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P81383

- OXLA_OPHHA

UniProt

P81383 - OXLA_OPHHA

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Ophiophagus hannah (King cobra) (Naja hannah)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 3 (21 Sep 2011)
      Previous versions | rss
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    Functioni

    Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Unlike most snake L-amino-acid oxidases, this enzyme exhibits potent activity against L-Lys. Has also potent activity against L-Met, L-Leu, L-His, L-Lys and L-Ile. Its activity on platelet aggregation is controversial. It has potent inhibitory activity on platelet aggregation induced by ADP and the thromboxane analog U46619, but not by thrombin, mucetin, ristocetin and stejnulxin (PubMed:17543361), but it has also been shown to induce platelet aggregation through the formation of hydrogen peroxide (PubMed:7886693). It binds to bacteria and shows antibacterial activities by generating hydrogen peroxide. Binding and antibacterial activities are higher against Gram-positive than against Gram-negative bacteria. May also have an ability to induce hemorrhage, hemolysis, edema, apoptosis.6 Publications

    Catalytic activityi

    An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

    Cofactori

    FAD.2 Publications

    Kineticsi

    1. KM=2.3 mM for L-His3 Publications
    2. KM=2.9 mM for L-Ile3 Publications
    3. KM=2.2 mM for L-Leu3 Publications
    4. KM=2.6 mM for L-Lys3 Publications
    5. KM=0.7 mM for L-Met3 Publications
    6. KM=0.20 mM for L-Leu3 Publications
    7. KM=0.63 mM for L-Met3 Publications
    8. KM=0.10 mM for L-Phe3 Publications
    9. KM=0.10 mM for L-Trp3 Publications

    Temperature dependencei

    Exhibits unusual thermal stability. At pH 7.4, the enzyme retains full activity after incubation at 25 degrees Celsius for 30 days. Is stable at alkaline condition and is not inactivated by freezing.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891FADBy similarity
    Binding sitei106 – 1061SubstrateBy similarity
    Binding sitei269 – 2691FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei380 – 3801SubstrateBy similarity
    Binding sitei465 – 4651FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi61 – 622FADBy similarity
    Nucleotide bindingi81 – 822FADBy similarity
    Nucleotide bindingi103 – 1064FADBy similarity
    Nucleotide bindingi472 – 4776FADBy similarity
    Nucleotide bindingi472 – 4732SubstrateBy similarity

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: UniProtKB
    2. L-amino-acid oxidase activity Source: UniProtKB
    3. protein dimerization activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. defense response to bacterium Source: UniProtKB-KW
    3. hemolysis in other organism Source: UniProtKB-KW
    4. killing of cells of other organism Source: UniProtKB
    5. modification of morphology or physiology of other organism Source: UniProtKB

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation inhibiting toxin, Toxin

    Keywords - Biological processi

    Apoptosis, Cytolysis, Hemolysis

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    SABIO-RKP81383.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase (EC:1.4.3.2)
    Short name:
    LAAO
    Short name:
    LAO
    Short name:
    Oh-LAAO
    OrganismiOphiophagus hannah (King cobra) (Naja hannah)
    Taxonomic identifieri8665 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeOphiophagus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Toxic dosei

    LD50 is 5 mg/kg by intravenous injection into mice.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20203 PublicationsAdd
    BLAST
    Chaini21 – 491471L-amino-acid oxidasePRO_0000099871Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 182By similarity
    Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi338 ↔ 420By similarity
    Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.4 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliP81383.
    SMRiP81383. Positions 25-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG005729.

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P81383-1 [UniParc]FASTAAdd to Basket

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    MNDFLLLLLV LFLGVPRSEN HVINLEECFQ EPEYENWLAT ASHGLTKTLN    50
    PKKIVIVGAG ISGLTAAKLF REAGHEVVIL EASDRVGGRI KTHREDGWYV 100
    DVGPMRVPQT HRIVREYIKK FNISLNPFRQ TDENAWYLIK HVRQKMSANN 150
    PENFGYQLNP NERGKSASQL FDETLDKVTD DCTLQKEKYD SFSTKEYLIK 200
    EGKLSTGAVE MIGDFLNEEA GFHNSFLISV MDHFLFLNNS FDEITGGFDQ 250
    LPERFFKDMD SIVHLNSTVE KIVHINNKVT VFYEGLSTNM RLVADYVLIT 300
    ATARATRLIK FVPPLSIPKT RALRSLIYAS ATKIILVCTD KFWEKDGIHG 350
    GRSITDLPSR VIYYPNHDFT NGIGVLLASY TWYSDSEFYT TLSDEKCVDV 400
    VMDDLVEIHN VSKDYLKSVC GKHVVQKWAL DQYSMGAFST YTPYQITHYS 450
    QMLAQNEGRI YFAGEYTAHP HGWIETSMKS AIREAINIHN A 491
    Length:491
    Mass (Da):55,977
    Last modified:September 21, 2011 - v3
    Checksum:i2FD1E740BD73313E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211H → S AA sequence (PubMed:9304806)Curated
    Sequence conflicti28 – 281C → S AA sequence (PubMed:8080286)Curated
    Sequence conflicti28 – 281C → S AA sequence (PubMed:9304806)Curated
    Sequence conflicti37 – 371W → H AA sequence (PubMed:8080286)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF080831 mRNA. Translation: ABN72538.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF080831 mRNA. Translation: ABN72538.1 .

    3D structure databases

    ProteinModelPortali P81383.
    SMRi P81383. Positions 25-491.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG005729.

    Enzyme and pathway databases

    SABIO-RK P81383.

    Family and domain databases

    InterProi IPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00757. AMINEOXDASEF.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of L-amino acid oxidase from king cobra venom."
      Jin Y., Lee W.-H., Zeng L., Zhang Y.
      Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-45; 121-129; 189-195; 272-278 AND 428-439, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
      Tissue: Venom and Venom gland.
    2. "Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom."
      Ponnudurai G., Chung M.C.M., Tan N.-H.
      Arch. Biochem. Biophys. 313:373-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-39, SUBUNIT, GLYCOSYLATION, COFACTOR.
      Tissue: Venom.
    3. "Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)."
      Ahn M.Y., Lee B.M., Kim Y.S.
      Int. J. Biochem. Cell Biol. 29:911-919(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, GLYCOSYLATION.
      Tissue: Venom.
    4. "Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom."
      Tan N.H., Saifuddin M.N.
      Biochem. Int. 19:937-944(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, TOXIC DOSE.
    5. "Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
      Tan N.H., Saifuddin M.N.
      Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
      Tissue: Venom.
    6. "The edema inducing activity of Ophiophagus hannah (king cobra) venom L-amino acid oxidase."
      Tan N.-H., Choy S.-K.
      Toxicon 32:539-539(1994)
      Cited for: ISOFORM.
    7. "Purification and characterization of L-amino acid oxidase from king cobra (Ophiophagus hannah) venom and its effects on human platelet aggregation."
      Li Z.Y., Yu T.F., Lian E.C.
      Toxicon 32:1349-1358(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Tissue: Venom.
    8. "Antibacterial action of a heat-stable form of L-amino acid oxidase isolated from king cobra (Ophiophagus hannah) venom."
      Lee M.L., Tan N.H., Fung S.Y., Sekaran S.D.
      Comp. Biochem. Physiol. 153:237-242(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ANTIBACTERIAL ACTIVITY.
      Tissue: Venom.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_OPHHA
    AccessioniPrimary (citable) accession number: P81383
    Secondary accession number(s): A8QL50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 57 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    The existence of two isoforms has been reported (PubMed:7886693), and could explain the differences in sequence and kinetic parameters.Curated

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3