OXLA_DABRR
ID OXLA_DABRR Reviewed; 504 AA.
AC G8XQX1;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=L-amino-acid oxidase;
DE Short=DrLAO {ECO:0000303|PubMed:21802487};
DE Short=LAAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:21802487};
DE Flags: Precursor;
OS Daboia russelii (Russel's viper) (Vipera russelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=8707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-38, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-241, MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, 3D-STRUCTURE
RP MODELING IN COMPLEX WITH SUBSTRATE, AND SUBSTRATE SPECIFICITY.
RC STRAIN=Eastern India; TISSUE=Venom, and Venom gland;
RX PubMed=21802487; DOI=10.1016/j.biochi.2011.07.022;
RA Chen H.-S., Wang Y.-M., Huang W.-T., Huang K.-F., Tsai I.-H.;
RT "Cloning, characterization and mutagenesis of Russell's viper venom L-amino
RT acid oxidase: insights into its catalytic mechanism.";
RL Biochimie 94:335-344(2012).
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:21802487). Is highly active on L-Tyr followed by L-Phe,
CC L-Met, L-Leu, L-Trp, and weakly active on L-Ile, L-Arg, L-Val, L-Lys,
CC and L-Ala (PubMed:21802487). Inhibits ADP- and collagen-induced
CC platelet aggregation (PubMed:21802487). This inhibition is inhibited by
CC catalase, indicating the importance of generated H(2)O(2) for the
CC inhibitory effect (PubMed:21802487). This effect on platelets among
CC snake L-amino-acid oxidases is however controversial, since some of
CC them induce aggregation, whereas the other inhibit agonist-induced
CC aggregation (By similarity). In vivo, this enzyme induces a rapid,
CC substantial and reversible increase in the paw volume of mice (edema)
CC (PubMed:21802487). In addition, myofibrosis, and inflammatory cell
CC infiltration on the paw tissue are also observed (PubMed:21802487).
CC {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:21802487}.
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:21802487};
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:21802487};
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:21802487};
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:21802487};
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:21802487};
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:21802487};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.081 mM for L-Tyr (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:21802487};
CC KM=0.142 mM for L-Phe (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:21802487};
CC KM=0.373 mM for L-Met (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:21802487};
CC KM=0.318 mM for L-Trp (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:21802487};
CC KM=0.490 mM for L-Leu (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:21802487};
CC KM=1.40 mM for L-Ile (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:21802487};
CC KM=12.20 mM for L-Arg (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:21802487};
CC KM=13.92 mM for L-Val (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:21802487};
CC KM=64.00 mM for L-Lys (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:21802487};
CC KM=116.48 mM for L-Ala (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:21802487};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000250|UniProtKB:P81382}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21802487}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:21802487}.
CC -!- MASS SPECTROMETRY: Mass=62025; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21802487};
CC -!- MISCELLANEOUS: Does not induce dermal hemorrhage when subcutaneously
CC injected into mice at the dose of 40 ug. {ECO:0000305|PubMed:21802487}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; EU663622; ACF70483.1; -; mRNA.
DR AlphaFoldDB; G8XQX1; -.
DR SMR; G8XQX1; -.
DR PRIDE; G8XQX1; -.
DR SABIO-RK; G8XQX1; -.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0043655; C:host extracellular space; NAS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; TAS:UniProtKB.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044398; P:envenomation resulting in induction of edema in another organism; IDA:UniProtKB.
DR GO; GO:0044477; P:envenomation resulting in negative regulation of platelet aggregation in another organism; IDA:UniProtKB.
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 Cytolysis; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Glycoprotein; Hemolysis; Hemostasis impairing toxin; Oxidoreductase;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:21802487"
FT CHAIN 19..504
FT /note="L-amino-acid oxidase"
FT /id="PRO_5000825648"
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 241
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 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
FT MUTAGEN 241
FT /note="H->A: Shows high reactivity toward L-Arg, but does
FT not induce change toward L-Leu, L-Phe and L-Met."
FT /evidence="ECO:0000269|PubMed:21802487"
FT MUTAGEN 241
FT /note="H->N: No change in activity."
FT /evidence="ECO:0000269|PubMed:21802487"
FT MUTAGEN 241
FT /note="H->S: Shows middle reactivity toward L-Arg and L-
FT Phe, but does not induce change toward L-Leu, and L-Met."
FT /evidence="ECO:0000269|PubMed:21802487"
SQ SEQUENCE 504 AA; 56888 MW; 938FBF23BBAA7681 CRC64;
MNVFFMFSLL FLATLGSCAD DKNPLEECFR EDDYEEFLEI AKNGLKKTSN PKHIVIVGAG
MSGLSAAYVL AGAGHKVTVL EASERPGGRV RTHRNVKEGW YANLGPMRVP EKHRIIREYI
RKFGLKLNEF VQETENGWYF IKNIRKRVGE VKKDPGLLKY PVKPSEAGKS AGQLYQESLG
KAVEELKRTN CSYILNKYDT YSTKEYLIKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK
HDDIFAYEKR FDEIVGGMDQ LPTSMYRAIE ESVHFKARVI KIQQNAEKVT VTYQTTQKNL
LLETADYVIV CTTSRAARRI TFKPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIQ
GGKSTTDLPS RFIYYPNHNF TTGVGVIIAY GIGDDANFFQ ALNLNECADI VFNDLSSIHQ
LPKKDLQTFC YPSIIQKWSL DKYAMGAITT FTPYQFQHFS EALTAPVGRI FFAGEYTANA
HGWIDSTIKS GLTAARDVNR ASEL
