OXLA_APLCA
ID OXLA_APLCA Reviewed; 535 AA.
AC Q6IWZ0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:16155232};
DE Short=LAAO {ECO:0000303|PubMed:16155232};
DE Short=LAO {ECO:0000250|UniProtKB:P81382};
DE EC=1.4.3.2 {ECO:0000269|PubMed:16155232, ECO:0000269|PubMed:18852282, ECO:0000269|PubMed:19130530};
DE AltName: Full=Escapin {ECO:0000303|PubMed:16155232};
DE Flags: Precursor;
OS Aplysia californica (California sea hare).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC Aplysiidae; Aplysia.
OX NCBI_TaxID=6500;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAT12273.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND LACK OF
RP GLYCOSYLATION.
RC TISSUE=Ink {ECO:0000269|PubMed:16155232}, and
RC Ink gland {ECO:0000269|PubMed:16155232};
RX PubMed=16155232; DOI=10.1242/jeb.01795;
RA Yang H., Johnson P.M., Ko K.C., Kamio M., Germann M.W., Derby C.D.,
RA Tai P.C.;
RT "Cloning, characterization and expression of escapin, a broadly
RT antimicrobial FAD-containing L-amino acid oxidase from ink of the sea hare
RT Aplysia californica.";
RL J. Exp. Biol. 208:3609-3622(2005).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16354780; DOI=10.1242/jeb.01972;
RA Johnson P.M., Kicklighter C.E., Schmidt M., Kamio M., Yang H., Elkin D.,
RA Michel W.C., Tai P.C., Derby C.D.;
RT "Packaging of chemicals in the defensive secretory glands of the sea hare
RT Aplysia californica.";
RL J. Exp. Biol. 209:78-88(2006).
RN [3] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Ink {ECO:0000269|PubMed:18852282};
RX PubMed=18852282; DOI=10.1128/aac.01103-08;
RA Ko K.C., Wang B., Tai P.C., Derby C.D.;
RT "Identification of potent bactericidal compounds produced by escapin, an L-
RT amino acid oxidase in the ink of the sea hare Aplysia californica.";
RL Antimicrob. Agents Chemother. 52:4455-4462(2008).
RN [4] {ECO:0000305}
RP CATALYTIC ACTIVITY.
RC TISSUE=Ink {ECO:0000269|PubMed:19130530};
RX PubMed=19130530; DOI=10.1002/chem.200801696;
RA Kamio M., Ko K.C., Zheng S., Wang B., Collins S.L., Gadda G., Tai P.C.,
RA Derby C.D.;
RT "The chemistry of escapin: identification and quantification of the
RT components in the complex mixture generated by an L-amino acid oxidase in
RT the defensive secretion of the sea snail Aplysia californica.";
RL Chemistry 15:1597-1603(2009).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=20570851; DOI=10.1086/bblv218n3p282;
RA Nusnbaum M., Derby C.D.;
RT "Effects of sea hare ink secretion and its escapin-generated components on
RT a variety of predatory fishes.";
RL Biol. Bull. 218:282-292(2010).
CC -!- FUNCTION: Catalyzes the oxidative deamination of positively charged L-
CC amino acids L-Lys and L-Arg and, much less efficiently, of amino acids
CC L-His and L-Tyr. Has antimicrobial activity. Inhibits growth of Gram-
CC negative bacteria E.coli strain MC4100 (MIC=0.62 ug/ml), E.coli strain
CC C921-b2, S.typhimurium strain AA 140 (MIC=0.62 ug/ml), P.aeruginosa
CC strain PAO1 (MIC=0.31 ug/ml) and V.harveyi strain BB170 (MIC=0.25
CC ug/ml). Inhibits growth of Gram-positive bacteria S.aureus strain 6835
CC (MIC=0.31 ug/ml), S.pyogenes strain NZ131 (MIC=0.62 ug/ml), B.subtilis
CC strain 168 (MIC=2.50 ug/ml) and B.subtilis strain WB600 (MIC=2.50
CC ug/ml). The antibacterial effect can be bacteriostatic, mediated mostly
CC by H(2)O(2), as well as bactericidal. The latter appears to be due to
CC unstable intermediates generated from alpha-keto-epsilon-aminocaproic
CC acid, an intermediate of escapin-deaminated L-Lys, and H(2)O(2). The
CC bactericidal effect is stronger at lower pH levels. Intermediates
CC generated from L-Arg have no bactericidal effect. Inhibits growth of
CC yeast species S.cerevisiae strain BY4761 (MIC=5.0 ug/ml) and C.krusei
CC (MIC=5.0 ug/ml). Inhibits growth of C.sphaerospermum in a lysine-
CC dependent manner. As components of ink, products from escapin's
CC enzymatic activity may play a role in deterring eukaryotic predators.
CC {ECO:0000269|PubMed:16155232, ECO:0000269|PubMed:18852282,
CC ECO:0000269|PubMed:20570851}.
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:16155232,
CC ECO:0000269|PubMed:18852282, ECO:0000269|PubMed:19130530};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16155232};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=85.5 uM for L-Lys {ECO:0000269|PubMed:16155232};
CC KM=120.5 uM for L-Arg {ECO:0000269|PubMed:16155232};
CC Vmax=4.5 umol/sec/ug enzyme with L-Lys as substrate
CC {ECO:0000269|PubMed:16155232};
CC Vmax=5.5 umol/sec/ug enzyme with L-Arg as substrate
CC {ECO:0000269|PubMed:16155232};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16354780}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in the ink gland. Within the
CC ink gland, it is only detected in amber vesicles (at protein level).
CC {ECO:0000269|PubMed:16354780}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:16155232}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000255}.
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DR EMBL; AY615888; AAT12273.1; -; mRNA.
DR RefSeq; NP_001191570.1; NM_001204641.2.
DR AlphaFoldDB; Q6IWZ0; -.
DR SMR; Q6IWZ0; -.
DR GeneID; 100533346; -.
DR OrthoDB; 367611at2759; -.
DR BRENDA; 1.4.3.2; 390.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of 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; Direct protein sequencing; FAD; Flavoprotein;
KW Fungicide; Oxidoreductase; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:16155232"
FT CHAIN 19..535
FT /note="L-amino-acid oxidase"
FT /evidence="ECO:0000269|PubMed:16155232"
FT /id="PRO_5000093471"
FT BINDING 46..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 66..67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 74
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 91..94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 406
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 513..518
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 513..514
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
SQ SEQUENCE 535 AA; 60300 MW; 4F288F95F9B423FC CRC64;
MSSAFLLLAC ALVISVHADG VCRNRRQCNK EVCGSSYDVA IVGAGPGGAN SAYMLRESGL
DIAVFEYSDR VGGRLFTYQL PNTPDVNLEI GGMRFIEGAM HRLWKVISEL GLTPKVFKEG
FGKEGRQRFY LRGQSLTKKQ VKSGDVPYDL SPEEKANQGR LVEYYLEKLT GLQLNGGPLK
REVALKLTVP DGRFLYDLTF DEALDLVASP EGKEFARDTH VFTSEVTLDA SAISIFDDHL
GEDYYGSEIY TLEEGMSSVP QGLLQTFLDA AKSNEFFPNN HLKALRRRTN GQYVLYFEPT
TSKDGQTTIN YLEPLKVVCA QRVILAMPVY ALRQLDWSQL RNDRATQAYR AVRPMPASKV
FMTFDQPWWL QNERKSWVTK SDALFSQMYD WQKSEASGDY ILIASYADGL KAQYLRELKN
QGEDIPGSDP GYNQVTVPLK DAILEHLTEA YGVERDSIPE PVTAASQFWT DYPFGCGWIT
WRAGYHFDDV ISTMRRPSLK DEVYVVGSDY SWGLISSWIE GALETSENVI NDYFL
