OXLA_TRIPP
ID OXLA_TRIPP Reviewed; 488 AA.
AC P0DPS2;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=L-amino oxidase;
DE Short=CP-LAAO {ECO:0000303|PubMed:29890640};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:29890640};
DE Flags: Fragment;
OS Trimeresurus purpureomaculatus (Mangrove pit viper) (Cryptelytrops
OS purpureomaculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=101163;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=29890640; DOI=10.3390/molecules23061388;
RA Zainal Abidin S.A., Rajadurai P., Hoque Chowdhury M.E., Othman I.,
RA Naidu R.;
RT "Cytotoxic, anti-proliferative and apoptosis activity of L-amino acid
RT oxidase from malaysian Cryptelytrops purpureomaculatus (CP-LAAO) venom on
RT human colon cancer cells.";
RL Molecules 23:0-0(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 diverse toxic effects of this
CC enzyme (PubMed:29890640). Shows activity on L-Leu (PubMed:29890640).
CC Exhibits diverse biological activities, such as hemorrhage, hemolysis,
CC edema, antibacterial and antiparasitic activities, as well as
CC regulation of platelet aggregation (By similarity). In vitro, when
CC tested on colon cancer cells, shows inhibition of cell proliferation,
CC and induction of apoptosis, which is probably a consequence of the
CC increased caspase-3 activity and the decreased Bcl-2 expression
CC (PubMed:29890640). {ECO:0000250|UniProtKB:P0CC17,
CC ECO:0000269|PubMed:29890640}.
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:29890640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13782;
CC Evidence={ECO:0000269|PubMed:29890640};
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:29890640};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.376 mM for L-leucine {ECO:0000269|PubMed:29890640};
CC -!- SUBUNIT: Monomer. This is in contrast with most of its orthologs, that
CC are non-covalently linked homodimers. {ECO:0000269|PubMed:29890640}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29890640}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:29890640}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR SABIO-RK; P0DPS2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC.
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 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; Oxidoreductase; Secreted.
FT CHAIN 1..>488
FT /note="L-amino oxidase"
FT /evidence="ECO:0000269|PubMed:29890640"
FT /id="PRO_0000446020"
FT BINDING 60..61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 80..81
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 104..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 474
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 480..485
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 480..481
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 481..486
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 481..482
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 347..428
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_TER 488
FT /evidence="ECO:0000303|PubMed:29890640"
SQ SEQUENCE 488 AA; 54544 MW; C452E0C6C222C7E5 CRC64;
MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARXXXXTSNP KHVVRVGAGM
SGLSAAYVLA GAGHQVTVLE ASERPGGRXX XXXXXXEGWY ANLGPMRXXX XXXXXXXXXX
KFGLNLNEFS QENDNAWYFI KXXXXXXXXX XDPGLLKYPV KPSEAGKSAG QLYEESLGKX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXFD EIVDGMDKLP TSMYQAIXXX XXXXXXXXXX XXXXXKVTVT YQTPAKXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXIFLTCTKK FWEDDGIHGG
KSTTDLPSRX XXXXXXXXXX XXXVIIAYGI GDDANFFQAL DFKDCADIVF NDLSLIHQLP
KEEIPSFCYP SMIQKXXXXX XXXXXITTFF TPYQFQHFSE AXXXXXXXIY FAGEYTAQAH
GWIDSTIK
