Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-amino-acid oxidase

Gene
N/A
Organism
Daboia russelii (Russel's viper) (Vipera russelii)
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 (L-Tyr followed by L-Phe, L-Met, L-Leu, L-Trp), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Inhibits ADP- and collagen-induced platelet aggregation. This inhibition is inhibited by catalase, indicating the importance of generated H2O2 for the inhibitory effect. This effect on platelets among snake L-amino-acid oxidases is however controversial, since some of them induce aggregation, whereas the other inhibit agonist-induced aggregation. In vivo, this enzyme induces a rapid, substantial and reversible increase in the paw volume of mice (edema). In addition, myofibrosis, and inflammatory cell infiltration on the paw tissue are also observed.1 Publication

Catalytic activityi

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

Cofactori

FADBy similarity

Kineticsi

  1. KM=0.081 mM for L-Tyr (at pH 7.5 and 25 degrees Celsius)1 Publication
  2. KM=0.142 mM for L-Phe (at pH 7.5 and 25 degrees Celsius)1 Publication
  3. KM=0.373 mM for L-Met (at pH 7.5 and 25 degrees Celsius)1 Publication
  4. KM=0.318 mM for L-Trp (at pH 7.5 and 25 degrees Celsius)1 Publication
  5. KM=0.490 mM for L-Leu (at pH 7.5 and 25 degrees Celsius)1 Publication
  6. KM=1.40 mM for L-Ile (at pH 7.5 and 25 degrees Celsius)1 Publication
  7. KM=12.20 mM for L-Arg (at pH 7.5 and 25 degrees Celsius)1 Publication
  8. KM=13.92 mM for L-Val (at pH 7.5 and 25 degrees Celsius)1 Publication
  9. KM=64.00 mM for L-Lys (at pH 7.5 and 25 degrees Celsius)1 Publication
  10. KM=116.48 mM for L-Ala (at pH 7.5 and 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891FADBy similarity
    Binding sitei108 – 1081SubstrateBy similarity
    Binding sitei241 – 2411SubstrateBy similarity
    Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei390 – 3901SubstrateBy similarity
    Binding sitei475 – 4751FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi61 – 622FADBy similarity
    Nucleotide bindingi81 – 822FADBy similarity
    Nucleotide bindingi105 – 1084FADBy similarity
    Nucleotide bindingi482 – 4876FADBy similarity
    Nucleotide bindingi482 – 4832SubstrateBy 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

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

    Keywords - Biological processi

    Cytolysis, Hemolysis

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase (EC:1.4.3.2)
    Short name:
    DrLAO
    Short name:
    LAAO
    OrganismiDaboia russelii (Russel's viper) (Vipera russelii)
    Taxonomic identifieri31159 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeDaboia

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: UniProtKB
    • extracellular space of host Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi241 – 2411H → A: Shows high reactivity toward L-Arg, but does not induce change toward L-Leu, L-Phe and L-Met. 1 Publication
    Mutagenesisi241 – 2411H → N: No change in activity. 1 Publication
    Mutagenesisi241 – 2411H → S: Shows middle reactivity toward L-Arg and L-Phe, but does not induce change toward L-Leu, and L-Met. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 504486L-amino-acid oxidasePRO_5000825648Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 191By similarity
    Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi349 ↔ 430By similarity
    Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.By similarity

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    G8XQX1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNVFFMFSLL FLATLGSCAD DKNPLEECFR EDDYEEFLEI AKNGLKKTSN
    60 70 80 90 100
    PKHIVIVGAG MSGLSAAYVL AGAGHKVTVL EASERPGGRV RTHRNVKEGW
    110 120 130 140 150
    YANLGPMRVP EKHRIIREYI RKFGLKLNEF VQETENGWYF IKNIRKRVGE
    160 170 180 190 200
    VKKDPGLLKY PVKPSEAGKS AGQLYQESLG KAVEELKRTN CSYILNKYDT
    210 220 230 240 250
    YSTKEYLIKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK HDDIFAYEKR
    260 270 280 290 300
    FDEIVGGMDQ LPTSMYRAIE ESVHFKARVI KIQQNAEKVT VTYQTTQKNL
    310 320 330 340 350
    LLETADYVIV CTTSRAARRI TFKPPLPPKK AHALRSVHYR SGTKIFLTCT
    360 370 380 390 400
    KKFWEDDGIQ GGKSTTDLPS RFIYYPNHNF TTGVGVIIAY GIGDDANFFQ
    410 420 430 440 450
    ALNLNECADI VFNDLSSIHQ LPKKDLQTFC YPSIIQKWSL DKYAMGAITT
    460 470 480 490 500
    FTPYQFQHFS EALTAPVGRI FFAGEYTANA HGWIDSTIKS GLTAARDVNR

    ASEL
    Length:504
    Mass (Da):56,888
    Last modified:February 22, 2012 - v1
    Checksum:i938FBF23BBAA7681
    GO

    Mass spectrometryi

    Molecular mass is 62025 Da from positions 19 - 504. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EU663622 mRNA. Translation: ACF70483.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EU663622 mRNA. Translation: ACF70483.1.

    3D structure databases

    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Cloning, characterization and mutagenesis of Russell's viper venom L-amino acid oxidase: insights into its catalytic mechanism."
      Chen H.-S., Wang Y.-M., Huang W.-T., Huang K.-F., Tsai I.-H.
      Biochimie 94:335-344(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-38, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-241, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, 3D-STRUCTURE MODELING IN COMPLEX WITH SUBSTRATE.
      Strain: Eastern India.
      Tissue: Venom and Venom gland.

    Entry informationi

    Entry nameiOXLA_DABRR
    AccessioniPrimary (citable) accession number: G8XQX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2012
    Last sequence update: February 22, 2012
    Last modified: November 26, 2014
    This is version 16 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Does not induce dermal hemorrhage when subcutaneously injected into mice at the dose of 40 µg.1 Publication

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.