OXLAB_CERCE
ID OXLAB_CERCE Reviewed; 172 AA.
AC P0DQH9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=L-amino acid oxidase {ECO:0000303|PubMed:30647580};
DE AltName: Full=CC-LAAO {ECO:0000303|PubMed:30647580};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:30647580};
DE Flags: Fragments;
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 PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND SUBSTRATE
RP SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=30647580; DOI=10.1016/j.jgeb.2015.09.003;
RA El Hakim A.E., Salama W.H., Hamed M.B., Ali A.A., Ibrahim N.M.;
RT "Heterodimeric l-amino acid oxidase enzymes from Egyptian Cerastes cerastes
RT venom: Purification, biochemical characterization and partial amino acid
RT sequencing.";
RL J. Genet. Eng. Biotechnol. 13:165-176(2015).
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:30647580). Shows high specificity for L-Arg, L-Met, L-
CC Phe, L-Leu, L-Tyr, L-Ile and L-Trp, low specificity for L-Val, L-Ala,
CC L-Asn, L-Gln, and no specificity for L-Pro, L-Ser, L-Thr, L-Cys, L-Gly
CC and L-Asp (PubMed:30647580). Exhibits diverse biological activities,
CC such as hemorrhage, hemolysis, edema, antibacterial and antiparasitic
CC activities, as well as regulation of platelet aggregation. Its effect
CC on 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. {ECO:0000250,
CC ECO:0000269|PubMed:30647580}.
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:30647580};
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:30647580};
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:30647580};
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:30647580};
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:30647580};
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:30647580};
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:30647580};
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:30647580};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- ACTIVITY REGULATION: Activity is increased by Mn(2+) ions. Inhibited by
CC Zn(2+), Ni(2+), Co(2+), Cu(2+) and Al(3+). No significant activity
CC change by Na(+), K(+), Ca(2+), Mg(2+) and Ba(2+) ions. Both isoform are
CC completely inhibited by L-Cys and reduced glutathione. O-
CC phenanthroline, beta-mercaptoethanol and PMSF completely inhibit the
CC enzymatic activity of LAAOII, but have no activity on LAAOI. Iodoacitic
CC acid inhibits the enzymatic activity of LAAOII by 46% but has no effect
CC on the LAAOI activity. {ECO:0000269|PubMed:30647580}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.67 mM for L-Leu (Cc-LAAOI isoform)
CC {ECO:0000269|PubMed:30647580};
CC KM=0.82 mM for L-Leu (Cc-LAAOII isoform)
CC {ECO:0000269|PubMed:30647580};
CC pH dependence:
CC Optimum pH is 7.8 (Cc-LAAOI) and 7 (Cc-LAAOII).
CC {ECO:0000269|PubMed:30647580};
CC Temperature dependence:
CC Optimum temperature is 50 (Cc-LAAOI) and 60 (Cc-LAAOII) degrees
CC Celsius. {ECO:0000269|PubMed:30647580};
CC -!- SUBUNIT: Heterodimer; non-covalently linked.
CC {ECO:0000305|PubMed:30647580}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30647580}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:30647580}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Two L-amino-acid oxidase isoforms from C.cerastes venom have
CC been described: Cc-LAAOI and Cc-LAAOII. Both isoforms show very similar
CC activities on different substrates tested, as well as for activity
CC regulation by metal ions. It is unknown which isoform is presented
CC here. {ECO:0000269|PubMed:30647580}.
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DR AlphaFoldDB; P0DQH9; -.
DR SMR; P0DQH9; -.
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 GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW Hemostasis impairing toxin; Oxidoreductase;
KW Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN 1..>172
FT /note="L-amino acid oxidase"
FT /id="PRO_0000448257"
FT BINDING 44..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 10..?
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_CONS 24..25
FT /evidence="ECO:0000303|PubMed:30647580"
FT NON_CONS 33..34
FT /evidence="ECO:0000303|PubMed:30647580"
FT NON_CONS 51..52
FT /evidence="ECO:0000303|PubMed:30647580"
FT NON_CONS 67..68
FT /evidence="ECO:0000303|PubMed:30647580"
FT NON_CONS 89..90
FT /evidence="ECO:0000303|PubMed:30647580"
FT NON_CONS 102..103
FT /evidence="ECO:0000303|PubMed:30647580"
FT NON_CONS 133..134
FT /evidence="ECO:0000303|PubMed:30647580"
FT NON_CONS 145..146
FT /evidence="ECO:0000303|PubMed:30647580"
FT NON_TER 172
FT /evidence="ECO:0000303|PubMed:30647580"
SQ SEQUENCE 172 AA; 19921 MW; 9AC75A4391D4DD5C CRC64;
ADDKNPLEEC FREADYEEFL EIAKVTVLEA SERNDKEDWY ANLGPMRLPE KLNEFVQETE
NGWYFIKYPV KPSEEGKSAG QLYEESLRKS AGQLYQESLG KAHDDIFAYE KRFDEIVDGM
DKLPTSMYQA IQERINFKPP LPPKKYAMGA ITTFTPYQFQ HFSEALTAPV GR
