OXLA_MICMP
ID OXLA_MICMP Reviewed; 501 AA.
AC A0A2U8QPE6;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=L-amino acid oxidase;
DE Short=LAO;
DE Short=MipLAAO1 {ECO:0000303|PubMed:29900074};
DE EC=1.4.3.2 {ECO:0000269|PubMed:29900074};
DE Flags: Precursor;
OS Micrurus mipartitus (Red-tailed coral snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=430902;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=29900074; DOI=10.7717/peerj.4924;
RA Rey-Suarez P., Acosta C., Torres U., Saldarriaga-Cordoba M., Lomonte B.,
RA Nunez V.;
RT "MipLAAO, a new L-amino acid oxidase from the redtail coral snake Micrurus
RT mipartitus.";
RL PeerJ 6:E4924-E4924(2018).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Venom;
RX PubMed=31129208; DOI=10.1016/j.ijbiomac.2019.05.174;
RA Bedoya-Medina J., Mendivil-Perez M., Rey-Suarez P., Jimenez-Del-Rio M.,
RA Nunez V., Velez-Pardo C.;
RT "L-amino acid oxidase isolated from Micrurus mipartitus snake venom
RT (MipLAAO) specifically induces apoptosis in acute lymphoblastic leukemia
RT cells mostly via oxidative stress-dependent signaling mechanism.";
RL Int. J. Biol. Macromol. 134:1052-1062(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:29900074, PubMed:31129208). Shows activity on L-Leu, L-
CC Trp, and L-Tyr (PubMed:29900074, PubMed:31129208). Is not active on L-
CC His, L-Ser, L-Arg, L-Ala, L-Glu, L-Cys,L-Lys, L-Val, L-Ile, and L-Thr
CC (PubMed:29900074). Induces apoptosis in Jurkat cells through a hydrogen
CC peroxide-mediated signaling pathway dependent mostly on CASPASE-3
CC pathway (PubMed:31129208). Remarkably, does no induce toxic effect on
CC peripheral blood lymphocytes (PubMed:31129208). Also exhibits diverse
CC biological activities, such as hemorrhage, hemolysis, edema, and
CC antiparasitic activities, as well as regulation of platelet aggregation
CC (By similarity). Its effect on platelets is controversial, since it
CC either induces aggregation or inhibits agonist-induced aggregation.
CC These different effects are probably due to different experimental
CC conditions (By similarity). Shows antibacterial activity against
CC S.aureus, but not against E.coli (PubMed:29900074).
CC {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:29900074}.
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:29900074,
CC ECO:0000269|PubMed:31129208};
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:29900074,
CC ECO:0000269|PubMed:31129208};
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:29900074};
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:29900074};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:29900074};
CC -!- SUBUNIT: Monomer. This is in contrast with most of its orthologs, that
CC are non-covalently linked homodimers. {ECO:0000269|PubMed:29900074}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29900074}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:29900074}.
CC -!- MASS SPECTROMETRY: Mass=59100.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:29900074};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MH010800; AWM11661.1; -; mRNA.
DR AlphaFoldDB; A0A2U8QPE6; -.
DR SMR; A0A2U8QPE6; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; 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; 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; Disulfide bond; FAD;
KW Flavoprotein; Glycoprotein; Hemolysis; Hemostasis impairing toxin;
KW Oxidoreductase; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CHAIN 19..501
FT /note="L-amino acid oxidase"
FT /id="PRO_5015972047"
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 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:0000255"
FT DISULFID 28..191
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 349..430
FT /evidence="ECO:0000250|UniProtKB:P81382"
SQ SEQUENCE 501 AA; 57115 MW; 55B97E9DFE1A069A CRC64;
MNVFFMFSLV FLAAFGSCAD DTRPLGECFR EADYEEFLEI ARNGLKKTSN PKHVVVVGAG
MSGLSAAYVL AKAGHKVTLL EASEGVGGRV KTYRNKQEGW YINLGPMRLP ERHRIVREYI
RKFHLPLSEF VQENENTWYY IKNIRKRVSE VKKNPDLFEY PVNPSEKGKS ASQLYQESLE
KVIDELKRTN CNHILNKYDT YSTKEYLIKE GNLSPGAVDM IGDLLNEDSS FYLSFIESLK
SDDIFSYEKR FDEIVGGFDQ LPISMYQAIA EMVHLNAQVI KIQHNAKKVI VTYQTPAKTL
PSVTADYVIV CSTSRAARHI RFQPPLPTNK ARALRSIHYR SAIKIFLTCT KRFWEADGIH
GGKSTTDLPS RFIYYFNQNF TNGIGVIMAY VLADDAKFFQ PHDLKTNADI VINDLSLIHQ
LPKEEIQALC RPSWIQKWSL DKYAMGSITS FTPYQFLDYF EIAAAPVGRI HFAGEYTAKH
HGWIDSTIKS GLRAARDVNR A
