OXLAA_CERCE
ID OXLAA_CERCE Reviewed; 516 AA.
AC X2JCV5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=L-amino acid oxidase;
DE AltName: Full=CC-LAAO {ECO:0000303|PubMed:25009089};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:25009089};
DE Flags: Precursor;
OS Cerastes cerastes (Horned desert viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Cerastes.
OX NCBI_TaxID=8697;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-48, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=25009089; DOI=10.1016/j.toxicon.2014.06.020;
RA Abdelkafi-Koubaa Z., Jebali J., Othman H., Morjen M., Aissa I.,
RA Zouari-Kesentini R., Bazaa A., Ellefi A.A., Majdoub H., Srairi-Abid N.,
RA Gargouri Y., El Ayeb M., Marrakchi N.;
RT "A thermoactive L-amino acid oxidase from Cerastes cerastes snake venom:
RT purification, biochemical and molecular characterization.";
RL Toxicon 89:32-44(2014).
RN [2]
RP FUNCTION, AND INTERACTION WITH CELL MEMBRANES.
RX PubMed=26433175; DOI=10.1016/j.ijbiomac.2015.09.065;
RA Abdelkafi-Koubaa Z., Aissa I., Morjen M., Kharrat N., El Ayeb M.,
RA Gargouri Y., Srairi-Abid N., Marrakchi N.;
RT "Interaction of a snake venom L-amino acid oxidase with different cell
RT types membrane.";
RL Int. J. Biol. Macromol. 82:757-764(2016).
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:25009089). Is highly active on L-Met>L-Leu>L-Phe>L-
CC Trp=L-Ile (PubMed:25009089). Binds to the cell surface and enables the
CC production of highly localized concentration of hydrogen peroxide in or
CC near the binding interfaces (PubMed:26433175). Does not bind to
CC phospholipids (PubMed:26433175). Induces platelet-rich plasma
CC aggregation, shows cytotoxic effects on some cancer cells lines and
CC shows antibacterial activities against both Gram-positive and Gram-
CC negative bacteria (PubMed:26433175). Also exhibits hemorrhage and edema
CC (By similarity). Does not show cytotoxicity on erythrocytes and
CC peripheral blood mononuclear cells (PubMed:26433175). Its effect on
CC platelets is controversial, since it either induces aggregation or
CC inhibits agonist-induced aggregation. These different effects are
CC probably due to different experimental conditions.
CC {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:25009089,
CC ECO:0000269|PubMed:26433175}.
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;
CC Evidence={ECO:0000269|PubMed:25009089};
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:25009089};
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:25009089};
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:25009089};
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:25009089};
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:25009089};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- ACTIVITY REGULATION: Inhibited by the substrate analog N-acetyl
CC tryptophan. {ECO:0000269|PubMed:25009089}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.10 mM for L-Met {ECO:0000269|PubMed:25009089};
CC KM=0.25 mM for L-Leu {ECO:0000269|PubMed:25009089};
CC KM=0.08 mM for L-Phe {ECO:0000269|PubMed:25009089};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:25009089};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:25009089};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000305|PubMed:25009089}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25009089}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:25009089}.
CC -!- PTM: N-glycosylated (14%). The enzymatic activity remains unchanged
CC after deglycosylation. {ECO:0000269|PubMed:25009089}.
CC -!- MISCELLANEOUS: Two L-amino-acid oxidase isoforms from C.cerastes venom
CC have been described: Cc-LAAOI and Cc-LAAOII. It is unknown which
CC isoform is presented here. {ECO:0000250|UniProtKB:P0DQH9}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000250|UniProtKB:B0VXW0}.
CC -!- CAUTION: Lacks two of the six Cys residues found in other family
CC members, resulting in the lost of one disulfide bond.
CC {ECO:0000305|PubMed:25009089}.
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DR EMBL; KJ028110; AHN53388.1; -; mRNA.
DR AlphaFoldDB; X2JCV5; -.
DR SMR; X2JCV5; -.
DR BRENDA; 1.4.3.2; 1251.
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: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 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; Direct protein sequencing; Disulfide bond; FAD;
KW Flavoprotein; Glycoprotein; Hemostasis impairing toxin; Oxidoreductase;
KW Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:25009089"
FT CHAIN 19..516
FT /note="L-amino acid oxidase"
FT /id="PRO_0000430749"
FT BINDING 61..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 81..82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 105..108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 475
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 482..487
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 482..483
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 349..430
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
SQ SEQUENCE 516 AA; 58557 MW; 41A6F22D886D0235 CRC64;
MNVFFMFSLL FLAALESCAD DKNPLEEEFF EADYEEFLLI AKNGLQQTSN PKRVVIVGAG
MSGLSAAYVL AKTGHEVILL EASERVGGRV STYRNDQEGW YANLGPMRLP ERHRIVREYI
RKFGLQLNEF SQENENAWYF IKNIRKRVGE VNKDPGVLEY PVKPSEKGKS APQLYRDSLQ
KIIEEYGRSN CSYILNKYDT YSTKDYLIKE GNLSPGAVDM VGDLLNEDSG YYVSFIESLK
PDDIFAYENR FDEIVGGFDK LPTSMYQAIQ EKVRLNVRVI KIQQDVKEVT VTYQTPAKNL
SYVTADYVIV CTTSGAARRI KFEPPLPLKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIH
GGKSITDRPS RLIHYPNHNF PNGIGVLVIF TIADDADFFL ALDNKTIADI VIHDLSLIHQ
LPKEKIRDLC YVSMIQKWSL DKYAMGGITT FTPYQFQHFS EALTAPVDRI YFAGEYTAQA
HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEL
