OXLA_CRODU
ID OXLA_CRODU Reviewed; 516 AA.
AC C0HJE7;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 2.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=L-amino acid oxidase bordonein-L {ECO:0000303|PubMed:26273287};
DE Short=LAAO {ECO:0000303|PubMed:26273287};
DE Short=LAO {ECO:0000250|UniProtKB:P0C2D2};
DE EC=1.4.3.2 {ECO:0000269|PubMed:26273287, ECO:0000269|PubMed:31078582};
DE Flags: Precursor;
OS Crotalus durissus terrificus (South American rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8732;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=30270628; DOI=10.1021/acs.jproteome.8b00610;
RA Wiezel G.A., Shibao P.Y.T., Cologna C.T., Morandi Filho R.,
RA Ueira-Vieira C., De Pauw E., Quinton L., Arantes E.C.;
RT "In-depth venome of the Brazilian rattlesnake crotalus durissus terrificus:
RT an integrative approach combining its venom gland transcriptome and venom
RT proteome.";
RL J. Proteome Res. 17:3941-3958(2018).
RN [2]
RP PROTEIN SEQUENCE OF 19-57, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=26273287; DOI=10.1186/s40409-015-0025-8;
RA Bordon K.C., Wiezel G.A., Cabral H., Arantes E.C.;
RT "Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus
RT snake venom: isolation, preliminary characterization and enzyme
RT stability.";
RL J. Venom. Anim. Toxins Incl. Trop. Dis. 21:26-26(2015).
RN [3]
RP PROTEIN SEQUENCE OF 19-31 AND 184-203, IDENTIFICATION BY MASS SPECTROMETRY,
RP 3D-STRUCTURE MODELING, GLYCOSYLATION AT ASN-379, DISULFIDE BOND,
RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE
RP SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=31078582; DOI=10.1016/j.biochi.2019.05.009;
RA Wiezel G.A., Rustiguel J.K., Morgenstern D., Zoccal K.F., Faccioli L.H.,
RA Nonato M.C., Ueberheide B., Arantes E.C.;
RT "Insights into the structure, function and stability of bordonein-L, the
RT first L-amino acid oxidase from Crotalus durissus terrificus snake venom.";
RL Biochimie 163:33-49(2019).
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 diverse toxic effects of this
CC enzyme (PubMed:26273287, PubMed:31078582). Is highly active on L-Met,
CC L-Leu, L-Trp, and L-Phe, moderately active on L-Ile, L-His, and L-Arg,
CC and weakly or not active on L-Gln, L-Val, L-Asn, L-Ala, L-Lys, L-Ser,
CC L-Thr, L-Pro, L-Asp, L-Gly, L-Tyr, L-Cys and L-Glu (PubMed:31078582).
CC This enzyme exhibits diverse biological activities, such as hemorrhage,
CC hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell
CC lines, antibacterial and antiparasitic activities, as well as
CC regulation of platelet aggregation (PubMed:26273287). Its effect on
CC platelets is controversial, since it either induces aggregation or
CC inhibits agonist-induced aggregation (PubMed:26273287). These different
CC effects are probably due to different experimental conditions
CC (PubMed:26273287). In vitro, the enzyme exhibits cytotoxicity against
CC fibroblast cell line and kills Leishmania amazonensis promastigotes,
CC intensified by substrate addition (PubMed:31078582).
CC {ECO:0000269|PubMed:26273287, ECO:0000269|PubMed:31078582}.
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:26273287,
CC ECO:0000269|PubMed:31078582};
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:31078582};
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:31078582};
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:31078582};
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:31078582};
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:31078582};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:31078582};
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:31078582};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P0C2D2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for L-Phe {ECO:0000269|PubMed:31078582};
CC KM=0.48 mM for L-Trp {ECO:0000269|PubMed:31078582};
CC KM=0.58 mM for L-Leu {ECO:0000269|PubMed:31078582};
CC KM=0.97 mM for L-Met {ECO:0000269|PubMed:31078582};
CC KM=3.9 mM for L-Ile {ECO:0000269|PubMed:31078582};
CC pH dependence:
CC Optimum pH is 7.0. Activity is reduced to about 70% and 60% after
CC incubation at pH 5.0 and pH 9.0, respectively, for 1 hour.
CC {ECO:0000269|PubMed:26273287};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:26273287}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26273287}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:26273287}.
CC -!- PTM: N-glycosylated (PubMed:26273287, PubMed:31078582). N-glycan
CC probably consists of the disaccharide N-acetylglucosamine-fucose
CC (HexNAc-Fuc) (PubMed:31078582). {ECO:0000269|PubMed:26273287,
CC ECO:0000269|PubMed:31078582}.
CC -!- MASS SPECTROMETRY: Mass=58702; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:26273287};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HJE7; -.
DR SMR; C0HJE7; -.
DR iPTMnet; C0HJE7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
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;
KW Hemostasis impairing toxin; Oxidoreductase;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..516
FT /note="L-amino acid oxidase bordonein-L"
FT /id="PRO_0000438321"
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 103..106
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 239
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 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:31078582"
FT DISULFID 28..189
FT /evidence="ECO:0000269|PubMed:31078582"
FT DISULFID 349..430
FT /evidence="ECO:0000269|PubMed:31078582"
SQ SEQUENCE 516 AA; 58919 MW; 95B518BF40095212 CRC64;
MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI ARNGLTVTSN PKHVVIVGAG
MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA NLGPMRLPTK HRIVREYIRK
FGLQLNEFFQ ENENAWYFIK NIRKRVREVK NNPGILEYPV KPSEEGKSAA QLYVESLRKV
VKELKRTNCK YILDKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD
DIFGYEKRFD EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDRETK VTYQTSANEM
SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCK RKFWEDDGIR
GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHQ
LPKEDIQTFC RPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPFKRI YFAGEYTAQF
HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF
