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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Ophiophagus hannah (King cobra) (Naja hannah)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

FAD2 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

    • flavin adenine dinucleotide binding Source: UniProtKB
    • L-amino-acid oxidase activity Source: UniProtKB
    • protein dimerization activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    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

    BRENDAi1.4.3.2. 4419.
    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

    • extracellular region Source: UniProtKB
    Complete GO annotation...

    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

    Proteomic databases

    TopDownProteomicsiP81383.

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.4 Publications

    GO - Molecular functioni

    • protein dimerization activity Source: UniProtKB

    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

    Gene3Di3.50.50.60. 3 hits.
    InterProiIPR002937. Amino_oxidase.
    IPR023753. FAD/NAD-binding_dom.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.
    SUPFAMiSSF51905. SSF51905. 2 hits.

    Sequencei

    Sequence statusi: Complete.

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

    P81383-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNDFLLLLLV LFLGVPRSEN HVINLEECFQ EPEYENWLAT ASHGLTKTLN
    60 70 80 90 100
    PKKIVIVGAG ISGLTAAKLF REAGHEVVIL EASDRVGGRI KTHREDGWYV
    110 120 130 140 150
    DVGPMRVPQT HRIVREYIKK FNISLNPFRQ TDENAWYLIK HVRQKMSANN
    160 170 180 190 200
    PENFGYQLNP NERGKSASQL FDETLDKVTD DCTLQKEKYD SFSTKEYLIK
    210 220 230 240 250
    EGKLSTGAVE MIGDFLNEEA GFHNSFLISV MDHFLFLNNS FDEITGGFDQ
    260 270 280 290 300
    LPERFFKDMD SIVHLNSTVE KIVHINNKVT VFYEGLSTNM RLVADYVLIT
    310 320 330 340 350
    ATARATRLIK FVPPLSIPKT RALRSLIYAS ATKIILVCTD KFWEKDGIHG
    360 370 380 390 400
    GRSITDLPSR VIYYPNHDFT NGIGVLLASY TWYSDSEFYT TLSDEKCVDV
    410 420 430 440 450
    VMDDLVEIHN VSKDYLKSVC GKHVVQKWAL DQYSMGAFST YTPYQITHYS
    460 470 480 490
    QMLAQNEGRI YFAGEYTAHP HGWIETSMKS AIREAINIHN A
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF080831 mRNA. Translation: ABN72538.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF080831 mRNA. Translation: ABN72538.1.

    3D structure databases

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

    Proteomic databases

    TopDownProteomicsiP81383.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    HOVERGENiHBG005729.

    Enzyme and pathway databases

    BRENDAi1.4.3.2. 4419.
    SABIO-RKP81383.

    Family and domain databases

    Gene3Di3.50.50.60. 3 hits.
    InterProiIPR002937. Amino_oxidase.
    IPR023753. FAD/NAD-binding_dom.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.
    SUPFAMiSSF51905. SSF51905. 2 hits.
    ProtoNetiSearch...

    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: September 7, 2016
    This is version 65 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 (Ref. 6), 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.