhibition391814 2D-image
NH4+Agkistrodon piscivorus piscivorus, Crotalus adamanteus, Rattus norvegicus-inhibition of amino acid oxidase activity, no inhibition of L-hydroxy acid oxidase activity391766 2D-image
NH4+Synechococcus elongatus PCC 7942--391805 2D-image
Ni2+Synechococcus elongatus PCC 7942--391808 2D-image
Nordihydroguaiaretic acidSynechococcus elongatus PCC 7942--391808 2D-image
o-aminobenzoateCrotalus adamanteus--391799 2D-image
o-aminobenzoic acidGloydius blomhoffiQ90W54LAO inhibitor, slightly inhibiting the degradation of fibrinogen698669 2D-image
o-chlorobenzoateCrotalus adamanteus--391799 2D-image
o-fluorobenzoateCrotalus adamanteus--391799 2D-image
o-hydroxybenzoateCrotalus adamanteus--391799 2D-image
o-mercaptobenzoateCrotalus adamanteus--391799 2D-image
o-NitrobenzoateCrotalus adamanteus--391799 2D-image
o-phenanthrolineSynechococcus elongatus PCC 7942--391808 2D-image
orthanilic acidCrotalus adamanteus--391799 2D-image
p-AminobenzoateCrotalus adamanteus--391799 2D-image
p-Aminobenzoic acidProtobothrops mucrosquamatus--391773 2D-image
p-ChlorobenzoateCrotalus adamanteus--391799 2D-image
p-chloromercuribenzoateProtobothrops mucrosquamatus--391773 2D-image
p-chloromercuribenzoateRattus norvegicus--391802 2D-image
p-fluorobenzoateCrotalus adamanteus--391799 2D-image
p-hydroxybenzoateCrotalus adamanteus--391799 2D-image
p-nitrobenzoateCrotalus adamanteus--391799 2D-image
quinine sulfateProteus sp., Providencia sp.--391768 2D-image
Sodium azideProteus sp., Providencia sp.-slight391768 2D-image
Sodium azideSynechococcus elongatus PCC 7942--391808 2D-image
Sr2+Synechococcus elongatus PCC 7942--391808 2D-image
ThiosemicarbazideChlamydomonas reinhardtii-5 mM, 40% inhibition391814 2D-image
TunicamycinCalloselasma rhodostoma-inhibits secretion of recombinant LAAO670798 2D-image
VinylglycineCrotalus adamanteus--391783 2D-image
Zn2+Synechococcus elongatus PCC 7942--391805, 391808 2D-image
ZnCl2Protobothrops mucrosquamatus--391773 2D-image
MnCl2Protobothrops mucrosquamatus--391773 2D-image
additional informationCrotalus adamanteus-good substrates, not poor substrates are inhibitors; substrate inhibition391770-
additional informationOphiophagus hannah-substrate inhibition391772-
additional informationCorynebacterium sp.-substrate inhibition391784-
additional informationCrotalus adamanteus-insensitive to KCN at 1 mM; substrate inhibition391791-
additional informationCrotalus adamanteus-substrate inhibition391800-
additional informationGallus gallus-naturally occuring inhibitors391801-
additional informationSynechococcus elongatus PCC 7942-inhibition by cations increases in alkaline pH, inhibition by anions increases in acidic pH391805-
additional informationsnake-not: 5,5-dithiobis-(2-nitrobenzoic acid), trinitrobenzene sulfonic acid391813-
additional informationSebastes schlegeliiA1IGW6catalase almost completely abolishs the antibacterial activity of SSAP, indicating that H2O2 is the mediator of the activity of SSAP668580-
additional informationNaja atra-LAAO has no activity on platelets in platelet-rich plasma. Catalase inhibits the platelet aggregation and platelet protein phosphorylation induced by LAAO690221-
additional informationPseudoalteromonas luteoviolacea-antimicrobial activity can be partially inhibited by catalase690575-
additional informationBothrops jararacussuQ6TGQ9catalase inhibits dose-dependent parasite killing690693-
additional informationBothrops moojeniQ6TGQ8catalase inhibits dose-dependent parasite killing690693-
additional informationBothrops jararaca-antiparasite effects are inhibited by catalase690856-
additional informationSebastes schlegelii-antibacterial activity of SSAP is completely abolished by addition of catalase691917-
additional informationNaja oxiana-the antibacterial and anti-aggregating activity of LAAO is abolished by catalase691918-
additional informationDaboia russellii russellii-initial uncompetitive inhibition of L1 followed by mixed inhibition at higher concentrations suggesting the existence of two different inhibitor-binding sites distinct from the substrate-binding site. In the case of L2, initial linear competitive inhibition followed by mixed inhibition suggesting the existence of two nonoverlapping inhibitor-binding sites, one of which is the substrate-binding site692288-
additional informationSebastes schlegelii-antibacterial activities are completely abolished by catalase692408-
additional informationBothrops moojeni-is inactivated by freezing or low pH. Bactericidal, antitumoral, trypanocidal, edematogenic, platelet-aggregating activities, and apoptotic DNA fragmentation in HL-60 cells are inhibited by catalase692650-
additional informationCalloselasma rhodostoma-catalase (1.5 micromol) at various concentrations of leucine does not completely inhibit cell death caused by LAAO (1.2 micromol) in leucine auxotrophic strain695276-
additional informationAmanita phalloides-no inhibition by caspase III inhibitor benzyloxycarbonyl-Asp(OMe)-fluoromethylketone711980-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
CaCl2Chlamydomonas reinhardtii-2 mM, 50% activation391814 2D-image
additional informationSebastes schlegelii-antibacterial activity of SSAP results from the generation of H2O2691917-
additional informationBothrops moojeni-the glycosylation site of the enzyme is not important for structural delineation of the active site692650-
additional informationStreptococcus oligofermentans-peptone up-regulates expression of the aaoSo gene692863-
additional informationHebeloma sp.-activities are the highest in mycelia grown in nitrogen-rich conditions694300-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.05-cysteineCorynebacterium sp.--391784 2D-image
3.1-djenkolic acidCrotalus terrificus terrificus--391775 2D-image
83-djenkolic acidProvidencia rettgeri--391775 2D-image
0.274-L-AlaRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
28.3-L-AlaBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.274-L-alanineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.31-L-alanineRhodococcus opacusQ8VPD4wild-type enzyme, 30°C, pH 7.6653762 2D-image
0.45-L-alanineRhodococcus opacusQ8VPD4recombinant enzyme, expressed in Streptomyces lividans, 30°C, pH 7.6653762 2D-image
5.12-L-alanineAgkistrodon blomhoffi ussuriensis--695208 2D-image
12.5-L-alanineCalloselasma rhodostoma--391819 2D-image
5-L-Aminobutyric acidCalloselasma rhodostoma--391819 2D-image
0.07-L-ArgRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
18.75-L-ArgBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.037-L-arginineBacillus carotarum--391824 2D-image
0.07-L-arginineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.27-L-arginineProvidencia rettgeri-fraction II391785 2D-image
2-L-arginineCalloselasma rhodostoma--391819 2D-image
2.33-L-arginineAgkistrodon blomhoffi ussuriensis--695208 2D-image
2.9-L-arginineMeleagris gallopavo--391789 2D-image
3-L-arginineSynechococcus elongatus PCC 7942--695281 2D-image
4-L-arginineSynechococcus cedrorum PCC 6908--695281 2D-image
5-L-arginineSynechococcus elongatus PCC 6301P72346-695281 2D-image
19.07-L-AsnBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.028-L-AspRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.04-L-AspBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.028-L-asparagineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.259-L-asparagineBacillus carotarum--391824 2D-image
0.36-L-asparagineAgkistrodon blomhoffi ussuriensis--695208 2D-image
2.5-L-asparagineCalloselasma rhodostoma--391819 2D-image
0.026-L-citrullineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
21.3-L-citrullineProvidencia rettgeri-fraction II391785 2D-image
4.5-L-cysteineCrotalus terrificus terrificus--391775 2D-image
5.3-L-cysteineProvidencia rettgeri--391775 2D-image
5-L-cystineCrotalus terrificus terrificus--391775 2D-image
0.085-L-GlnRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
5.88-L-GlnBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.411-L-GluRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
1.44-L-GluBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.411-L-Glutamic acidRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.085-L-glutamineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.34-L-glutamineBacillus carotarum--391824 2D-image
8-L-glutamineCalloselasma rhodostoma--391819 2D-image
4.84-L-HisBungarus fasciatus-pH 8.5, 25°C701332 2D-image
1.8-L-histidineProvidencia rettgeri-fraction II391785 2D-image
2.3-L-histidineOphiophagus hannahA8QL50-695209 2D-image
2.5-L-histidineCalloselasma rhodostoma--391819 2D-image
4.97-L-histidineAgkistrodon blomhoffi ussuriensis--695208 2D-image
6.2-L-histidineMeleagris gallopavo--391789 2D-image
1.3-L-homocysteineCrotalus terrificus terrificus, Providencia rettgeri--391775 2D-image
0.72-L-homocystineCrotalus terrificus terrificus--391775 2D-image
12.5-L-homocystineProvidencia rettgeri--391775 2D-image
1.64-L-IleBungarus fasciatus-pH 8.5, 25°C701332 2D-image
5.11-L-IleRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.00144-L-isoleucineDaboia russellii russellii-isoform L1692288 2D-image
0.00189-L-isoleucineDaboia russellii russellii-isoform L2692288 2D-image
0.8-L-isoleucineCalloselasma rhodostoma--391819 2D-image
2.9-L-isoleucineOphiophagus hannahA8QL50-695209 2D-image
4.02-L-isoleucineAgkistrodon blomhoffi ussuriensis--695208 2D-image
5.11-L-isoleucineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
71-L-isoleucineProvidencia rettgeri-fraction I391785 2D-image
0.028-L-LeuRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.25-L-LeuGloydius halys--654119 2D-image
2.1-L-LeuAgkistrodon blomhoffi ussuriensis-pH 4.7, 37°C711329 2D-image
60.7-L-LeuBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.028-L-leucineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.0465-L-leucineCrotalus durissus cascavella-pH 8.0, 37°C670964 2D-image
0.11-L-leucineAgkistrodon blomhoffi ussuriensis--695208 2D-image
0.14-L-leucineOphiophagus hannah--391772 2D-image
0.4-L-leucineMacrovipera lebetina-pH 8.5, 25°C670968 2D-image
0.56-L-leucineCalloselasma rhodostoma--391815 2D-image
0.6-L-leucineDaboia russellii russellii-isoform L2692288 2D-image
0.63-L-leucineCalloselasma rhodostoma--391819 2D-image
0.75-L-leucineNaja oxiana--691918 2D-image
0.75-L-leucineDaboia russellii russellii-isoform L1692288 2D-image
1-L-leucineGallus gallus--391801 2D-image
1.17-L-leucineProtobothrops mucrosquamatus--391773 2D-image
2.2-L-leucineOphiophagus hannahA8QL50-695209 2D-image
2.6-L-leucineProvidencia rettgeri-fraction I391785 2D-image
0.015-L-LysRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.16-L-LysMyoxocephalus polyacanthocephalusB5U98237°C, isozymes MPLAO1 and MPLAO3697466 2D-image
21.5-L-LysBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.015-L-lysineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.04-L-lysineCorynebacterium sp.--391784 2D-image
0.19-L-lysineSebastes schlegeliiA1IGW6; 37°C668580 2D-image
0.37-L-lysineSebastes schlegelii-pH 4.0, 37°C711786 2D-image
0.97-L-lysineAgkistrodon blomhoffi ussuriensis--695208 2D-image
1.6-L-lysineMeleagris gallopavo--391789 2D-image
2.6-L-lysineOphiophagus hannahA8QL50-695209 2D-image
10-L-lysineCalloselasma rhodostoma--391819 2D-image
23.2-L-lysineProvidencia rettgeri-fraction II391785 2D-image
0.039-L-MetRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
15-L-MetBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.039-L-methionineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.223-L-methionineDaboia russellii russellii-isoform L2692288 2D-image
0.24-L-methionineCalloselasma rhodostoma--391819 2D-image
0.297-L-methionineDaboia russellii russellii-isoform L1692288 2D-image
0.35-L-methionineCrotalus terrificus terrificus--391775 2D-image
0.65-L-methionineMacrovipera lebetina-pH 8.5, 25°C670968 2D-image
0.7-L-methionineOphiophagus hannahA8QL50-695209 2D-image
0.88-L-methionineAgkistrodon blomhoffi ussuriensis--695208 2D-image
0.885-L-methionineNaja oxiana--691918 2D-image
9.6-L-methionineProvidencia rettgeri--391775, 391785 2D-image
10-L-methionineMeleagris gallopavo--391789 2D-image
0.026-L-NorleucineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.13-L-NorleucineCalloselasma rhodostoma--391819 2D-image
0.91-L-norvalineCalloselasma rhodostoma--391819 2D-image
0.034-L-OrnRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.034-L-ornithineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
6.2-L-ornithineMeleagris gallopavo--391789 2D-image
13.3-L-ornithineCalloselasma rhodostoma--391819 2D-image
14.2-L-ornithineProvidencia rettgeri-fraction II391785 2D-image
0.022-L-PheRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.13-L-PheBungarus fasciatus-pH 8.5, 25°C701332 2D-image
6.5-L-PheMus musculus--656435 2D-image
0.011-L-phenylalanineCorynebacterium sp.--391784 2D-image
0.022-L-phenylalanineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.0493-L-phenylalanineDaboia russellii russellii-isoform L2692288 2D-image
0.05-L-phenylalanineCalloselasma rhodostoma--391819 2D-image
0.051-L-phenylalanineNaja oxiana--691918 2D-image
0.0665-L-phenylalanineDaboia russellii russellii-isoform L1692288 2D-image
0.16-L-phenylalanineNeurospora crassa--391788 2D-image
2.2-L-phenylalanineHebeloma sp.-strain SE5694300 2D-image
3.1-L-phenylalanineProvidencia rettgeri-fraction I391785 2D-image
3.5-L-phenylalanineMeleagris gallopavo--391789 2D-image
4.28-L-phenylalanineAgkistrodon blomhoffi ussuriensis--695208 2D-image
5-L-phenylalanineHebeloma sp.-strain F-NB01694300 2D-image
1.36-L-SerRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
1.36-L-serineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.27-L-TrpBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.08-L-tryptophanCalloselasma rhodostoma--391819 2D-image
0.147-L-tryptophanNaja oxiana--691918 2D-image
0.17-L-tryptophanMacrovipera lebetina-pH 8.5, 25°C670968 2D-image
0.211-L-tryptophanDaboia russellii russellii-isoform L1692288 2D-image
0.235-L-tryptophanDaboia russellii russellii-isoform L2692288 2D-image
2.2-L-tryptophanMeleagris gallopavo--391789 2D-image
2.3-L-tryptophanAgkistrodon blomhoffi ussuriensis--695208 2D-image
4.2-L-tryptophanProvidencia rettgeri-fraction I391785 2D-image
0.019-L-TyrRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.05-L-TyrBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.019-L-tyrosineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.052-L-tyrosineDaboia russellii russellii-isoform L1692288 2D-image
0.538-L-tyrosineDaboia russellii russellii-isoform L2692288 2D-image
1-L-tyrosineProvidencia rettgeri-fraction I391785 2D-image
1.57-L-tyrosineAgkistrodon blomhoffi ussuriensis--695208 2D-image
2.2-L-tyrosineMeleagris gallopavo--391789 2D-image
3.73-L-ValRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
0.27-L-valineAgkistrodon blomhoffi ussuriensis--695208 2D-image
3.73-L-valineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
1.2-O2Neurospora crassa--391788 2D-image
1.9-S-adenosyl-L-homocysteineCrotalus terrificus terrificus--391775 2D-image
24.8-S-adenosyl-L-homocysteineRattus norvegicus--391796 2D-image
100-S-adenosyl-L-homocysteine sulfoxideProvidencia rettgeri--391775 2D-image
14-S-adenosylhomocysteineProvidencia rettgeri--391785 2D-image
14-S-adenosylmethionineProvidencia rettgeri--391775 2D-image
2.2-S-ribosyl-L-homocysteineCrotalus terrificus terrificus--391775 2D-image
2.2-S-ribosyl-L-homocysteineChlamydomonas reinhardtii--391814 2D-image
13-S-ribosyl-L-homocysteineProvidencia rettgeri--391775 2D-image
45-methionine sulfoxideProvidencia rettgeri--391775 2D-image
additional information-additional informationCrotalus adamanteus-effect of pH on Km391793-
additional information-additional informationAplysia californicaQ6IWZ0kinetics697333-
additional information-additional informationCrotalus atrox-a chiral ligand exchange CE essay with zinc(II)-L-valine complex for determining enzyme kinetic constant of LAAO, method, overview713525-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
293-L-AlaBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.0522.1L-alanineRhodococcus opacusQ8VPD4wild-type enzyme653762 2D-image
0.0570.65L-alanineRhodococcus opacusQ8VPD4recombinant enzyme, expressed in and Streptomyces lividans, 30°C, pH 7.6653762 2D-image
26.89-L-alanineAgkistrodon blomhoffi ussuriensis--695208 2D-image
228.8-L-ArgBungarus fasciatus-pH 8.5, 25°C701332 2D-image
22.54-L-arginineAgkistrodon blomhoffi ussuriensis--695208 2D-image
84.08-L-AsnBungarus fasciatus-pH 8.5, 25°C701332 2D-image
47.49-L-AspBungarus fasciatus-pH 8.5, 25°C701332 2D-image
5.26-L-asparagineAgkistrodon blomhoffi ussuriensis--695208 2D-image
430.4-L-GlnBungarus fasciatus-pH 8.5, 25°C701332 2D-image
790.5-L-GluBungarus fasciatus-pH 8.5, 25°C701332 2D-image
483.1-L-HisBungarus fasciatus-pH 8.5, 25°C701332 2D-image
4.15-L-histidineAgkistrodon blomhoffi ussuriensis--695208 2D-image
66.7-L-IleBungarus fasciatus-pH 8.5, 25°C701332 2D-image
6.33-L-isoleucineAgkistrodon blomhoffi ussuriensis--695208 2D-image
26-L-lactic acidRattus norvegicus--391769 2D-image
31.1-L-LeuGloydius halys--654119 2D-image
1025-L-LeuBungarus fasciatus-pH 8.5, 25°C701332 2D-image
6.3-L-leucineRattus norvegicus--391769 2D-image
47.98-L-leucineNaja oxiana--691918 2D-image
48.22-L-leucineAgkistrodon blomhoffi ussuriensis--695208 2D-image
52-L-leucineMacrovipera lebetina-pH 8.5, 25°C670968 2D-image
86.6-L-leucineOphiophagus hannah--391772 2D-image
2.6-L-LysMyoxocephalus polyacanthocephalusB5U98237°C, isozyme MPLAO1697466 2D-image
4.7-L-LysMyoxocephalus polyacanthocephalusB5U98237°C, isozyme MPLAO3697466 2D-image
318.9-L-LysBungarus fasciatus-pH 8.5, 25°C701332 2D-image
10.51-L-lysineAgkistrodon blomhoffi ussuriensis--695208 2D-image
20.4-L-lysineSebastes schlegeliiA1IGW6; 37°C668580 2D-image
57.1-L-lysineSebastes schlegelii-pH 4.0, 37°C711786 2D-image
589.3-L-MetBungarus fasciatus-pH 8.5, 25°C701332 2D-image
0.21-L-methionineMacrovipera lebetina-pH 8.5, 25°C670968 2D-image
24.13-L-methionineAgkistrodon blomhoffi ussuriensis--695208 2D-image
66.26-L-methionineNaja oxiana--691918 2D-image
80.3-L-methionineMacrovipera lebetina-pH 8.5, 25°C670968 2D-image
142.6-L-PheBungarus fasciatus-pH 8.5, 25°C701332 2D-image
17.18-L-phenylalanineNaja oxiana--691918 2D-image
48.23-L-phenylalanineAgkistrodon blomhoffi ussuriensis--695208 2D-image
98.82-L-TrpBungarus fasciatus-pH 8.5, 25°C701332 2D-image
6.58-L-tryptophanAgkistrodon blomhoffi ussuriensis--695208 2D-image
42.6-L-tryptophanMacrovipera lebetina-pH 8.5, 25°C670968 2D-image
81.04-L-tryptophanNaja oxiana--691918 2D-image
100.6-L-TyrBungarus fasciatus-pH 8.5, 25°C701332 2D-image
8.42-L-tyrosineAgkistrodon blomhoffi ussuriensis--695208 2D-image
5.08-L-valineAgkistrodon blomhoffi ussuriensis--695208 2D-image
additional information-additional informationCrotalus adamanteus-mol amino acid/min x mol of enzyme bound FAD: 11000 L-arginine, 280 L-phenylalanine, 40 L-valine, 600 L-leucine391778-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.01189-2-aminobenzoic acidDaboia russellii russellii-isoform L2, free enzyme692288 2D-image
0.02544-2-aminobenzoic acideDaboia russellii russellii-isoform L2, enzyme-substrate complex692288-
1.7-BenzoateCrotalus adamanteus--391799 2D-image
11-D-mandelateCrotalus adamanteus--391799 2D-image
4.5-GlyRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
4.5-glycineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
221-L-alanineRhodococcus opacusQ8VPD4recombinant L-AAO, expressed in and Streptomyces lividans, 30°C, pH 7.6653762 2D-image
5.42-L-ArgRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
5.42-L-arginineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
20.6-L-citrullineRhodococcus opacusQ8VPD4pH 7.6, 30°C; pH 7.6, 30°C651026 2D-image
5.69-L-LeuRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
5.69-L-leucineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
63.7-L-LysRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
63.7-L-lysineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
11-L-MandelateCrotalus adamanteus--391799 2D-image
6.84-L-MetRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
6.84-L-methionineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
2.91-L-NorleucineRhodococcus opacusQ8VPD4pH 7.6, 30°C; pH 7.6, 30°C651026 2D-image
12.5-L-OrnRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
12.5-L-ornithineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
2.28-L-PheRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
2.28-L-phenylalanineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
192-L-SerRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
192-L-serineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
1.06-L-TyrRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
1.06-L-tyrosineRhodococcus opacusQ8VPD4pH 7.6, 30°C651026 2D-image
1.6-m-AminobenzoateCrotalus adamanteus--391799 2D-image
0.15-m-chlorobenzoateCrotalus adamanteus--391799 2D-image
0.37-m-fluorobenzoateCrotalus adamanteus--391799 2D-image
2.1-m-HydroxybenzoateCrotalus adamanteus--391799 2D-image
0.3788-N-acetyl-L-tryptophan amideDaboia russellii russellii-isoform L2, free enzyme692288 2D-image
0.3846-N-acetyl-L-tryptophan amideDaboia russellii russellii-isoform L1, enzyme-substrate complexe692288 2D-image
0.5916-N-acetyl-L-tryptophan amideDaboia russellii russellii-isoform L1, free enzyme692288 2D-image
0.7448-N-acetyl-L-tryptophan amideDaboia russellii russellii-isoform L2, enzyme-substrate complex692288 2D-image
0.0935-N-acetyltryptophanDaboia russellii russellii-isoform L1, enzyme-substrate complex692288 2D-image
0.1146-N-acetyltryptophanDaboia russellii russellii-isoform L2, free enzyme692288 2D-image
0.1275-N-acetyltryptophanDaboia russellii russellii-isoform L1, free enzyme692288 2D-image
0.2001-N-acetyltryptophanDaboia russellii russellii-isoform L2, enzyme-substrate complex692288 2D-image
0.42-o-aminobenzoateCrotalus adamanteus--391799 2D-image
1-o-chlorobenzoateCrotalus adamanteus--391799 2D-image
1.4-o-fluorobenzoateCrotalus adamanteus--391799 2D-image
2.2-o-hydroxybenzoateCrotalus adamanteus--391799 2D-image
1-o-mercaptobenzoateCrotalus adamanteus--391799 2D-image
0.86-o-NitrobenzoateCrotalus adamanteus--391799 2D-image
1.2-orthanilic acidCrotalus adamanteus--391799 2D-image
1.4-p-AminobenzoateCrotalus adamanteus--391799 2D-image
0.7-p-ChlorobenzoateCrotalus adamanteus--391799 2D-image
1.3-p-fluorobenzoateCrotalus adamanteus--391799 2D-image
2.3-p-hydroxybenzoateCrotalus adamanteus--391799 2D-image
2.3-p-nitrobenzoateCrotalus adamanteus--391799 2D-image
0.34-m-NitrobenzoateCrotalus adamanteus--391799 2D-image
additional information-additional informationRhodococcus opacusQ8VPD4wild-type L-AAO, no substrate inhibition up to 0.5 M L-alanine653762-

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1.1-CaCl2Synechococcus cedrorum PCC 6908, Synechococcus elongatus PCC 7942--695281 2D-image
1.6-CaCl2Synechococcus elongatus PCC 6301P72346-695281 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.01-Calloselasma rhodostoma-supernatant from the culture medium670798
0.24-Naja oxiana-activity against L-lysine691918
0.38-Naja oxiana-activity against L-glutamine691918
0.5-Naja oxiana-activity against L-isoleucine691918
0.67-Naja oxiana-activity against L-tyrosine691918
0.81-Naja oxiana-activity against L-glutaminic acid691918
1.19-Naja oxiana-activity against L-histidine691918
1.4-Chlamydomonas reinhardtii-glycine391814
1.45-Neurospora crassa--391787
1.56-Agkistrodon blomhoffi ussuriensis-crude venom695208
1.98-Rattus norvegicus--391802
3.15-Calloselasma rhodostoma-purified enzyme670798
3.8-Macrovipera lebetina-substrate L-isoleucine, pH 8.5, 25°C670968
4.4-Chlamydomonas reinhardtii-L-threonine391814
4.5-Macrovipera lebetina-substrate L-arginine, pH 8.5, 25°C; substrate L-phenylalanine, pH 8.5, 25°C670968
4.6-Rhodococcus opacusQ8VPD4homogenous enzyme, L-alanine as susbtrate, 30°C, pH 7.6651026
4.61-Rhodococcus opacusQ8VPD4-651026
4.9-Chlamydomonas reinhardtii-L-aspartate391814
5-Bothrops moojeni-with glycine or L-lysine as substrate692650
5.4-Rhodococcus opacusQ8VPD4wild-type and recombinant enzyme; wild-type enzyme: 76fold purification, recombinant enzyme, expressed in and Streptomyces lividans: 186fold purification, 30°C, pH 7.6653762
5.5-Macrovipera lebetina-substrate L-histidine, pH 8.5, 25°C670968
5.75-Naja oxiana-activity against L-arginine691918
6-Chlamydomonas reinhardtii-L-glutamate391814
6.5-Macrovipera lebetina-substrate L-leucine, pH 8.5, 25°C670968
6.94-Daboia russellii russellii-isoform L2692288
7.2-Macrovipera lebetina-substrate L-tryptophan, pH 8.5, 25°C670968
8.75-Naja oxiana-activity against L-tryptophan691918
8.96-Daboia russellii russellii-isoform L1692288
9-Agkistrodon blomhoffi ussuriensis-purified native enzyme, pH 4.7, 37°C711329
9.38-Naja oxiana-activity against L-phenylalanine691918
10-Bothrops moojeni-with L-glutamine as substrate692650
10.2-Sebastes schlegeliiA1IGW6; 37°C668580
12.5-Chlamydomonas reinhardtii-L-histidine391814
14.4-Chlamydomonas reinhardtii-L-valine391814
14.4-Macrovipera lebetina-substrate L-methionine, pH 8.5, 25°C670968
14.8-Chlamydomonas reinhardtii-L-tyrosine391814
15-Naja oxiana-activity against L-leucine691918
15.5-Chlamydomonas reinhardtii-L-tryptophan391814
16.6-Chlamydomonas reinhardtii-L-arginine391814
17-Chlamydomonas reinhardtii-L-isoleucine391814
17.4-Chlamydomonas reinhardtii-S-adenosy-L-cysteine391814
17.8-Chlamydomonas reinhardtii-L-alanine391814
18.4-Chlamydomonas reinhardtii-L-asparagine391814
18.8-Chlamydomonas reinhardtii-L-leucine391814
18.9-Chlamydomonas reinhardtii-L-lysine391814
20.4-Chlamydomonas reinhardtii-L-cystine391814
21-Naja oxiana-activity against L-methionine691918
21.4-Chlamydomonas reinhardtii-L-ornithine391814
24.2-Chlamydomonas reinhardtii-L-serine391814
24.3-Chlamydomonas reinhardtii-L-methionine391814
25.2-Chlamydomonas reinhardtii-S-adenosyl-L-homocysteine391814
26-Sebastes schlegelii-purified native enzyme, pH 4.0, 37°C711786
26.5-Chlamydomonas reinhardtii-L-ethionine; L-phenylalanine391814
30.5-Chlamydomonas reinhardtii-L-methionine sulfoximine391814
35-Bothrops moojeni-with L-serine as substrate692650
37.8-Bothrops moojeni--692650
39.5-Chlamydomonas reinhardtii-L-glutamine391814
40-Bothrops moojeni-with L-threonine or L-proline as substrate692650
60-Bothropoides pauloensisB5AR80purified enzyme, substrate L-Ala696493
79.92-Agkistrodon blomhoffi ussuriensis-51.3fold purified695208
87.5-Bothrops atrox-purified enzyme, substrate L-Leu697450
90-Bothrops moojeni-with L-arginine as substrate692650
110-Bothropoides pauloensisB5AR80purified enzyme, substrate L-Val696493
120-Synechococcus elongatus PCC 7942--391808
140-Bothrops moojeni-with L-histidine as substrate692650
140-Bothropoides pauloensisB5AR80purified enzyme, substrates L-Tyr or L-Glu696493
159-Agkistrodon contortrix laticinctus-L-alanine391821
230-Bothrops moojeni-with L-alanine as substrate692650
272-Agkistrodon contortrix laticinctus-L-histidine391821
282-Agkistrodon contortrix laticinctus-L-tryptophan391821
300-Bothrops pirajai-substrate L-histidine, 25°C, pH 7.2667933
310-Bothropoides pauloensisB5AR80purified enzyme, substrate L-Trp696493
335-Bothropoides pauloensisB5AR80purified enzyme, substrate L-His696493
340-Bothropoides pauloensisB5AR80purified enzyme, substrate L-Arg696493
410-Bothrops pirajai-substrate L-valine, 25°C, pH 7.2667933
430-Bothrops moojeni-with L-valine as substrate692650
435-Bothrops pirajai-substrate L-isoleucine, 25°C, pH 7.2667933
435-Bothrops moojeni-with L-isoleucine as substrate692650
440-Bothrops pirajai-substrate L-methionine, 25°C, pH 7.2667933
460-Bothrops moojeni-with L-methionine as substrate692650
480-Bothrops moojeni-with L-leucine as substrate692650
480-Bothropoides pauloensisB5AR80purified enzyme, substrate L-Ile696493
487.7-Bothrops moojeni-12.9fold purified692650
545-Bothropoides pauloensisB5AR80purified enzyme, substrate L-Phe696493
564-Agkistrodon contortrix laticinctus-L-leucine391821
575-Bothropoides pauloensisB5AR80purified enzyme, substrate L-Leu696493
580-Bothrops pirajai-substrate L-leucine, 25°C, pH 7.2667933
580-Bothropoides pauloensisB5AR80purified enzyme, substrate L-Met696493
585-Bothrops pirajai-substrate L-tryptophan, 25°C, pH 7.2667933
585-Bothrops moojeni-with L-tryptophan as substrate692650
590-Agkistrodon contortrix laticinctus-L-arginine391821
635-Bothrops moojeni-with L-tyrosine as substrate692650
665-Bothrops moojeni-with L-phenylalanine as substrate692650
685-Bothrops pirajai-substrate L-tyrosine, 25°C, pH 7.2667933
751-Agkistrodon contortrix laticinctus-L-valine391821
765-Bothrops pirajai-substrate L-phenylalanine, 25°C, pH 7.2667933
772-Agkistrodon contortrix laticinctus-L-methionine391821
776-Agkistrodon contortrix laticinctus-L-phenylalanine391821
868-Agkistrodon contortrix laticinctus-L-isoleucine391821
additional information-Rattus norvegicus--391769
additional information-Crotalus adamanteus--391770
additional information-snake-enzyme assays391771, 391781
additional information-Meleagris gallopavo--391789
additional information-Rattus norvegicus-enzyme assays391796
additional information-Bothrops sp.-activity in 19 different genus Bothrops venoms391823
additional information-Bothropoides pauloensisB5AR80substrate specificity, overview696493

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
4-Mus musculus--656435
4-Sebastes schlegelii-assay at711786
4.7-Agkistrodon blomhoffi ussuriensis-first optimum711329
5.2-Agkistrodon blomhoffi ussuriensis--695208
67.4Bothrops pirajai--667933
6.57Crotalus adamanteus--391791
6.5-Crotalus durissus cascavella--670964
6.6-Gallus gallus-L-leucine391801
77.6Proteus sp., Providencia sp.--391768
7-Protobothrops mucrosquamatus-L-Ile, L-Leu, L-Cys, L-Met, L-Phe, L-Tyr391773
7-Aplysia californicaQ6IWZ0bactericidal assay at695637
7-Rhodococcus sp.-assay at711874
7.27.5Agkistrodon piscivorus piscivorus, Crotalus adamanteus, Rattus norvegicus--391766
7.27.5Crotalus terrificus terrificus-2 optima, one between pH 7.2 and 7.5 and the other above pH 8.5, L-cysteine, S-adenosyl-L-homocysteine391775
7.2-Bothropoides pauloensisB5AR80assay at696493
7.2-Bothrops atrox-assay at697450
7.47.8Providencia rettgeri-S-ribosyl-L-homocysteine, S-adenosyl-L-homocysteine, S-adenosyl-L-methionine, L-methionine391775
7.4-Gloydius blomhoffiQ90W54assay at698669
7.5-Crotalus adamanteus-L-leucine391770
7.5-Crotalus adamanteus--391774
7.6-Rhodococcus opacusQ8VPD4assay at653762
88.4Crotalus terrificus terrificus-homocysteine, cysteine391775
88.5Bacillus carotarum-L-phenylalanine391824
89Rhodococcus opacusQ8VPD4; for 10 mM L-alanine, L-leucine, L-phenylalanine, the pH-profiles are almost identical651026
8-Rattus norvegicus-L-lactic acid391769
8-Protobothrops mucrosquamatus-L-His391773
8-Hebeloma cylindrosporum, Hebeloma sp., Laccaria bicolor--694300
8.1-Crotalus atrox-assay at713525
8.58.8Providencia rettgeri-djenkolic acid391775
8.5-Ophiophagus hannah--391772
8.5-Crotalus terrificus terrificus-2 optima, one between pH 7.2 and 7.5 and the other above pH 8.5, L-cysteine, S-adenosylhomocysteine, with S-adenosyl-homocysteine and djenkolic acid increase of activity beyond pH 8.5391775
8.5-Bungarus fasciatus-assay at701332
8.5-Agkistrodon blomhoffi ussuriensis-second optimum711329
8.5-Ophiophagus hannah-assay at711791
8.5-Bothrops jararaca-assay at713559
8.7-Rattus norvegicus-L-leucine391769
8.89.2Rattus norvegicus-S-adenosyl-L-homocysteine391796
8.8-Gloydius halys--654119
8.8-Daboia russellii siamensisQ4F867-701333
9-Protobothrops mucrosquamatus-L-Trp391773
9-Chlamydomonas reinhardtii-broad optimum391814
9.5-Neurospora crassa-L-phenylalanine391787

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
3.512Neurospora crassa-half maximal activity at pH 3.5 and 12391787
411Rhodococcus opacusQ8VPD4L-phenylalanine as substrate, pH 4: ca. 10% of the activity, pH 11: ca. 60% of the activity651026
4.49.6Agkistrodon blomhoffi ussuriensis--695208
4.510.5Bacillus carotarum--391824
4.510.5Rhodococcus opacusQ8VPD4L-alanine as substrate, pH 4.5, ca. 3% of the activity, pH 10.5, ca. 30% of the activity651026
4.58.5Aplysia californicaQ6IWZ0pH-profile, overview697333
5.58.5Rhodococcus sp.-activity assay range711874
610Hebeloma sp.--694300

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
20-Crotalus atrox--713525
25-Bothropoides pauloensisB5AR80assay at696493
25-Aplysia californicaQ6IWZ0assay at697333
25-Bungarus fasciatus-assay at701332
25-Daboia russellii siamensisQ4F867assay at701333
25-Bothrops jararaca-assay at713559
30-Rhodococcus opacusQ8VPD4assay at653762
30-Rhodococcus sp.-assay at711874
37-Bothrops pirajai--667933
37-Aplysia californicaQ6IWZ0bactericidal assay at695637
37-Myoxocephalus polyacanthocephalusB5U982assay at697466
37-Gloydius blomhoffiQ90W54assay at698669
37-Agkistrodon blomhoffi ussuriensis-assay at711329
37-Sebastes schlegelii-assay at711786
37-Ophiophagus hannah-assay at711791
49-Neurospora crassa-L-phenylalanine391787
50-Bacillus carotarum--391824

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
037Crotalus atrox-almost inactive at 0°C and 37°C713525

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
4.4-Bothrops atrox-isoelectric focussing697450
4.6-Aplysia punctataQ6T277calculated670963
4.7-Bothrops moojeni-isoelectric focusing692650
4.8-Rhodococcus opacusQ8VPD4isoelectric focusing, using a narrow pH-range of 4-6651026
4.9-Bothrops moojeni, Gloydius blomhoffi, Ophiophagus hannah--391781
4.9-Rhodococcus opacusQ8VPD4-651026
4.9-Bothrops alternatus--654954
4.9-Bothrops pirajai-isoelectric focusing667933
4.96-Myoxocephalus polyacanthocephalusB5U982mature MPLAO3, sequence calculation697466
5-Bothrops jararacaQ6TGQ9-690684
5.3-Platichthys stellatusD2KWB6isoelectric focusing711987
5.43-Crotalus durissus cascavella-isoelectric focusing670964
5.63-Bothrops jararacussuQ6TGQ9estimated690693
5.7-Bothrops jararaca-isoelectric focusing690856
5.8-Bothrops moojeniQ6TGQ8estimated690693
6.3-Bothropoides pauloensisB5AR80sequence calculation696493
6.9-Naja kaouthia--391781
8-Naja oxiana-isoelectric focusing691918
8.52-Synechococcus elongatus PCC 6301P72346-695281
9.4-Pseudoalteromonas flavipulchra-isoelectric focusing711872

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
B-cell lymphoma cellHomo sapiens-most primary mediastinal B-cell lymphoma (89%) are positive for enzyme immunostaining with strong intracytoplasmic staining in up to 100% of tumor cells, CD19(+) and CD19(-) cells display enzyme activity699933Manually annotated by BRENDA team
bloodCrotalus adamanteus--391792Manually annotated by BRENDA team
culture filtrateNeurospora crassa--391787Manually annotated by BRENDA team
epidermal mucusPlatichthys stellatusD2KWB6-711987Manually annotated by BRENDA team
follicular lymphoma cellHomo sapiens-64% positive immunostaining, no correlation between staining and histological grade of the follicular lymphoma, in small lymphocytic lymphoma 40% positive, restricted to paraimmunoblasts of proliferative centers, high enzyme activity, 7fold higher than in spleen lysate699933Manually annotated by BRENDA team
fruitbodyAmanita phalloides--711980Manually annotated by BRENDA team
gillSebastes schlegelii-dominantly expressed692408Manually annotated by BRENDA team
gillPlatichthys stellatusD2KWB6-711987Manually annotated by BRENDA team
histiocyteHomo sapiens-variable percentage of positive staining in several tissues, solid tumors, interfollicular areas, sinuses of reactive lymph nodes, red pulp of lymphoid follicles, thymus medulla, all lymphoma subtypes, particularly high enzyme expression in classical Hodgkin lymphoma and nodular lymphocyte predominant Hodgkin lymphoma cells699933Manually annotated by BRENDA team
inkAplysia californica--669658, 695637, 697333Manually annotated by BRENDA team
inkAplysia punctataQ6T277-670963Manually annotated by BRENDA team
kidneyRattus norvegicus--391766, 391769, 391794, 391796, 391798, 391802Manually annotated by BRENDA team
kidneySebastes schlegelii-weakly expressed692408Manually annotated by BRENDA team
leukocyteMus musculus--656435Manually annotated by BRENDA team
liverRattus norvegicus--391766, 391796Manually annotated by BRENDA team
liverMeleagris gallopavo--391789Manually annotated by BRENDA team
liverGallus gallus--391801Manually annotated by BRENDA team
lymphoma cellHomo sapiens-42% positive staining of classical Hodgkin lymphoma in Hodgkin and Reed Sternberg cells, 91% positive staining of nodular lymphocyte predominant Hodgkin lymphoma cells699933Manually annotated by BRENDA team
macrophageHomo sapiens-immunostaining in macrophages associated with non small-cell lung carcinomas, mesotheliomas, colorectal carcinomas and testicular germ cell tumors, positive staining in germinal centers of reactive lymph nodes and hyperplastic tonsils, and in the spleen699933Manually annotated by BRENDA team
mammary glandMus musculus-lactating, tissue-specific LAO697859Manually annotated by BRENDA team
myceliumNeurospora crassa--391787, 391788Manually annotated by BRENDA team
myceliumHebeloma sp.--694300Manually annotated by BRENDA team
ovarySebastes schlegelii-weakly expressed692408Manually annotated by BRENDA team
serumSebastes schlegelii--711786Manually annotated by BRENDA team
skinSebastes schlegeliiA1IGW6mucus; skin mucus668580Manually annotated by BRENDA team
skinSebastes schlegelii-mucus691917Manually annotated by BRENDA team
skinSebastes schlegelii-mucus, dominantly expressed. Quantity of SSAP mRNA in skin varies among individuals, ranging from 1.1 to 13.9 nanog/microg total RNA, although no relationship is found between the size of fish and gene expression692408Manually annotated by BRENDA team
skin mucusMyoxocephalus polyacanthocephalusB5U982isozymes MPLAO1, MPLAO2, and MPLAO3697466Manually annotated by BRENDA team
venomCrotalus adamanteus--391766, 391770, 391774, 391782, 391792, 391797, 391799, 391804Manually annotated by BRENDA team
venomAgkistrodon piscivorus piscivorus--391766Manually annotated by BRENDA team
venomOphiophagus hannah--391772, 695209, 711791Manually annotated by BRENDA team
venomProtobothrops mucrosquamatus--391773Manually annotated by BRENDA team
venomCrotalus terrificus terrificus, Providencia rettgeri--391775Manually annotated by BRENDA team
venomGloydius halys--654119Manually annotated by BRENDA team
venomViridovipera stejnegeriQ6WP39-654441Manually annotated by BRENDA team
venomGloydius blomhoffi--654872Manually annotated by BRENDA team
venomBothrops alternatus--654954Manually annotated by BRENDA team
venomProtobothrops jerdonii--656581Manually annotated by BRENDA team
venomBothrops pirajai--667933Manually annotated by BRENDA team
venomCrotalus durissus cascavella--670964Manually annotated by BRENDA team
venomMacrovipera lebetina--670968Manually annotated by BRENDA team
venomNaja atra--690221, 695209Manually annotated by BRENDA team
venomBothrops jararaca--690684, 690856, 701330, 713559Manually annotated by BRENDA team
venomBothrops moojeni--690693, 692650Manually annotated by BRENDA team
venomBothrops jararacussuQ6TGQ9-690693Manually annotated by BRENDA team
venomNaja oxiana--691918Manually annotated by BRENDA team
venomDaboia russellii russellii--692288Manually annotated by BRENDA team
venomDeinagkistrodon acutus--693949, 694317Manually annotated by BRENDA team
venomCrotalus atrox--694300, 713525Manually annotated by BRENDA team
venomAgkistrodon blomhoffi ussuriensis--695208, 711329Manually annotated by BRENDA team
venomBungarus fasciatus--695209, 701332Manually annotated by BRENDA team
venomBungarus multicinctusA8QL51-695209Manually annotated by BRENDA team
venomBothrops insularis--695212Manually annotated by BRENDA team
venomCalloselasma rhodostoma--695276Manually annotated by BRENDA team
venomVipera ammodytes ammodytes-five LAAO isozymes695361Manually annotated by BRENDA team
venomBothropoides pauloensisB5AR80-696493Manually annotated by BRENDA team
venomBothrops atrox--697450Manually annotated by BRENDA team
venomDaboia russellii siamensisQ4F867-701333Manually annotated by BRENDA team
venomVipera ammodytes ammodytes--712998Manually annotated by BRENDA team
venomBothrops marajoensis--713558Manually annotated by BRENDA team
venom glandBothrops jararacussuQ6TGQ9-690693Manually annotated by BRENDA team
venom glandBothrops moojeniQ6TGQ8-690693Manually annotated by BRENDA team
venom glandOphiophagus hannahA8QL50-695209Manually annotated by BRENDA team
milkMus musculus--697859Manually annotated by BRENDA team
additional informationSebastes schlegelii-no expression in muscle, stomach, intestine, liver and spleen692408Manually annotated by BRENDA team
additional informationHomo sapiens-enzyme expression in solid tumors only in 7.4% of 121 cases (5/10 mesotheliomas, 2/13 non small-cell carcinomas, 1/6 thyroid carcinoma, and 1/3 ovarian carcinoma), observations suggest aril in inflammatory processes, only occasional positive staining (17%) of non-mediastinal diffuse large B cell lymphoma; strong enzyme activity in L428 cell-line associated with detectable enzyme secretion, higher enzymatic activity than in SU-DHL-4 cells, higher enzyme activity in KM-H2 cell line than in Su-DHL-4 cells but lower than in L428 cells, total tumor cell lysate with negligible enzyme activity, CD19(+) fraction of marginal zone lymphoma cell with negligible enzyme activity, some activity in CD19(-) stromal cells699933Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cell envelopeProteus mirabilis--30313391786Manually annotated by BRENDA team
cytoplasmic membraneProteus sp., Providencia sp.-constituent part of-391768Manually annotated by BRENDA team
extracellularAplysia californicaQ6IWZ0--669658Manually annotated by BRENDA team
extracellularCalloselasma rhodostoma---670798Manually annotated by BRENDA team
extracellularVipera ammodytes ammodytes-venom-695361Manually annotated by BRENDA team
extracellularAplysia californica-defensive ink-695637, 697333Manually annotated by BRENDA team
extracellularBothropoides pauloensisB5AR80venom-696493Manually annotated by BRENDA team
extracellularBothrops atrox-venom-697450Manually annotated by BRENDA team
extracellularMyoxocephalus polyacanthocephalusB5U982skin mucus, isozyme MPLAO3 contains a signal peptide, comprising residues Met1-Ala26-697466Manually annotated by BRENDA team
extracellularMus musculus-milk-697859Manually annotated by BRENDA team
extracellularBothrops jararaca-venom-701330Manually annotated by BRENDA team
extracellularBungarus fasciatus-venom-701332Manually annotated by BRENDA team
extracellularDaboia russellii siamensisQ4F867venom-701333Manually annotated by BRENDA team
extracellularAgkistrodon blomhoffi ussuriensis---711329Manually annotated by BRENDA team
extracellularPlatichthys stellatusD2KWB6--711987Manually annotated by BRENDA team
extracellularVipera ammodytes ammodytes---712998Manually annotated by BRENDA team
extracellularCrotalus atrox---713525Manually annotated by BRENDA team
extracellularBothrops marajoensis---713558Manually annotated by BRENDA team
extracellularBothrops jararaca---713559Manually annotated by BRENDA team
lysosomeMus musculus--5764656435Manually annotated by BRENDA team
membraneSynechococcus elongatus PCC 7942-enzyme is part of photosystem II particles16020391807Manually annotated by BRENDA team
membraneSynechococcus elongatus PCC 7942-photosynthetic membranes16020391809Manually annotated by BRENDA team
mitochondrionMeleagris gallopavo--5739391789Manually annotated by BRENDA team
mitochondrionRattus norvegicus--5739391802Manually annotated by BRENDA team
periplasmChlamydomonas reinhardtii---391814Manually annotated by BRENDA team
periplasmSynechococcus cedrorum PCC 6908---695281Manually annotated by BRENDA team
periplasmSynechococcus elongatus PCC 6301P72346--695281Manually annotated by BRENDA team
periplasmSynechococcus elongatus PCC 7942---695281Manually annotated by BRENDA team
peroxisomeRattus norvegicus--5777391769, 391794Manually annotated by BRENDA team
solubleCorynebacterium sp.---391784Manually annotated by BRENDA team
solubleNeurospora crassa---391787Manually annotated by BRENDA team
solubleRattus norvegicus---391794, 391802Manually annotated by BRENDA team
solubleSynechococcus cedrorum PCC 6908---695281Manually annotated by BRENDA team
solubleSynechococcus elongatus PCC 6301P72346--695281Manually annotated by BRENDA team
solubleSynechococcus elongatus PCC 7942---695281Manually annotated by BRENDA team
spheroplastSynechococcus cedrorum PCC 6908---695281Manually annotated by BRENDA team
spheroplastSynechococcus elongatus PCC 6301P72346--695281Manually annotated by BRENDA team
spheroplastSynechococcus elongatus PCC 7942---695281Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
4e0v, downloadSCOP (4e0v)CATH (4e0v)Bothrops jararacussu
1f8s, downloadSCOP (1f8s)CATH (1f8s)Calloselasma rhodostoma
2iid, downloadSCOP (2iid)CATH (2iid)Calloselasma rhodostoma
1tdk, downloadSCOP (1tdk)CATH (1tdk)Gloydius blomhoffii
1tdn, downloadSCOP (1tdn)CATH (1tdn)Gloydius blomhoffii
1tdo, downloadSCOP (1tdo)CATH (1tdo)Gloydius blomhoffii
1reo, downloadSCOP (1reo)CATH (1reo)Gloydius halys
2jae, downloadSCOP (2jae)CATH (2jae)Rhodococcus opacus
2jb1, downloadSCOP (2jb1)CATH (2jb1)Rhodococcus opacus
2jb2, downloadSCOP (2jb2)CATH (2jb2)Rhodococcus opacus
2jb3, downloadSCOP (2jb3)CATH (2jb3)Rhodococcus opacus

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
12000-Agkistrodon contortrix laticinctus-gel filtration391821
53000-Sebastes schlegelii-Western blotting692408
53780-Bothrops moojeniQ6TGQ8sequence analysis690693
54130-Synechococcus elongatus PCC 6301P72346sequence analysis695281
54760-Bothrops jararacussuQ6TGQ9sequence analysis690693
54770-Bothrops jararaca-sequence analysis690856
59000-Eristocophis macmahonii-matrix-assisted laser desorption/ionization mass spectroscopy391820
60000-Aplysia californicaQ6IWZ0gel filtration669658
60700-Gloydius halys-MALDI-TOF mass spectrometry654119
68000-Crotalus durissus cascavella-gel filtration670964
68000-Bothrops insularis-HPLC695212
70000-Bungarus fasciatus-gel filtration701332
96000-Deinagkistrodon acutus-gel filtration, mass spectrometry694317
98000-Synechococcus elongatus PCC 7942-gel filtration391808
99000-Rhodococcus opacusQ8VPD4gel filtartion; gel filtration651026
102000115000Bacillus carotarum-gel filtration, native PAGE391824
104000-Rhodococcus opacusQ8VPD4MALDI-TOF/MS651026
108800-Agkistrodon blomhoffi ussuriensis-gel filtration695208
110000-Protobothrops jerdonii-gel filtration656581
110000-Pseudoalteromonas luteoviolacea-SDS-PAGE690575
110000-Naja oxiana-gel filtration691918
112000-Naja kaouthia--391781
113000-Mus musculusO09046gel filtration391817
113000-Mus musculus-mammary gland-specific isozyme, gel filtration697859
120000-Agkistrodon contortrix laticinctus--391781
120000-Bothrops alternatus-gel filtration654954
120000-Sebastes schlegeliiA1IGW6gel filtration; gel filtration668580
120000-Daboia russellii siamensisQ4F867gel filtration701333
124400-Agkistrodon blomhoffi ussuriensis-gel filtration711329
125000-Bothrops jararacaQ6TGQ9gel filtration690684
128000153000Crotalus adamanteus-approach to equilibrium method391774
130000140000Corynebacterium sp.-gel filtration391784
130000140000Crotalus adamanteus-sedimentation equilibrium391797
130000-Crotalus adamanteus--391770, 391774
130000-Bothrops pirajai-gel filtration667933
130800-Bothrops moojeni-mass spectrometry692650
132000-Calloselasma rhodostoma, Eristicophis macmahoni--391781
132000-Calloselasma rhodostoma-gel filtration391819
135000-Ophiophagus hannah--391781
135000-Ophiophagus hannah-gel filtration391825
138000-Rattus norvegicus-calculation from diffusion constant, sedimentation coefficient and FAD content391766
140000-Ophiophagus hannah-gel filtration391772
140000-Protobothrops mucrosquamatus-gel filtration391773
140000-Bothrops moojeni, Crotalus atrox, Protobothrops mucrosquamatus--391781
140000-Macrovipera lebetina-or above, gel filtration670968
140000-Myoxocephalus polyacanthocephalusB5U982isozyme MPLAO3, gel filtration697466
142000-Pseudechis australis--391781
145000-Myoxocephalus polyacanthocephalusB5U982isozyme MPLAO1, gel filtration697466
150000-Agkistrodon piscivorus piscivorus-approach to equilibrium method391766
150000-Ophiophagus hannah-gel filtration391826
160000-Sebastes schlegelii-gel filtration711786
280000-Myoxocephalus polyacanthocephalusB5U982isozyme MPLAO2, peak 1, gel filtration697466
300000-Neurospora crassa-disc gel electrophoresis, linear acrylamide concentration391787
310000314000Rattus norvegicus-high speed equilibrium method, gel filtration391769, 391798
600000-Myoxocephalus polyacanthocephalusB5U982isozyme MPLAO2, peak 2, gel filtration697466
9000001000000Chlamydomonas reinhardtii-form Malpha, gel filtration, sedimentation equilibrium391814
12000001300000Chlamydomonas reinhardtii-form Mbeta, gel filtration, sedimentation equilibrium391814

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Rhodococcus opacusQ8VPD4x * 53200, SDS-PAGE651026
?Calloselasma rhodostoma-x * 62000, SDS-PAGE670798
?Aplysia punctataQ6T277x * 60000, SDS-PAGE, x * 60167, calculated670963
?Streptococcus oligofermentans-x * 43000, SDS-PAGE692863
?Vipera ammodytes ammodytes-x * 55000, LAAO I, SDS-PAGE695361
?Bothrops atrox-x * 67000, SDS-PAGE697450
?Mus musculus-x * 58000, mammary gland-specific isozyme, SDS-PAGE697859
?Gloydius blomhoffiQ90W54x * 60000, SDS-PAGE698669
?Bothrops jararaca-x * 38200, deglycosylated enzyme, SDS-PAGE701330
?Pseudoalteromonas flavipulchra-x * 60000, SDS-PAGE711872
?Platichthys stellatusD2KWB6x * 52000, SDS-PAGE, 6 m urea ?PAGE, and 2D-PAGE711987
?Bothrops marajoensis-x * 72000, SDS-PAGE713558
dimerOphiophagus hannah-2 * 68000, SDS-PAGE391772
dimerProtobothrops mucrosquamatus-2 * 70000, SDS-PAGE391773
dimerAgkistrodon contortrix laticinctus-2 * 60000391781
dimerBothrops moojeni-2 * 69000391781
dimerCalloselasma rhodostoma-2 * 66000391781
dimerCrotalus adamanteus-2 * 58700391781
dimerCrotalus atrox-2 * 69000391781
dimerEristicophis macmahoni-2 * 66000391781
dimerNaja kaouthia-2 * 57400391781
dimerOphiophagus hannah-2 * 65000391781
dimerProtobothrops mucrosquamatus-2 * 70000391781
dimerPseudechis australis-2 * 56000391781
dimerCrotalus adamanteus-2 * 70000, sedimentation equilibrium in presence of 6 M guanidine hydrochloride, 2 types of polypeptide chains391797
dimerSynechococcus elongatus PCC 7942-2 * 49000, SDS-PAGE391808
dimerMus musculusO090462 * 60000, SDS-PAGE391817
dimerCalloselasma rhodostoma-2 * 66000, SDS-PAGE391819
dimerAgkistrodon contortrix laticinctus-2 * 60000, SDS-PAGE391821
dimerBacillus carotarum-2 * 54000, SDS-PAGE391824
dimerOphiophagus hannah-2 * 65000-70000, SDS-PAGE391825, 391826
dimerRhodococcus opacusQ8VPD42 * 53000, SDS-PAGE, 2 * 54000, MALDI-TOF/MS, correlates with a homodimer containing 2 FAD molecules651026
dimerBothrops alternatus-2 * 66000, SDS-PAGE654954
dimerProtobothrops jerdonii-2 * 55000, SDS-PAGE656581
dimerRhodococcus opacus-2 * 542000, calculated and crystallization data667079
dimerBothrops pirajai-2 * 66000, SDS-PAGE667933
dimerSebastes schlegeliiA1IGW62 * 53000, SDS-PAGE668580
dimerMacrovipera lebetina-2 * 60900, MALDI-TOF, 2 * 66000, SDS-PAGE670968
dimerNaja oxiana-gel filtration691918
dimerAgkistrodon blomhoffi ussuriensis-2 * 60000, SDS-PAGE under reducing conditions, 2 * 58000, SDS-PAGE under nonreducing conditions695208
dimerMyoxocephalus polyacanthocephalusB5U982x * 58000, isozyme MPLAO1, SDS-PAGE, x * 56000, isozyme MPLAO3, SDS-PAGE, x * 54769, mature MPLAO3, sequence calculation697466
dimer or trimerSebastes schlegelii-x * 53000, SDS-APGE711786
homodimerSebastes schlegeliiA1IGW62 * 53000, SDS-PAGE, 2 * 55261, sequence analysis668580
homodimerRhodococcus opacus-high-resolution669894
homodimerCalloselasma rhodostoma-2 * 60000, SDS-PAGE670798
homodimerBothrops jararacaQ6TGQ92 * 60000, SDS-PAGE690684
homodimerBothrops moojeni-2 * 64889, mass spectrometry, 1 * 66000, SDS-PAGE692650
homodimerDeinagkistrodon acutus-SDS-PAGE694317
homodimerBothropoides pauloensisB5AR802 * 65000, SDS-PAGE, 2 * 58000, about, sequence calculation696493
homodimerDaboia russellii siamensisQ4F8672 * 58000, SDS-PAGE701333
homodimerAgkistrodon blomhoffi ussuriensis-2 * 65000, SDS-PAGE711329
monomerAplysia californicaQ6IWZ01 * 60000, SDS-PAGE669658
monomerPseudoalteromonas luteoviolacea-1 * 110000, SDS-PAGE690575
monomerBothrops jararaca-1 * 60000, SDS-PAGE690856
monomerNaja oxiana-1 * 57000, SDS-PAGE691918
monomerDaboia russellii russellii-1 * 60000-63000, purified isoforms L1 and L2, size exclusion HPLC and SDS-PAGE692288
monomerSebastes schlegelii-1 * 53000, SDS-PAGE692408
monomerOphiophagus hannahA8QL501 * 64000, SDS-PAGE under non-reducing conditions, 1 * 67000, SDS-PAGE under reducing conditions, 1 * 53686, sequence analysis695209
oligomerChlamydomonas reinhardtii-Malpha, ? * 66000, Mbeta, ? * 66000 + ? * 135000, latter polypeptide not required for amino acid oxidase activity391814
monomerBungarus fasciatus-1 * 55000, SDS-PAGE701332
additional informationsnake-overview on structural properties391781
additional informationVipera ammodytes ammodytes-peptide mapping by mass spectrometry695361
additional informationBothropoides pauloensisB5AR80structure analysis and molecular dynamics simulation, overview696493
additional informationBothrops atrox-peptide mapping697450
additional informationMyoxocephalus polyacanthocephalusB5U982isozyme MPLAO3 contains a signal peptide, comprising residues Met1-Ala26, and the mature protein, Val28-Phe520, peptide mapping and sequencing of isozymes MPLAO3 and MPLAO1697466
additional informationAmanita phalloides-toxophallin peptide mapping and sequence analysis by MALDI-TOF mass spectrometry, overview711980
additional informationVipera ammodytes ammodytes-LAAO comprises the FAD-binding domain, the substrate binding domain, and the alpha-helical domain, the substrate binding domain is made up by residues 5-25, 73-129, 233-236 and 323-420, and contains 4 alpha-helices, formed by residues 16-25, 96-104, 375-383 and 386-401, and 11 beta-strands, residues 74-77, 82-85, 109-112, 120-123, 126-129, 233-236, 324-331, 345-347, 354-356, 367-374 and 412-419712998

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
glycoproteinAplysia californicaQ6IWZ0sequence contains one potential glycosylation site. Glycosylation is not essential for antimicrobial activity669658
proteolytic modificationAplysia californicaQ6IWZ0sequence contains a signal peptide of 18 amino acids669658
glycoproteinAplysia punctataQ6T277weakly glycosylated, sequence lacks classical N-glycosylation sites670963
flavoproteinBothropoides pauloensisB5AR80-696493
glycoproteinBothropoides pauloensisB5AR80-696493
glycoproteinBothrops alternatus-deglycosylation does not alter the enzymatic activity of the acid glycoprotein654954
glycoproteinBothrops atrox--697450
flavoproteinBothrops jararaca--701330
glycoproteinBothrops jararaca--701330
glycoproteinBothrops pirajai-deglycosylation does not alter enzymatic activity667933
glycoproteinCalloselasma rhodostoma-glycan is a bis-sialylated, biantennary, core-fucosylated dodecasaccharide391816
glycoproteinCalloselasma rhodostoma--391818, 391819, 670798
glycoproteinCalloselasma rhodostoma-desialysation reduces cytotoxicity of enzyme. Glycan moiety of enzyme is involved in binding and internalization to Jurkat cells667235
glycoproteinChlamydomonas reinhardtii-both polypeptide chains are glycosylated391814
glycoproteinCrotalus adamanteus-2-5% carbohydrate, including sialic acid391770
glycoproteinCrotalus adamanteus--391781, 391797
flavoproteinGloydius blomhoffiQ90W54-698669
glycoproteinMus musculus-N-linked glycosylation656435
glycoproteinOphiophagus hannah-3.8% carbohydrate391772
glycoproteinOphiophagus hannah--391781, 391826
glycoproteinSebastes schlegeliiA1IGW6protein contains N-linked glycochains668580
glycoproteinVipera ammodytes ammodytes-an N-acetylglucosamine group bound to the Asn172 side chain712998

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Agkistrodon contortrix laticinctus-391821
in complex with substrate L-phenylalanineCalloselasma rhodostoma-669893
in presence of citrate and o-aminobenzoate, comparison with D-amino acid oxidasesCalloselasma rhodostoma-391818
-Crotalus adamanteus-391766, 391770, 391774
hanging drop vapour-diffusion methodGloydius halys-654119
-Rattus norvegicus-391766, 391769, 391802
-Rhodococcus opacus-667079
; as HgCl2-derivative, native protein and in complex with L-alanine, L-phenylalanine or o-aminobenzoateRhodococcus opacus-669894
native isozyme LAAO I from venom, sitting drop vapour-diffusion method, mixing of 0.001 ml of protein solution with 10 mg/ml protein with 0.001 ml of a precipitant solution consisting of 16% w/v PEG 3350 and 0.04 M zinc acetate against 1 ml of reservoir solution at 20°C for 2 days, X-ray diffraction structure determination and analysis at 2.6 A resolutionVipera ammodytes ammodytes-695361
purified native enzyme by sitting drop vapour diffusion method, using a protein concentration of 10 mg/ml, with 0.04 M zinc acetate and 16% w/v PEG 3350 as the precipitant, X-ray diffraction structure determination and analysis at 2.57 A resolutionVipera ammodytes ammodytes-712998

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
4-Bothrops moojeni-at a pH below 4, enzymatic activity is completely lost692650
5-Protobothrops mucrosquamatus-4°C, 24 h, complete inactivation391773
5.57Rhodococcus sp.-40°C, 60 min, loss of about 20-30% activity711874
6.58.8Daboia russellii russellii-both isoforms retain 100% activity, drastic inactivation above and below this range692288
78Protobothrops mucrosquamatus-4°C, 24 h, stable391773
78.5Rhodococcus sp.-40°C, 60 min, highly stable711874
7-Crotalus adamanteus-reversible inactivation: at pH near neutrality change into inactive configuration, regaining of active configuration on lowering the pH, monovalent anions, substrate and substrate analogs prevent inactivation391782
7-Calloselasma rhodostoma-at pH above neutrality reversible inactivation391815
9-Ophiophagus hannah-25°C, 1 h stable; 25°C, 5 min, 47% loss of activity, complete loss of activity after 30 min391772
9-Crotalus adamanteus-unstable at391777
10-Protobothrops mucrosquamatus-4°C, 24 h, complete inactivation391773
additional information-Crotalus adamanteus-slow reversible and temperature-dependent transition to an inactive form under alkaline conditions391770
additional information-Crotalus adamanteus-protection by acetate (high concentration) and some aliphatic and aromatic monocarboxylic acids at pH 9.0391777

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
-70-Naja oxiana-the enzyme is stable at low temperatures (-20°C, -70°C) for one week and completely loses its activity after heating at 70°C for 10 min691918
050Aplysia punctataQ6T277stable within this range670963
4-Ophiophagus hannah-3 months, no loss of activity391772
4-Bothrops moojeni-at temperatures lower than 4°C, enzymatic activity is completely lost692650
2550Rhodococcus opacusQ8VPD4inactivation in 50 mM triethylamine/HCl buffer, pH 7.6 in the same range as 50 mM potassium-phosphate buffer pH 6.6651026
25-Ophiophagus hannah-1 month, no loss of activity391772
3050Rhodococcus sp.-pH 7.0, 60 min, stable up to 30°C, 80% of the enzyme activity remains at 40°C, the enzyme activity is almost completely lost at 50°C711874
30-Rhodococcus opacusQ8VPD4incubation for 30 min with 0.28 M H2O2 results in 50% inactivation651026
37-Ophiophagus hannah-5 days, no loss of activity, 14 days, 20% loss of activity391772
37-Rhodococcus opacusQ8VPD4half-life: 938 min in glycine/NaOH buffer, 35 min in TEA/HCL buffer and 44 min in potassium phosphate buffer; t1/2: 35 min, increases more than 20fold by incubating the L-AAO in glycine/NaOH buffer: 938 min, potassium phosphate buffer t1/2: 44 min651026
45-Rattus norvegicus-5 min, stable391802
45-Bothrops jararacaQ6TGQ9after heating to 45°C, LAAO activity gradually decreases. After heating at 60°C and 70°C for 10 min., 85% and 100% of activity is lost, respectively. Freezing at -70°C for 24 h causes a 50% loss of enzyme activity. After lyophilization, about 15% only of activity is retained690684
50-Protobothrops mucrosquamatus-10 min, pH 6.8, stable up to391773
50-Daboia russellii russellii-both isoforms are stable up to 50°C but are sharply inactivated above 60°C692288
50-Pseudoalteromonas flavipulchra-30 min, completely stable antibacterial activity711872
51-Rattus norvegicus-5 min, inactivation above 51°C391802
60-Aplysia punctataQ6T27710 min, 80% loss of activity670963
60-Pseudoalteromonas flavipulchra-30 min, partial loss of antibacterial activity711872
65-Protobothrops mucrosquamatus-10 min, 54% loss of activity391773
70-Agkistrodon piscivorus piscivorus-rapid loss of activity391766
70-Aplysia punctataQ6T27710 min, complete loss of activity670963
70-Macrovipera lebetina-15 min, complete inactivation670968
70-Pseudoalteromonas flavipulchra-30 min, complete loss of antibacterial activity711872
71-Rattus norvegicus-5 min, complete inactivation391802
73-Crotalus adamanteus-no loss of activity after 5 min, heat-stable in presence of 0.01 mM L-leucine391774
75-Protobothrops mucrosquamatus-10 min, 97% loss of activity391773
additional information-Crotalus adamanteus-reduced form of the enzyme is much more stable to heat than oxidized form, substrates: e.g. L-Leu, L-Phe, L-Met protect from heat denaturation, no protection by D-leucine and L-lysine391774
additional information-Crotalus adamanteus-labile to heating at 60°C391791
additional information-Calloselasma rhodostoma-freezing causes reversible inactivation391815

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
resistant against tryptic digestAplysia punctataQ6T277670963
2-mercaptoethanol stabilizesCorynebacterium sp.-391784
KCl stabilizesCorynebacterium sp.-391784
acetate at high concentrations increases pH-stability at pH 9Crotalus adamanteus-391777
aliphatic and aromatic monocarboxylic acids protect at pH 9.0Crotalus adamanteus-391777
freezing, inactivation between -5°C and -60°C, maximal inactivation at -20°C, rate of inactivation is dependent on pH of storage, in most cases complete reactivation by heating at pH 5, inactivation not prevented by monovalent cationsCrotalus adamanteus-391776, 391782
freezing, quick freezing with dry ice/acetone mixture and storage at -15°C for 60 h, enzyme loses 33% of activity, complete reactivation by heating at pH 5, inactivation not prevented by monovalent cationsCrotalus adamanteus-391776, 391782
freezing, quick freezing with dry ice/acetone mixture and storage at -15°C for 60 h, enzyme is stableOphiophagus hannah-391772
freezing, irreversible inactivationProtobothrops mucrosquamatus-391773
irreversible inactivation by lyophilizationProtobothrops mucrosquamatus-391773
stability of enzyme in immobilized whole cellsProvidencia sp.-391780
freezing at -18°C without addition of glycerol inactivates the enzymeRhodococcus opacusQ8VPD4651026
stability of the enzyme can be increased by storage or incubation of the enzyme in glycine/NaOH bufferRhodococcus opacusQ8VPD4651026

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
no decrease in antimicrobial activity during storage for up to 5 months at room temperatureAplysia californicaQ6IWZ0669658
-20°C, 4 months, no loss of activityBacillus carotarum-391824
4°C, 4 months, no loss of activityBacillus carotarum-391824
-40°CBothrops insularis-695212
4°C, 66 mM KCl, 10 mM 2-mercaptoethanol, 1 month, 5-10% loss of activityCorynebacterium sp.-391784
0-5°C, crystalline suspension in water, pH 7.2, stable for several monthsCrotalus adamanteus-391770
-80°C, at least 3 yearsHebeloma sp.-694300
-20°C, loss of 80% of activityMacrovipera lebetina-670968
25°C, stable for at least 24hMacrovipera lebetina-670968
4°C, stable for at least 24hMacrovipera lebetina-670968
4°C, several monthsNaja oxiana-691918
4°C, purified enzyme stable for weeksNeurospora crassa-391787
4°C, pH 7.4, 20 mM Tris-HCl, 3 monthsOphiophagus hannah-391772
0°C, several weeksProteus sp.-391768
4°C, 40% v/v glycerol, 3 monthsProtobothrops mucrosquamatus-391773
0°C, several weeksProvidencia sp.-391768
0-3°C, dialyzed enzyme, 2 weeks, 10% loss of activityRattus norvegicus-391769
-18°C, 50 mM glycine/NaOH buffer, pH 8.6, 50% glycerol, stable for several months, withou glycerol inactivationRhodococcus opacusQ8VPD4651026
4°C or -18°C, pH 8.6, 50 mM glycine/NaOH buffer, 50% glycerol, stable for several monthsRhodococcus opacusQ8VPD4651026
4°C, 50 mM glycine/NaOH buffer, pH 8.6, stable for several monthsRhodococcus opacusQ8VPD4651026

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
by gel filtration followed by ion-exchange chromatography, 51.3foldAgkistrodon blomhoffi ussuriensis-695208
native extracellular enzyme 11.2fold from venom by anion exchange chromatography and 3 steps of gel filtration, one of which is HPLCAgkistrodon blomhoffi ussuriensis-711329
-Agkistrodon contortrix laticinctus-391821
-Agkistrodon piscivorus piscivorus-391766
-Bacillus carotarum-391824
native enzyme from venom by cation exchange and hydrophobic interaction chromatography, followed by adosrption chromatography and HPLCBothropoides pauloensisB5AR80696493
-Bothrops alternatus-654954
native enzyme 54fold from venom by gel filtration and ultrafiltration, anion exchange chromatography, and lectin affinity chromatography to homogeneityBothrops atrox-697450
by HPLC and sequence gradeBothrops insularis-695212
by gel filtration, affinity and hydrophobic interaction chromatographyBothrops jararacaQ6TGQ9690684
native enzyme from venom by gel filtration, anion exchange and heparin affinity chromatographyBothrops jararaca-701330
native extracellular enzyme from venom by gel filtration and anion exchange chromatographyBothrops jararaca-713559
three chromatographic stepsBothrops jararaca-690856
by molecular exclusion, ion exchange and hydrophobic chromatographyBothrops jararacussuQ6TGQ9690693
native enzyme to high molecular homogeneity by ion exchange chromatography and reverse phase chromatography, followed by anion exchange chromatgography, ultrafiltration, and gel filtrationBothrops marajoensis-713558
by ion-exchange chromatography and gel filtration, 12.9foldBothrops moojeni-692650
by molecular exclusion, ion exchange and hydrophobic chromatographyBothrops moojeniQ6TGQ8690693
-Bothrops pirajai-667933
native enzyme from venom by anion exchange and heparin affinity chromatographyBungarus fasciatus-701332
-Calloselasma rhodostoma-391815, 391819
by ion exchange and gel filtration, to homogeneity; recombinant enzymeCalloselasma rhodostoma-670798
-Chlamydomonas reinhardtii-391814
-Crotalus adamanteus-391766, 391770, 391774
-Crotalus durissus cascavella-670964
gel filtration followed by ion exchange chromatography, to homogeneityDaboia russellii russellii-692288
native enzyme by anion exchange chromatography, gel filtration, and heparin affinity chromatography to homogeneityDaboia russellii siamensisQ4F867701333
by gel filtrationDeinagkistrodon acutus-694317
-Eristocophis macmahonii-391820
-Gloydius blomhoffi-654872
native enzyme by gel filtration, cation and anion exchange chromatography, and hydroxyapatite chromatographyGloydius blomhoffiQ90W54698669
-Gloydius halys-654119
whole cell lysates of viable cryopreserved lymph node cells from follicular lymphomas, spelnocytes from marginal zone lymphoma, and traumatic normal spleens, and cell lines or cells are submitted to magnetic cell sorting using anti-human CD19 MACS beadsHomo sapiens-699933
-Macrovipera lebetina-670968
-Meleagris gallopavo-391789
native isozymes by lectin affinity and anion exchange chromatography, isozyme MPLAO1 and MPLAO3 are purified to homogeneity, while isozyme MPLAO2 is notMyoxocephalus polyacanthocephalusB5U982697466
by cation ion exchange chromatography, gel filtration and anion ion exchange chromatography, to homogeneityNaja atra-690221
by gel filtration, ion exchange chromatography, 100fold purifiedNaja oxiana-691918
-Neurospora crassa-391787
-Ophiophagus hannah-391772, 391825, 391826
by gel filtration, ion-exchange and heparin chromatography, to homogeneityOphiophagus hannahA8QL50695209
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, native extracellular enzyme from Platichthys stellatus-derived epidermal mucus by ultracentrifugation, hydrophobic interaction chromatography, and gel filtrationPlatichthys stellatusD2KWB6711987
-Protobothrops jerdonii-656581
-Protobothrops mucrosquamatus-391773
gel filtrationPseudoalteromonas luteoviolacea-690575
-Rattus norvegicus-391766, 391769, 391796, 391802
-Rhodococcus opacus-669894
to homogeneity, recovery of 68% and 144foldRhodococcus opacusQ8VPD4651026
wild-type, 76fold, recombinant L-AAO expressed in and Streptomyces lividans, 186fold; wild-type and recombinant enzymeRhodococcus opacusQ8VPD4653762
; to homogeneity by affinity chromatography, anion-exchange chromatography and gel filtrationSebastes schlegeliiA1IGW6668580
gel filtrationSebastes schlegelii-692408
native enzyme 700fold from serum by concanavalin A lectin affinity chromatography, anion exchange HPLC, hydroxyapatite HPLC and gel filtration HPLCSebastes schlegelii-711786
by immobilized metal ion affinity chromatographyStreptococcus oligofermentans-692863
-Synechococcus elongatus PCC 7942-391808
native enzyme from venom by two repeated steps of anion exchange chromatographyVipera ammodytes ammodytes-712998
native isozymes from venom by 2times anion exchange chromatography and dialysis to homogeneityVipera ammodytes ammodytes-695361
-Viridovipera stejnegeriQ6WP39654441

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Aplysia californicaQ6IWZ0669658
-Aplysia punctataQ6T277670963
DNA and amino acid sequence determination and analysis, phylogenetic analysisBothropoides pauloensisB5AR80696493
-Bungarus fasciatusA8QL52695209
-Bungarus multicinctusA8QL51695209
-Calloselasma rhodostoma-391815
LAAO open reading frame inserted after the alpha-MF-signal sequence. Expressed in Pichia pastorisCalloselasma rhodostoma-670798
-Emericella nidulans-667254
-Mus musculusO09046391817
isozymes MPLAO1, MPLAO2, and MPLAO3, DNA and amino acid sequence determinhation and analysis, phylogenetic analysis and sequence comparisonsMyoxocephalus polyacanthocephalusB5U982697466
-Naja atraA8QL58695209
into pGEM-T vectorOphiophagus hannahA8QL50695209
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain Rosetta 2 (lambdaDE3)Platichthys stellatusD2KWB6711987
-Rhodococcus opacus-669894
expression in Streptomyces lividans; expression into different Escherchia coli and Streptomyces lividans vectors. Expression in Escherichia coli results in an insoluble protein whereas Steptomyces lividans is a suitable host for the heterologous production of L-AAORhodococcus opacusQ8VPD4653762
; into the pT7Blue T-vectorSebastes schlegeliiA1IGW6668580
overexpressed in Escherichia coli BL21(DE3)pLysSStreptococcus oligofermentans-692863
into pUC19 and pSVB30Synechococcus elongatus PCC 6301P72346695281
-Viridovipera stejnegeriQ6WP39654441

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
additional informationEmericella nidulans-loss of function mutants reverse the areA102 phenotype that results in pleiotropic effects on nitrogen utilization, areA102 encodes a GATA transkription factor. Elevated enzyme expression in an areA102 background accounts for the strong growth of these strains on amino acids that are substrates for the enzyme667254
additional informationNeurospora crassa-gln-1bR8, mutant altered in the regulation of L-amino acid oxidase391822
additional informationRhodococcus sp.-development of a simple enzymatic method for production of a wide variety of D-amino acids using L-amino acid oxidase from Rhodococcus sp. AIU Z-35-1, overview711874
additional informationStreptococcus oligofermentans-an aaoSo mutant loses H2O2 formation from L-amino acids. Inhibition by Streptococcus oligofermentans of Streptococcus mutans in a peptone-rich mixed-species biofilm is greatly reduced692863

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
medicineAgkistrodon blomhoffi ussuriensis-LAO potently induces lesions in lungs and livers. LAO causes severe pneumorrhagia, pulmonary interstitial edema, fusion of pulmonary alveoli, cardiac interstitial edema and bleeding when being intravenously injected into BALB/c mice. Also induces liver cell necrosis and release of cytokines including IL-6, IL-12 and IL-2 from highly purified human peripheral blood monocytes and T cells, respectively. The ability of LAO will contribute to the understanding of the pathogenesis of snakebite wound695208
medicineBothrops insularis-LAO decreases perfusion pressure, renal vascular resistance, glomerular filtration rate, sodium, potassium and chloride tubular reabsortion. Causes acute tubular necrosis foci695212
medicineBothrops jararacaQ6TGQ9significantly inhibits Ehrlich ascites tumour growth and induces an influx of polymorphonuclear cells, as well as spontaneous liberation of H2O2 from peritoneal macrophages. Later, LAAO-I induces mononuclear influx and peritoneal macrophage spreading. Animals treated with LAAO-I show higher survival time690684
medicineBothrops jararaca-antiviral (Dengue virus) and antiprotozoal (trypanocidal and leishmanicide) activities690856
drug developmentBothrops jararacussuQ6TGQ9purified LAAO-I exhibits antiprotozoal activities which are demonstrated to be hydrogen-peroxide mediated. Exposure of promastigotes of Leishmania sp. results in dose-dependent parasite killing. LAAOs are interesting multifunctional enzymes, not only for a better understanding of the ophidian envenomation mechanism, but also due to their biotechnological potential as model for therapeutic agents690693
drug developmentBothrops moojeniQ6TGQ8purified LAAO-I exhibits antiprotozoal activities which are demonstrated to be hydrogen-peroxide mediated. Exposure of promastigotes of Leishmania sp. results in dose-dependent parasite killing. LAAOs are interesting multifunctional enzymes, not only for a better understanding of the ophidian envenomation mechanism, but also due to their biotechnological potential as model for therapeutic agents690693
synthesisCrotalus adamanteus-use of enzyme as a catalyst in supercritical CO2. enzyme activity increases after exposure to supercritical conditions by up to 15%. Enzyme is more stable in supercritical CO2 than under atmospherical pressure, and oxidation of 3,4-dihydroxyphenyl-L-Ala is best under supercritical conditions667368
drug developmentDeinagkistrodon acutus-ACTX-6 demonstrates cytotoxicity in vitro and can inhibit tumor growth in vivo. It can markedly increase accumulation of sub-G1 phase, which suggests that this enzyme can induce apoptosis. ACTX-6 is a potential substance to develop into an antitumor drug694317
medicineViridovipera stejnegeriQ6WP39enzyme displays dosedependent inhibition on HIV-1 infection and replication654441
medicineBothrops moojeni-LAAO-I exhibited bactericidal, antitumoral, trypanocidal, edematogenic, and platelet-aggregating activities. It induces typical apoptotic DNA fragmentation in HL-60 cells. Potential use of LAAO-I as a therapeutic agent for treatment of diseases in which induction of H2O2 production can be beneficial692650
additional informationCalloselasma rhodostoma-expressed LAAO exhibits the same electrophoretic mobility as native LAAO and exhibits approximately the same extent of glycosylation as authentic LAAO from snake venom. Catalytic properties and substrate specificity of recombinant LAAO are similar to those of native enzyme670798
additional informationCalloselasma rhodostoma-LAAO causes cell death by induction of apoptosis in yeast. Lower concentrations of hydrogen peroxide accompanied by leucine deficiency may have a role in enhancing cell death in leucine auxotrophic yeast strain. LAAO interacts with the cell surface of yeast. Depletion of leucine from the medium by LAAO and the interaction of LAAO with yeast cells are shown to be the major factors responsible for cell demise in the presence of catalase695276
medicineDeinagkistrodon acutus-induces apoptosis in Hela cervical cancer cells in a concentration- and time-dependent manner. Caspase activation and PARP cleavage are involved in ACTX-8-induced apoptosis. ACTX-8 activates a mitochondrial pathway of apoptosis, which is regulated by Bcl-2 family members. Reactive oxygen species generated by ACTX-8 are involved in apoptosis. Translocation of Bax and Bad from the cytosol into mitochondria in ACTX-8-treated cells693949
additional informationHebeloma cylindrosporum, Hebeloma sp.-LAO is a potential candidate for a mechanism that catalyses nitrogen mineralization from amino acids at the ecosystem level694300
medicineHomo sapiens-a high level of enzyme expression seems associated with absence of bone marrow involvement and better outcome in follicular lymphoma cases, enzyme levels could serve as prognosis factor699933
additional informationLaccaria bicolor-LAO is a potential candidate for a mechanism that catalyses nitrogen mineralization from amino acids at the ecosystem level694300
additional informationNaja atra-LAAO dose-dependently induces aggregation of washed human platelets. It induces tyrosine phosphorylation of a number of platelet proteins including Src kinase, spleen tyrosine kinase, and phospholipase C gamma2. Both H2O2 production and binding to platelet membrane proteins may be involved in its action. The enzyme binds to the platelet membrane to enhance the sensitivity of platelets to H2O2. At the same time, H2O2 released by the enzyme activates platelets by an unknown mechanism690221
additional informationNaja oxiana-the enzyme has antibacterial activity inhibiting the growth of Gram-positive (Bacillus subtilis) and Gram-negative (Escherichia coli) bacteria. LAAO dose-dependently inhibits ADP- or collagen-induced platelet aggregation with IC50 of 0.094 micromol and 0.036 micromol, respectively691918
medicineOphiophagus hannahA8QL50LAAO 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 stejnulxin695209
additional informationPseudoalteromonas luteoviolacea-LAO is a macromolecule with antimicrobial activity, shows broad substrate specificity690575
additional informationRhodococcus opacus-a helical domain is exclusively responsible for the unusual dimerisation mode of the enzyme and is not found in other members of the family so far. Most groups present at the active site are involved in substrate recognition, binding and fixation, i.e. they direct the trajectory of the interacting orbitals. In this mode of catalysis orbital steering/interactions are the predominant factors for the chemical step(s). A mirrorsymmetrical relationship between the two substrate-binding sites of D and L-amino acid oxidases is observed which facilitates enantiomeric selectivity while preserving a common arrangement of the residues in the active site669894
additional informationSebastes schlegeliiA1IGW6LAO is involved in the innate immunity of fish skin. Shows potent antibacterial activity against fish pathogens, specifically Gram-negative bacteria such as Aeromonas hydrophila, Aeromonas salmonicida and Photobacterium damselae ssp. piscicida668580
additional informationSebastes schlegelii-potent and effective activity of SSAP against waterborne virulent pathogens. Shows antibacterial activity, acts selectively on Gram-negative bacteria. SSAP inhibits potently the growth of Aeromonas salmonicida, Photobacterium damselae subsp. piscicida and Vibrio parahaemolyticus with a minimum inhibitory concentration of 0.078, 0.16 and 0.63 microg/mL, respectively. Bacteria binding activity may be involved in the bacterial cell selectivity of SSAP. Treatments with SSAP induce cell surface damage to Aeromonas salmonicida, remarkable elongation of Photobacterium damselae subsp. piscicida bodies and pores into Vibrio parahaemolyticus cells691917
additional informationSebastes schlegelii-SSAP is predominantly synthesized in skin and gill and probably functions as an antibacterial LAO in both tissues. It shows antibacterial activity against Photobacterium damselae subsp. piscicida692408
additional informationStreptococcus oligofermentans-LAAO contributes to competitive edge of Streptococcus oligofermentans over Streptococcus mutans in mixed-species biofilm with peptone692863

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
Dermatitis HerpetiformisPresence of L-amino-acid oxidase in the blood in pemphigus, dermatitis herpetiformis Duhring and herpes zoster. PubMed
GranulomaDichotomy between factors inducing the immunosuppressive enzyme IL-4-induced gene 1 (IL4I1) in B lymphocytes and mononuclear phagocytes. PubMed
Herpes ZosterPresence of L-amino-acid oxidase in the blood in pemphigus, dermatitis herpetiformis Duhring and herpes zoster. PubMed
InfectionMolecular characterization of Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activity. PubMed
Leukemia, Lymphocytic, Chronic, B-CellThe novel immunosuppressive enzyme IL4I1 is expressed by neoplastic cells of several B-cell lymphomas and by tumor-associated macrophages. PubMed
LymphomaHuman IL4I1 is a secreted L-phenylalanine oxidase expressed by mature dendritic cells that inhibits T-lymphocyte proliferation. PubMed
LymphomaThe novel immunosuppressive enzyme IL4I1 is expressed by neoplastic cells of several B-cell lymphomas and by tumor-associated macrophages. PubMed
Lymphoma, B-CellInhibition of antitumor T-cell response and immune escape in mice associated with Interleukin 4-induced gene 1 expression. PubMed
Lymphoma, B-CellThe novel immunosuppressive enzyme IL4I1 is expressed by neoplastic cells of several B-cell lymphomas and by tumor-associated macrophages. PubMed
Lymphoma, FollicularThe novel immunosuppressive enzyme IL4I1 is expressed by neoplastic cells of several B-cell lymphomas and by tumor-associated macrophages. PubMed
MelanomaInhibition of antitumor T-cell response and immune escape in mice associated with Interleukin 4-induced gene 1 expression. PubMed
MesotheliomaInhibition of antitumor T-cell response and immune escape in mice associated with Interleukin 4-induced gene 1 expression. PubMed
NeoplasmsA cytotoxin isolated from Agkistrodon acutus snake venom induces apoptosis via Fas pathway in A549 cells. PubMed
NeoplasmsBiopolymers from marine invertebrates. XI. Characterization of an antineoplastic glycoprotein, dolabellanin A, from the albumen gland of a sea hare, Dolabella auricularia. PubMed
NeoplasmsInhibition of antitumor T-cell response and immune escape in mice associated with Interleukin 4-induced gene 1 expression. PubMed
NeoplasmsIsolation and characterization of ACTX-6: a cytotoxic L-amino acid oxidase from Agkistrodon acutus snake venom. PubMed
NeoplasmsPurification of dolabellanin-C an antineoplastic glycoprotein in the body fluid of a sea hare, Dolabella auricularia. PubMed
NeoplasmsThe novel immunosuppressive enzyme IL4I1 is expressed by neoplastic cells of several B-cell lymphomas and by tumor-associated macrophages. PubMed
PemphigusPresence of L-amino-acid oxidase in the blood in pemphigus, dermatitis herpetiformis Duhring and herpes zoster. PubMed
Uterine Cervical NeoplasmsACTX-8, a cytotoxic L-amino acid oxidase isolated from Agkistrodon acutus snake venom, induces apoptosis in Hela cervical cancer cells. PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
389803Bright, H.J.; Porter, D.J.T.Flavoprotein oxidasesThe Enzymes, 3rd Ed. (Boyer, P.D., ed.)12421-5051975Agkistrodon piscivorus piscivorus, Crotalus adamanteus-
391766Meister, A.; Wellner, D.Flavoprotein amino acid oxidasesThe Enzymes, 2nd Ed (Boyer, P.D., Lardy, H., Myrbäck, K., eds.)7609-6481963Agkistrodon piscivorus piscivorus, Crotalus adamanteus, Rattus norvegicus-
391768Cioaca, C.; Ivanof, A.Bacterial amino acid oxidases. I. L-amino acid oxidase and its distribution in bacteriaArch. Roum. Pathol. Exp. Microbiol.33211-2221974no activity in Acinetobacter anitratum, no activity in Alcaligenes faecalis, no activity in Bacillus subtilis, no activity in Diplococcus pneumoniae, no activity in Enterobacter aerogenes, no activity in Klebsiella pneumoniae, no activity in Micrococcus tetragenus, no activity in Moraxella catarrhalis, no activity in Mycobacterium phlei, no activity in Pseudomonas aeruginosa, no activity in Serratia marcescens, no activity in Shigella flexneri, no activity in Staphylococcus aureus, no activity in Staphylococcus epidermidis, no activity in Streptococcus viridans, Proteus sp., Providencia sp. PubMed
391769Nakano, M.; Danowski, T.S.L-Amino acid oxidase (rat kidney)Methods Enzymol.17B601-6051971Rattus norvegicus-
391770Weller, D.L-Amino acid oxidase (snake venom)Methods Enzymol.17B597-6001971Crotalus adamanteus-
391771Weller, D.; Lichtenberg, L.A.Assay of amino acid oxidaseMethods Enzymol.17B593-5961971snake-
391772Tan, N.H.; Saifuddin, M.N.Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venomBiochem. Int.19937-9441989Ophiophagus hannah PubMed
391773Ueda, M.; Chang, C.C.; Ohno, M.Purification and characterization of L-amino acid oxidase from the venom of Trimeresurus mucrosquamatus (Taiwan habu snake)Toxicon26695-7061988Protobothrops mucrosquamatus PubMed
391774Wellner, D.; Meister, A.Crystalline L-amino acid oxidase of Crotalus adamanteusJ. Biol. Chem.2352013-20181960Crotalus adamanteus PubMed
391775Chen, S.S.; Walgate, J.H.; Duerre, J.A.Oxidative deamination of sulfur amino acids by bacterial and snake venom L-amino acid oxidaseArch. Biochem. Biophys.14651-631971Crotalus terrificus terrificus, Providencia rettgeri-
391776Curti, B.; Massey, V.; Zmudka, M.Inactivation of snake venom L-amino acid oxidase by freezingJ. Biol. Chem.2432306-23141968Crotalus adamanteus PubMed
391777Paik, W.K.; Kim, S.Studies on the stability of L-amino-acid oxidase of snake venomBiochim. Biophys. Acta13949-551967Crotalus adamanteus PubMed
391778Massey, V.; Curti, B.On the reaction mechanism of Crotalus adamanteus L-amino acid oxidaseJ. Biol. Chem.2421259-12641967Crotalus adamanteus PubMed
391779Kimura, T.; Esaki, N.; Tanaka, H.; Soda, K.Action of S-carbamoyl and S-thiocarbamoyl derivatives of L-cysteine on L-amino acid oxidaseAgric. Biol. Chem.483157-31591984Crotalus adamanteus-
391780Szwajcer, E.; Brodelius, P.; Mosbach, K.Production of alpha-keto acids: 2. Immobilized whole cells of Providencia sp. PCM 1298 containing L-amino acid oxidaseEnzyme Microb. Technol.4409-4131982Providencia sp.-
391781Du, X.Y.; Clemetson, K.J.Snake venom L-amino acid oxidasesToxicon40659-6652002Agkistrodon contortrix laticinctus, Bothrops moojeni, Calloselasma rhodostoma, Crotalus adamanteus, Crotalus atrox, Eristicophis macmahoni, Gloydius blomhoffi, Naja kaouthia, Ophiophagus hannah, Protobothrops mucrosquamatus, Pseudechis australis, snake, Trimeresurus flavoviridis PubMed
391782Couer, C.J.; Edmondson, D.F.; Singer.T.P.Reversible inactivation of L-amino acid oxidase. Properties of the three conformational formsJ. Biol. Chem.2528035-80391977Crotalus adamanteus PubMed
391783Marcotte, P.; Walsh, C.Vinylglycine and proparglyglycine: complementary suicide substrates for L-amino acid oxidase and D-amino acid oxidaseBiochemistry153070-30761976Crotalus adamanteus PubMed
391784Coudert, M.; Vandecasteele, J.P.Charcterization and physiological function of a soluble L-amino acid oxidase in CorynebacteriumArch. Microbiol.102151-1531975Corynebacterium sp., no activity in Bacillus subtilis subsp. subtilis, no activity in Escherichia coli, no activity in Pseudomonas putida PubMed
391785Duerre, J.A.; Chakrabarty, S.L-amino acid oxidases of Proteus rettgeriJ. Bacteriol.121656-6631975Providencia rettgeri PubMed
391786Pelmont, J.; Arlaud, G.; Rossat, A.M.L-Amino acid oxidases of Proteus mirabilis: general propertiesBiochimie541359-13741972Proteus mirabilis PubMed
391787Aurich, H.; Luppa, D.; Schucker, G.Purification and properties of l-amino acid oxidase from neurosporaActa Biol. Med. Ger.28209-2201972Neurospora crassa PubMed
391788Luppa, D.; Aurich, H.Kinetic studies on the reaction mechanism of L-amino acid oxidase from Neurospora crassaActa Biol. Med. Ger.27839-8501971Neurospora crassa PubMed
391789Mizon, J.; Biserte, G.; Boulanger, P.Properties of turkey (Meleagris gallopavo L.)liver L-amino acid oxidaseBiochim. Biophys. Acta21233-421970Meleagris gallopavo PubMed
391790Page, D.S.; Vanetten, R.L.L-Amino acid oxidase. II. Deuterium isotope effects and the action mechanism for the reduction of L-amino acid oxidase by L-leucineBiochim. Biophys. Acta22716-311971Crotalus adamanteus PubMed
391791Skarnes, R.C.L-Amino-acid oxidase, a bactericidal systemNature2251072-10731970Crotalus adamanteus PubMed
391792Hayes, M.B.; Wellner, D.Microheterogeneity of L-amino acid oxidase. Separation of multiple components by polyacrylamide gel electrofucusingJ. Biol. Chem.2446636-66441969Crotalus adamanteus PubMed
391793Page, D.S.; Van Etten, R.L.L-Amino-acid oxidase. I. Effect of pHBiochim. Biophys. Acta19138-451969Crotalus adamanteus PubMed
391794Nakano, M.; Saga, M.; Tsutsumi, Y.Distribution and immunochemical properties of rat kidney L-amino-acid oxidase, with a note on peroxisomesBiochim. Biophys. Acta18519-301969Rattus norvegicus PubMed
391795Porter, D.J.T.; Bright, H.J.Location of hydrogen transfer steps in the mechanism of reduction of L-amino acid oxidaseBiochem. Biophys. Res. Commun.36209-2141969Crotalus adamanteus PubMed
391796Miller, C.H.; Duerre, J.A.Oxidative deamination of S-adenosyl-L-homocysteine by rat kidney L-amino acid oxidaseJ. Biol. Chem.2444273-42761969Rattus norvegicus PubMed
391797De Kok, A.; Rawitch, A.B.Studies on L-amino acid oxidase. II. Dissociation and characterization of its subunitsBiochemistry81405-14111969Crotalus adamanteus PubMed
391798Nakano, M.; Tarutani, O.; Danowski, T.S.Molecular weight of mammalian L-amino-acid oxidase from rat kidneyBiochim. Biophys. Acta168156-1571968Rattus norvegicus PubMed
391799De Kok, A.; Veeger, C.Studies on L-amino-acid oxidase. I. Effects of pH and competitive inhibitorsBiochim. Biophys. Acta16735-471968Crotalus adamanteus PubMed
391800Koster, J.K.; Veeger, C.The relation between temperature-inducible allosteric effects and the activation energies of amino-acid oxidasesBiochim. Biophys. Acta16748-631968Crotalus adamanteus PubMed
391801Shinwari, M.A.; Falconer, I.R.Naturally occuring inhibition and activation of avian liver L-amino acid oxidaseBiochem. J.104538-5481967Gallus gallus-
391802Nakano, M.; Tsutsumi, Y.; Danowski, T.S.Crystalline L-amino-acid oxidase from the soluble fraction of rat-kidney cellsBiochim. Biophys. Acta13940-481967Rattus norvegicus PubMed
391803Sikora, L.; Marzluf, G.A.Regulation of L-amino acid oxidase and of D-amino acid oxidase in Neurospora crassaMol. Gen. Genet.18633-391982Neurospora crassa PubMed
391804Cooper, A.J.L.; Meister, A.Action of liver glutamine transaminase and L-amino acid oxidase on several glutamine analogs. Preparation and properties of the 4-S, O, and NH analogs of alpha-ketoglutaramic acidJ. Biol. Chem.2488499-85051973Crotalus adamanteus PubMed
391805Pistorius, E.K.Further evidence for a functional relationship between L-amino acid oxidase activity and photosynthetic oxygen evolution in Anacystis nidulans. Effect of chloride on the two reactionsZ. Naturforsch. C40806-8131985Synechococcus elongatus PCC 7942-
391806Pistorius, E.K.Effects of Mn2+, Ca2+ and chlorpromazine on photosystem II of Anacystis nidulans. An attempt to establish a functional relationship of amino acid oxidase to photosystem IIEur. J. Biochem.135217-2221983Synechococcus elongatus PCC 7942 PubMed
391807Pistorius, E.K.; Voss, H.Presence of an amino acid oxidase in photosystem II of Anacystis nidulansEur. J. Biochem.126203-2091982Synechococcus elongatus PCC 7942 PubMed
391808Pistorius, E.K.; Voss, H.Some properties of a basic L-amino-acid oxidase from Anacystis nidulansBiochim. Biophys. Acta611227-2401980Synechococcus elongatus PCC 7942 PubMed
391809Löffelhardt, W.The biosynthesis of phenylacetic acids in the bluegreen alga anacystis nidulans: Evidence for the involvement of a thylakoid-bound L-amino acid oxidaseZ. Naturforsch. C32345-3501977Synechococcus elongatus PCC 7942-
391810Pistorius, E.K.; Kertsch, R.; Faby, S.Investigations abuot various possible functions of the L-amino acid oxidase in the cyanobacterium Anacystis nidulansZ. Naturforsch. C44370-3771989Synechococcus elongatus PCC 7942-
391811Meyer, R.; Pistorius, E.K.Some properties of photosystem II preparations from the cyanobacterium Synechococcus sp. - presence of an L-amino acid oxidase in photosystem II complexes from Synechococcus sp.Biochim. Biophys. Acta893426-4331987Synechococcus sp.-
391812Cooper, A.J.L.; Meister, A.Enzymatic oxidation of L-homocysteineArch. Biochem. Biophys.239556-5661985snake PubMed
391813Christman, M.F.; Cardenas, J.M.Essential arginine residues occur in or near the catalytic site of L-amino acid oxidaseExperientia38537-5381982snake PubMed
391814Vallon, O.; Bulte, L.; Kuras, R.; Olive, J.; Wollman, F.A.Extensive accumulation of an extracellular L-amino acid oxidase during gametogenesis of Chlamydomonas reinhardtiiEur. J. Biochem.215351-3601993Chlamydomonas reinhardtii PubMed
391815Macheroux, P.; Seth, O.; Bollschweiler, C.; Schwarz, M.; Kurfurst, M.; Au, L.C.; Ghisla, S.L-Amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma: comparative sequence analysis and characterization of active and inactive forms of the enzymeEur. J. Biochem.2681679-16862001Calloselasma rhodostoma PubMed
391816Geyer, A.; Fitzpatrick, T.B.; Pawelek, P.D.; Kitzing, K.; Vrielink, A.; Ghisla, S.; Macheroux, P.Structure and characterization of the glycan moiety of L-amino-acid oxidase from the Malayan pit viper Calloselasma rhodostomaEur. J. Biochem.2684044-40532001Calloselasma rhodostoma PubMed
391817Sun, Y.; Nonobe, E.; Kobayashi, Y.; Kuraishi, T.; Aoki, F.; Yamamoto, K.; Sakai, S.Characterization and expression of L-amino acid oxidase of mouse milkJ. Biol. Chem.27719080-190862002Mus musculus PubMed
391818Pawelek, P.D.; Cheah, J.; Coulombe, R.; Macheroux, P.; Ghisla, S.; Vrielink, A.The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active siteEMBO J.194204-42152000Calloselasma rhodostoma PubMed
391819Ponnudurai, G.; Chung, M.C.; Tan, N.H.Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venomArch. Biochem. Biophys.313373-3781994Calloselasma rhodostoma PubMed
391820Ali, S.A.; Stoeva, S.; Abbasi, A.; Alam, J.M.; Kayed, R.; Faigle, M.; Neumeister, B.; Voelter, W.Isolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venomArch. Biochem. Biophys.384216-2262000Eristocophis macmahonii PubMed
391821Souza, D.H.F.; Eugenio, L.M.; Fletcher, J.E.; Jiang, M.S.; Garratt, R.C.; Oliva, G.; Selistre-de-Araujo, H.S.Isolation and structural characterization of a cytotoxic L-amino acid oxidase from Agkistrodon contortrix laticinctus snake venom: Preliminary crystallographic dataArch. Biochem. Biophys.368285-2901999Agkistrodon contortrix laticinctus PubMed
391822Calderon, J.; Olvera, L.; Martinez, L.M.; Davila, G.A Neurospora crassa mutant altered in the regulation of L-amino acid oxidaseMicrobiology1431969-19741997Neurospora crassa-
391823Pessatti, M.; Fontana, J.D.; Furtado, M.F.; Guimaraes, M.F.; Zanette, L.R.; Costa, W.T.; Baron, M.Screening of Bothrops snake venoms for L-amino acid oxidase activityAppl. Biochem. Biotechnol.51-52197-2101995Bothrops sp. PubMed
391824Brearley, G.M.; Price, C.P.; Atkinson, T.; Hammond, P.M.Purification and partial characterization of a broad-range L-amino acid oxidase from Bacillus carotarum 2Pfa isolated from soilAppl. Microbiol. Biotechnol.41670-6761994Bacillus carotarum-
391825Li, 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 aggregationToxicon321349-13581994Ophiophagus hannah PubMed
391826Ahn, 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.29911-9191997Ophiophagus hannah PubMed
651026Geueke, B.; Hummel, W.A new bacterial L-amino acid oxidase with a broad substrate specificity: purification and characterizationEnzyme Microb. Technol.3177-872002Rhodococcus opacus-
653762Geueke, B.; Hummel, W.Heterologous expression of Rhodococcus opacus L-Amino acid oxidase of Streptomyces lividansProtein Expr. Purif.28303-3092003Rhodococcus opacus PubMed
654119Zhang, H.; Teng, M.; Niu, L.; Wang, Y.; Liu, Q.; Huang, Q.; Hao, Q.; Dong, Y.; Liu, P.Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venomActa Crystallogr. Sect. D60974-9772004Gloydius halys PubMed
654441Zhang, Y.J.; Wang, J.H.; Lee, W.H.; Wang, Q.; Liu, H.; Zheng, Y.T.; Zhang, Y.Molecular characterization of Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activityBiochem. Biophys. Res. Commun.309598-6042003Viridovipera stejnegeri PubMed
654872Sakurai, Y.; Shima, M.; Matsumoto, T.; Takatsuka, H.; Nishiya, K.; Kasuda, S.; Fujimura, Y.; Yoshioka, A.Anticoagulant activity of M-LAO, L-amino acid oxidase purified from Agkistrodon halys blomhoffii, through selective inhibition of factor IXBiochim. Biophys. Acta164951-572003Gloydius blomhoffi PubMed
654954Stabeli, R.G.; Marcussi, S.; Carlos, G.B.; Pietro, R.C.; Selistre-de-Araujo, H.S.; Giglio, J.R.; Oliveira, E.B.; Soares, A.M.Platelet aggregation and antibacterial effects of an l-amino acid oxidase purified from snake venomBioorg. Med. Chem.122881-28862004Bothrops alternatus PubMed
655316Iijima, R.; Kisugi, J.; Yamazaki, M.L-amino acid oxidase activity of an antineoplastic factor of a marine mollusk and its relationship to cytotoxicityDev. Comp. Immunol.27505-5122003Dolabella auricularia PubMed
656435Mason, J.M.; Naidu, M.D.; Barcia, M.; Porti, D.; Chavan, S.S.; Chu, C.C.IL-4-induced gene-1 is a leukocyte L-amino acid oxidase with an unusual acidic pH preference and lysosomal localizationJ. Immunol.1734561-45672004Mus musculus PubMed
656581Lu, Q.M.; Wei, Q.; Jin, Y.; Wei, J.F.; Wang, W.Y.; Xiong, Y.L.L-amino acid oxidase from Trimeresurus jerdonii snake venom: purification, characterization, platelet aggregation-inducing and antibacterial effectsJ. Nat. Toxins11345-3522002Protobothrops jerdonii PubMed
661038Cooper, A.J.; Pinto, J.T.Aminotransferase, L-amino acid oxidase and beta-lyase reactions involving L-cysteine S-conjugates found in allium extracts. Relevance to biological activity?Biochem. Pharmacol.69209-2202005Crotalus adamanteus PubMed
667079Faust, A.; Geueke, B.; Niefind, K.; Hummel, W.; Schomburg, D.Crystallization and preliminary X-ray analysis of a bacterial L-amino-acid oxidase from Rhodococcus opacusActa crystallogr. Sect. F62279-2812006Rhodococcus opacus PubMed
667235Ande, S.R.; Kommoju, P.R.; Draxl, S.; Murkovic, M.; Macheroux, P.; Ghisla, S.; Ferrando-May, E.Mechanisms of cell death induction by L-amino acid oxidase, a major component of ophidian venomApoptosis111439-14512006Calloselasma rhodostoma PubMed
667254Davis, M.A.; Askin, M.C.; Hynes, M.J.Amino acid catabolism by an areA-regulated gene encoding an L-amino acid oxidase with broad substrate specificity in Aspergillus nidulansAppl. Environ. Microbiol.713551-35552005Emericella nidulans PubMed
667368Findrik, Z.; Vasic-Racki, E.; Primozic, M.; Habulin, M.; Knez, Z.Enzymatic activity of L-amino acid oxidase from snake venom Crotalus adamanteus in supercritical CO2Biocatal. Biotransform.23315-3212005Crotalus adamanteus-
667933Izidoro, L.F.; Ribeiro, M.C.; Souza, G.R.; SantAna, C.D.; Hamaguchi, A.; Homsi-Brandeburgo, M.I.; Goulart, L.R.; Beleboni, R.O.; Nomizo, A.; Sampaio, S.V.; Soares, A.M.; Rodrigues, V.M.Biochemical and functional characterization of an L-amino acid oxidase isolated from Bothrops pirajai snake venomBioorg. Med. Chem.147034-70432006Bothrops pirajai PubMed
668580Kitani, Y.; Tsukamoto, C.; Zhang, G.; Nagai, H.; Ishida, M.; Ishizaki, S.; Shimakura, K.; Shiomi, K.; Nagashima, Y.Identification of an antibacterial protein as L-amino acid oxidase in the skin mucus of rockfish Sebastes schlegeliFEBS J.274125-1362007Sebastes schlegelii PubMed
669658Yang, H.; Johnson, P.M.; Ko, K.C.; Kamio, M.; Germann, M.W.; Derby, C.D.; Tai, P.C.Cloning, characterization and expression of escapin, a broadly antimicrobial FAD-containing L-amino acid oxidase from ink of the sea hare Aplysia californicaJ. Exp. Biol.2083609-36222005Aplysia californica PubMed
669893Moustafa, I.M.; Foster, S.; Lyubimov, A.Y.; Vrielink, A.Crystal structure of LAAO from Calloselasma rhodostoma with an L-phenylalanine substrate: insights into structure and mechanismJ. Mol. Biol.364991-10022006Calloselasma rhodostoma PubMed
669894Faust, A.; Niefind, K.; Hummel, W.; Schomburg, D.The structure of a bacterial l-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenationJ. Mol. Biol.367234-2482006Rhodococcus opacus PubMed
670798Kommoju, P.R.; Macheroux, P.; Ghisla, S.Molecular cloning, expression and purification of L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostomaProtein Expr. Purif.5289-952007Calloselasma rhodostoma PubMed
670963Butzke, D.; Hurwitz, R.; Thiede, B.; Goedert, S.; Rudel, T.Cloning and biochemical characterization of APIT, a new L-amino acid oxidase from Aplysia punctataToxicon46479-4892005Aplysia punctata PubMed
670964Toyama, M.H.; Toyama, D.d.e.O.; Passero, L.F.; Laurenti, M.D.; Corbett, C.E.; Tomokane, T.Y.; Fonseca, F.V.; Antunes, E.; Joazeiro, P.P.; Beriam, L.O.; Martins, M.A.; Monteiro, H.S.; Fonteles, M.C.Isolation of a new L-amino acid oxidase from Crotalus durissus cascavella venomToxicon4747-572006Crotalus durissus cascavella PubMed
670968Tonismaegi, K.; Samel, M.; Trummal, K.; Roennholm, G.; Siigur, J.; Kalkkinen, N.; Siigur, E.L-amino acid oxidase from Vipera lebetina venom: isolation, characterization, effects on platelets and bacteriaToxicon48227-2372006Macrovipera lebetina PubMed
690221Li, R.; Zhu, S.; Wu, J.; Wang, W.; Lu, Q.; Clemetson, K.J.L-amino acid oxidase from Naja atra venom activates and binds to human plateletsActa Biochim. Biophys. Sin.4019-262008Naja atra PubMed
690575Gomez, D.; Espinosa, E.; Bertazzo, M.; Lucas-Elio, P.; Solano, F.; Sanchez-Amat, A.The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an L: -amino acid oxidaseAppl. Microbiol. Biotechnol.79925-9302008Pseudoalteromonas luteoviolacea PubMed
690684De Vieira Santos, M.M.; SantAna, C.D.; Giglio, J.R.; da Silva, R.J.; Sampaio, S.V.; Soares, A.M.; Fecchio, D.Antitumoural effect of an L-amino acid oxidase isolated from Bothrops jararaca snake venomBasic Clin. Pharmacol. Toxicol.102533-5422008Bothrops jararaca PubMed
690693Franca, S.C.; Kashima, S.; Roberto, P.G.; Marins, M.; Ticli, F.K.; Pereira, J.O.; Astolfi-Filho, S.; Stabeli, R.G.; Magro, A.J.; Fontes, M.R.; Sampaio, S.V.; Soares, A.M.Molecular approaches for structural characterization of Bothrops L-amino acid oxidases with antiprotozoal activity: cDNA cloning, comparative sequence analysis, and molecular modelingBiochem. Biophys. Res. Commun.355302-3062007Bothrops jararacussu, Bothrops moojeni PubMed
690856Sant'Ana, C.D.; Menaldo, D.L.; Costa, T.R.; Godoy, H.; Muller, V.D.; Aquino, V.H.; Albuquerque, S.; Sampaio, S.V.; Monteiro, M.C.; Stabeli, R.G.; Soares, A.M.Antiviral and antiparasite properties of an L-amino acid oxidase from the snake Bothrops jararaca: cloning and identification of a complete cDNA sequenceBiochem. Pharmacol.76279-2882008Bothrops jararaca PubMed
691917Kitani, Y.; Kikuchi, N.; Zhang, G.; Ishizaki, S.; Shimakura, K.; Shiomi, K.; Nagashima, Y.Antibacterial action of L-amino acid oxidase from the skin mucus of rockfish Sebastes schlegeliiComp. Biochem. Physiol. B Biochem. Mol. Biol.149394-4002008Sebastes schlegelii PubMed
691918Samel, M.; Tonismaegi, K.; Roennholm, G.; Vija, H.; Siigur, J.; Kalkkinen, N.; Siigur, E.L-Amino acid oxidase from Naja naja oxiana venomComp. Biochem. Physiol. B Biochem. Mol. Biol.149572-5802008Naja oxiana PubMed
692288Mandal, S.; Bhattacharyya, D.Two L-amino acid oxidase isoenzymes from Russells viper (Daboia russelli russelli) venom with different mechanisms of inhibition by substrate analogsFEBS J.2752078-20952008Daboia russellii russellii PubMed
692408Kitani, Y.; Mori, T.; Nagai, H.; Toyooka, K.; Ishizaki, S.; Shimakura, K.; Shiomi, K.; Nagashima, Y.Gene expression and distribution of antibacterial L-amino acid oxidase in the rockfish Sebastes schlegeliFish Shellfish Immunol.231178-11862007Sebastes schlegelii PubMed
692650Stabeli, R.G.; SantAna, C.D.; Ribeiro, P.H.; Costa, T.R.; Ticli, F.K.; Pires, M.G.; Nomizo, A.; Albuquerque, S.; Malta-Neto, N.R.; Marins, M.; Sampaio, S.V.; Soares, A.M.Cytotoxic L-amino acid oxidase from Bothrops moojeni: biochemical and functional characterizationInt. J. Biol. Macromol.41132-1402007Bothrops moojeni PubMed
692863Tong, H.; Chen, W.; Shi, W.; Qi, F.; Dong, X.SO-LAAO, a novel L-amino acid oxidase that enables Streptococcus oligofermentans to outcompete Streptococcus mutans by generating H2O2 from peptoneJ. Bacteriol.1904716-47212008Streptococcus oligofermentans PubMed
693949Zhang, L.; Wei, L.J.ACTX-8, a cytotoxic L-amino acid oxidase isolated from Agkistrodon acutus snake venom, induces apoptosis in Hela cervical cancer cellsLife Sci.801189-11972007Deinagkistrodon acutus PubMed
694300Nuutinen, J.; Timonen, S.Identification of nitrogen mineralization enzymes, L-amino acid oxidases, from the ectomycorrhizal fungi Hebeloma spp. and Laccaria bicolorMycol. Res.1121453-14642008Crotalus atrox, Hebeloma cylindrosporum, Hebeloma sp., Laccaria bicolor PubMed
694317Zhang, L.; Wu, W.T.Isolation and characterization of ACTX-6: a cytotoxic L-amino acid oxidase from Agkistrodon acutus snake venomNat. Prod. Res.22554-5632008Deinagkistrodon acutus PubMed
695208Wei, X.L.; Wei, J.F.; Li, T.; Qiao, L.Y.; Liu, Y.L.; Huang, T.; He, S.H.Purification, characterization and potent lung lesion activity of an L-amino acid oxidase from Agkistrodon blomhoffii ussurensis snake venomToxicon501126-11392007Agkistrodon blomhoffi ussuriensis PubMed
695209Jin, Y.; Lee, W.H.; Zeng, L.; Zhang, Y.Molecular characterization of L-amino acid oxidase from king cobra venomToxicon50479-4892007Bungarus fasciatus, Bungarus multicinctus, Naja atra, Ophiophagus hannah PubMed
695212Braga, M.D.; Martins, A.M.; Amora, D.N.; de Menezes, D.B.; Toyama, M.H.; Toyama, D.O.; Marangoni, S.; Alves, C.D.; Barbosa, P.S.; de Sousa Alves, R.; Fonteles, M.C.; Monteiro, H.S.Purification and biological effects of L-amino acid oxidase isolated from Bothrops insularis venomToxicon51199-2072008Bothrops insularis PubMed
695276Ande, S.R.; Fussi, H.; Knauer, H.; Murkovic, M.; Ghisla, S.; Froehlich, K.U.; Macheroux, P.Induction of apoptosis in yeast by L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostomaYeast25349-3572008Calloselasma rhodostoma PubMed
695281Gau, A.E.; Heindl, A.; Nodop, A.; Kahmann, U.; Pistorius, E.K.L-amino acid oxidases with specificity for basic L-amino acids in cyanobacteriaZ. Naturforsch. C62273-2842007Gloeobacter violaceus PCC 7421, no activity in Anabaena variabilis ATCC 29413, no activity in Prochlorococcus marinus, no activity in Synechococcus sp., no activity in Synechococcus sp. WH 8102, no activity in Thermosynechococcus elongatus BP-1, Nostoc punctiforme PCC 73102, Nostoc sp. PCC 7120, Synechococcus cedrorum PCC 6908, Synechococcus elongatus PCC 6301, Synechococcus elongatus PCC 7942, Synechococcus sp. CC9605, Synechococcus sp. WH 5701, Synechococcus sp. WH 7805, Synechocystis sp. PCC 6803, Trichodesmium erythraeum IMS101 PubMed
695361Georgieva, D.; Kardas, A.; Buck, F.; Perbandt, M.; Betzel, C.Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venomActa Crystallogr. Sect. F64918-9212008Vipera ammodytes ammodytes PubMed
695637Ko, K.C.; Wang, B.; Tai, P.C.; Derby, C.D.Identification of potent bactericidal compounds produced by escapin, an L-amino acid oxidase in the ink of the sea hare Aplysia californicaAntimicrob. Agents Chemother.524455-44622008Aplysia californica PubMed
696493Rodrigues, R.S.; da Silva, J.F.; Boldrini Franca, J.; Fonseca, F.P.; Otaviano, A.R.; Henrique Silva, F.; Hamaguchi, A.; Magro, A.J.; Braz, A.S.; dos Santos, J.I.; Homsi-Brandeburgo, M.I.; Fontes, M.R.; Fuly, A.L.; Soares, A.M.; Rodrigues, V.M.Structural and functional properties of Bp-LAAO, a new L-amino acid oxidase isolated from Bothrops pauloensis snake venomBiochimie91490-5012009Bothropoides pauloensis PubMed
697333Kamio, M.; Ko, K.C.; Zheng, S.; Wang, B.; Collins, S.L.; Gadda, G.; Tai, P.C.; Derby, C.D.The chemistry of escapin: identification and quantification of the components in the complex mixture generated by an L-amino acid oxidase in the defensive secretion of the sea snail Aplysia californicaChemistry151597-16032009Aplysia californica PubMed
697450Alves, R.M.; Antonucci, G.A.; Paiva, H.H.; Cintra, A.C.; Franco, J.J.; Mendonca-Franqueiro, E.P.; Dorta, D.J.; Giglio, J.R.; Rosa, J.C.; Fuly, A.L.; Dias-Baruffi, M.; Soares, A.M.; Sampaio, S.V.Evidence of caspase-mediated apoptosis induced by l-amino acid oxidase isolated from Bothrops atrox snake venomComp. Biochem. Physiol. A151542-5502008Bothrops atrox PubMed
697466Nagashima, Y.; Tsukamoto, C.; Kitani, Y.; Ishizaki, S.; Nagai, H.; Yanagimoto, T.Isolation and cDNA cloning of an antibacterial L-amino acid oxidase from the skin mucus of the great sculpin Myoxocephalus polyacanthocephalusComp. Biochem. Physiol. B15455-612009Myoxocephalus polyacanthocephalus PubMed
697859Nagaoka, K.; Aoki, F.; Hayashi, M.; Muroi, Y.; Sakurai, T.; Itoh, K.; Ikawa, M.; Okabe, M.; Imakawa, K.; Sakai, S.L-amino acid oxidase plays a crucial role in host defense in the mammary glandsFASEB J.232514-25202009Mus musculus PubMed
698669Fujisawa, D.; Yamazaki, Y.; Morita, T.Re-evaluation of M-LAO, L-amino acid oxidase, from the venom of Gloydius blomhoffi as an anticoagulant proteinJ. Biochem.14643-492009Gloydius blomhoffi PubMed
699933Carbonnelle-Puscian, A.; Copie-Bergman, C.; Baia, M.; Martin-Garcia, N.; Allory, Y.; Haioun, C.; Cremades, A.; Abd-Alsamad, I.; Farcet, J.; Gaulard, P.; Castellano, F.; Molinier-Frenkel, V.The novel immunosuppressive enzyme IL4I1 is expressed by neoplastic cells of several B-cell lymphomas and by tumor-associated macrophagesLeukemia23952-9602009Homo sapiens PubMed
701330Ciscotto, P.; Machado de Avila, R.A.; Coelho, E.A.; Oliveira, J.; Diniz, C.G.; Farias, L.M.; de Carvalho, M.A.; Maria, W.S.; Sanchez, E.F.; Borges, A.; Chavez-Olortegui, C.Antigenic, microbicidal and antiparasitic properties of an L-amino acid oxidase isolated from Bothrops jararaca snake venomToxicon53330-3412009Bothrops jararaca PubMed
701332Wei, J.F.; Yang, H.W.; Wei, X.L.; Qiao, L.Y.; Wang, W.Y.; He, S.H.Purification, characterization and biological activities of the L-amino acid oxidase from Bungarus fasciatus snake venomToxicon54262-2712009Bungarus fasciatus PubMed
701333Zhong, S.R.; Jin, Y.; Wu, J.B.; Jia, Y.H.; Xu, G.L.; Wang, G.C.; Xiong, Y.L.; Lu, Q.M.Purification and characterization of a new L-amino acid oxidase from Daboia russellii siamensis venomToxicon54763-7712009Daboia russellii siamensis PubMed
711329Sun, M.Z.; Guo, C.; Tian, Y.; Chen, D.; Greenaway, F.T.; Liu, S.Biochemical, functional and structural characterization of Akbu-LAAO: a novel snake venom L-amino acid oxidase from Agkistrodon blomhoffii ussurensisBiochimie92343-3492010Agkistrodon blomhoffi ussuriensis PubMed
711786Kitani, Y.; Ishida, M.; Ishizaki, S.; Nagashima, Y.Discovery of serum L-amino acid oxidase in the rockfish Sebastes schlegeli: isolation and biochemical characterizationComp. Biochem. Physiol. B157351-3562010Sebastes schlegelii PubMed
711791Lee, 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) venomComp. Biochem. Physiol. C153237-2422010Ophiophagus hannah PubMed
711872Chen, W.; Lin, C.; Chen, C.; Wang, J.; Sheu, S.Involvement of an l-amino acid oxidase in the activity of the marine bacterium Pseudoalteromonas flavipulchra against methicillin-resistant Staphylococcus aureusEnzyme Microb. Technol.4752-582010Pseudoalteromonas flavipulchra-
711874Isobe, K.; Tamauchi, H.; Fuhshuku, K.; Nagasawa, S.; Asano, Y.A simple enzymatic method for production of a wide variety of D-amino acids using L-amino acid oxidase from Rhodococcus sp. AIU Z-35-1Enzyme Res.20105672102010Rhodococcus sp. PubMed
711980Stasyk, T.; Lutsik-Kordovsky, M.; Wernstedt, C.; Antonyuk, V.; Klyuchivska, O.; Souchelnytskyi, S.; Hellman, U.; Stoika, R.A new highly toxic protein isolated from the death cap Amanita phalloides is an L-amino acid oxidaseFEBS J.2771260-12692010Amanita phalloides PubMed
711987Kasai, K.; Ishikawa, T.; Komata, T.; Fukuchi, K.; Chiba, M.; Nozaka, H.; Nakamura, T.; Sato, T.; Miura, T.Novel L-amino acid oxidase with antibacterial activity against methicillin-resistant Staphylococcus aureus isolated from epidermal mucus of the flounder Platichthys stellatusFEBS J.277453-4652010Platichthys stellatus PubMed
712998Georgieva, D.; Murakami, M.; Perband, M.; Arni, R.; Betzel, C.The structure of a native L-amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ionsMol. Biosyst.7379-3842010Vipera ammodytes ammodytes PubMed
713525Qi, L.; Yang, G.; Zhang, H.; Qiao, J.A chiral ligand exchange CE essay with zinc(II)-L-valine complex for determining enzyme kinetic constant of L-amino acid oxidaseTalanta811554-15592010Crotalus atrox PubMed
713558Costa Torres, A.F.; Dantas, R.T.; Toyama, M.H.; Diz Filho, E.; Zara, F.J.; Rodrigues de Queiroz, M.G.; Pinto Nogueira, N.A.; Rosa de Oliveira, M.; de Oliveira Toyama, D.; Monteiro, H.S.; Martins, A.M.Antibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: phospholipase A2 and L-amino acid oxidaseToxicon55795-8042010Bothrops marajoensis PubMed
713559Deolindo, P.; Teixeira-Ferreira, A.S.; DaMatta, R.A.; Alves, E.W.L-amino acid oxidase activity present in fractions of Bothrops jararaca venom is responsible for the induction of programmed cell death in Trypanosoma cruziToxicon56944-9552010Bothrops jararaca PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.4.3.2)
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