OXLA_BOTMO
ID OXLA_BOTMO Reviewed; 502 AA.
AC Q6TGQ8; A0A2H4N3D4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=L-amino-acid oxidase BmooLAAO-I {ECO:0000303|PubMed:17292326};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:17320169};
DE Flags: Precursor;
OS Bothrops moojeni (Lance-headed viper) (Caissaca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=98334;
RN [1] {ECO:0000312|EMBL:ATU85535.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=29107670; DOI=10.1016/j.toxicon.2017.10.025;
RA Amorim F.G., Morandi-Filho R., Fujimura P.T., Ueira-Vieira C.,
RA Sampaio S.V.;
RT "New findings from the first transcriptome of the Bothrops moojeni snake
RT venom gland.";
RL Toxicon 140:105-117(2017).
RN [2] {ECO:0000312|EMBL:AAR31183.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-490, FUNCTION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom, and Venom gland;
RX PubMed=17292326; DOI=10.1016/j.bbrc.2006.12.217;
RA Franca S.C., Kashima S., Roberto P.G., Marins M., Ticli F.K., Pereira J.O.,
RA Astolfi-Filho S., Stabeli R.G., Magro A.J., Fontes M.R., Sampaio S.V.,
RA Soares A.M.;
RT "Molecular approaches for structural characterization of Bothrops L-amino
RT acid oxidases with antiprotozoal activity: cDNA cloning, comparative
RT sequence analysis, and molecular modeling.";
RL Biochem. Biophys. Res. Commun. 355:302-306(2007).
RN [3]
RP PROTEIN SEQUENCE OF 19-58, FUNCTION, SUBUNIT, GLYCOSYLATION, CIRCULAR
RP DICHROISM, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND SUBSTRATE
RP SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=17320169; DOI=10.1016/j.ijbiomac.2007.01.006;
RA Stabeli R.G., Sant'Ana C.D., Ribeiro P.H., Costa T.R., Ticli F.K.,
RA Pires M.G., Nomizo A., Albuquerque S., Malta-Neto N.R., Marins M.,
RA Sampaio S.V., Soares A.M.;
RT "Cytotoxic L-amino acid oxidase from Bothrops moojeni: biochemical and
RT functional characterization.";
RL Int. J. Biol. Macromol. 41:132-140(2007).
RN [4]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=11162565; DOI=10.1006/bbrc.2000.4175;
RA Tempone A.G., Andrade H.F. Jr., Spencer P.J., Lourenco C.O., Rogero J.R.,
RA Nascimento N.;
RT "Bothrops moojeni venom kills Leishmania spp. with hydrogen peroxide
RT generated by its L-amino acid oxidase.";
RL Biochem. Biophys. Res. Commun. 280:620-624(2001).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=30534149; DOI=10.1186/s40409-018-0172-9;
RA Costa T.R., Carone S.E.I., Tucci L.F.F., Menaldo D.L., Rosa-Garzon N.G.,
RA Cabral H., Sampaio S.V.;
RT "Kinetic investigations and stability studies of two Bothrops L-amino acid
RT oxidases.";
RL J. Venom. Anim. Toxins Incl. Trop. Dis. 24:37-37(2018).
CC -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC hydrophobic and aromatic L-amino acids, thus producing hydrogen
CC peroxide that may contribute to the toxicity of the venom
CC (PubMed:17320169). Shows very high activity on L-Met, and L-Leu, high
CC activity on L-Ile, L-Phe and L-Tyr and moderate activity on L-His, L-
CC Val and L-Ala (PubMed:17320169, PubMed:30534149). Exhibits diverse
CC biological activities, such as edema, apoptosis of tumor cell lines,
CC antibacterial activities against both Gram-positive and Gram-negative
CC bacteria, as well as induction of platelet aggregation. Effects of
CC snake L-amino oxidases on platelets are controversial, since they
CC either induce aggregation or inhibit agonist-induced aggregation. These
CC different effects are probably due to different experimental
CC conditions. Unlike other snake venom L-amino acid oxidases, does not
CC induce hemorrhage. It may also induce hemolysis. Has parasiticidal
CC activities against and leishmania, as a result of enzyme-catalyzed
CC hydrogen peroxide production (PubMed:11162565, PubMed:17292326).
CC {ECO:0000269|PubMed:11162565, ECO:0000269|PubMed:17292326,
CC ECO:0000269|PubMed:17320169, ECO:0000269|PubMed:30534149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:17320169,
CC ECO:0000269|PubMed:30534149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:17320169,
CC ECO:0000269|PubMed:30534149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:17320169,
CC ECO:0000269|PubMed:30534149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+);
CC Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:17320169};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate +
CC H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57844;
CC Evidence={ECO:0000269|PubMed:17320169, ECO:0000269|PubMed:30534149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2
CC + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146,
CC ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:17320169,
CC ECO:0000269|PubMed:30534149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidine + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595,
CC ChEBI:CHEBI:58133; Evidence={ECO:0000269|PubMed:17320169,
CC ECO:0000269|PubMed:30534149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:17320169,
CC ECO:0000269|PubMed:30534149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanine + O2 = H2O2 + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:61264, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:17320169};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-valine + O2 = 3-methyl-2-oxobutanoate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:61252, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57762; Evidence={ECO:0000269|PubMed:17320169};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- ACTIVITY REGULATION: Its enzymatic activities is reduced when it is
CC exposed to Ca(2+), Zn(2+), Al(3+), Cu(2+) or Ni(2+) salts.
CC {ECO:0000269|PubMed:30534149}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for L-Phe {ECO:0000269|PubMed:30534149};
CC KM=0.2 mM for L-Leu {ECO:0000269|PubMed:30534149};
CC KM=0.3 mM for L-Met {ECO:0000269|PubMed:30534149};
CC KM=1.1 mM for L-Tyr {ECO:0000269|PubMed:30534149};
CC KM=1.4 mM for L-Ile {ECO:0000269|PubMed:30534149};
CC KM=7.4 mM for L-His {ECO:0000269|PubMed:30534149};
CC KM=6.1 mM for L-Gln {ECO:0000269|PubMed:30534149};
CC pH dependence:
CC Optimum pH is 5.5-9.5. {ECO:0000269|PubMed:17320169,
CC ECO:0000269|PubMed:30534149};
CC Temperature dependence:
CC Optimum temperature depends on the study: 5-38 degrees Celsius
CC (PubMed:17320169) and 60 degrees Celsius (PubMed:30534149).
CC {ECO:0000269|PubMed:17320169, ECO:0000269|PubMed:30534149};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:11162565, ECO:0000269|PubMed:17320169}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11162565}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:11162565}.
CC -!- PTM: N-glycosylated (Probable). The enzymatic activity is not affected
CC by deglycosylation (PubMed:17320169). {ECO:0000269|PubMed:17320169,
CC ECO:0000305}.
CC -!- MISCELLANEOUS: Shows low or absent catalytic activity on L-Arg, L-Glu,
CC L-Asp, L-Lys, L-Asn, L-Ser, L-Thr, L-Pro, L-Gln, L-Gly, and L-Cys
CC (PubMed:17320169, PubMed:30534149). catalytic activity on L-Val and L-
CC Ala is moderate or low, depending on the study (PubMed:17320169,
CC PubMed:30534149). {ECO:0000269|PubMed:17320169,
CC ECO:0000269|PubMed:30534149}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; MG132016; ATU85535.1; -; mRNA.
DR EMBL; AY398692; AAR31183.1; -; mRNA.
DR AlphaFoldDB; Q6TGQ8; -.
DR SMR; Q6TGQ8; -.
DR BRENDA; 1.4.3.2; 913.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0044532; P:modulation of apoptotic process in another organism; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW Hemostasis impairing toxin; Oxidoreductase;
KW Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:17320169"
FT CHAIN 19..502
FT /note="L-amino-acid oxidase BmooLAAO-I"
FT /evidence="ECO:0000305|PubMed:17320169,
FT ECO:0000305|PubMed:29107670"
FT /id="PRO_0000273565"
FT BINDING 61..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 81..82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 105..108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 475
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 482..487
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 482..483
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..191
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 349..430
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CONFLICT 13..17
FT /note="AALGS -> RKAPC (in Ref. 2; AAR31183)"
FT /evidence="ECO:0000305"
FT CONFLICT 46..47
FT /note="ST -> KS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="S -> W (in Ref. 2; AAR31183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 56840 MW; 435DFE2429791655 CRC64;
MNVFFTFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI AKNGLSTTSN PKRVVIVGAG
MSGLSAAYVL ANAGHQVTVL EASERAGGRV KTYRNEKEGW YANLGPMRLP EKHRIVREYI
RKFDLQLNEF SQENENAWYF IKNIRKRVGE VNKDPGVLEY PVKPSEVGKS AGQLYEESLQ
KAVEELRRTN CSYMLNKYDT YSTKEYLLKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK
HDDIFAYEKR FDEIVGGMDK LPTSMYQAIQ EKVHLNARVI KIQQDVKEVT VTYQTSEKET
LSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIH
GGKSTTDLPS RFIYYPNHNF PNGVGVIIAY GIGDDANYFQ ALDFEDCGDI VINDLSLIHQ
LPKEEIQAIC RPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPVDRI YFAGEYTAQA
HGWIDSTIKS GLRAARDVNS AS
