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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

Miscellaneous

Does not induce dermal hemorrhage when subcutaneously injected into mice at the dose of 40 µg.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)DescriptionActionsGraphical viewLength
    Binding sitei89FADBy similarity1
    Binding sitei108SubstrateBy similarity1
    Binding sitei241SubstrateBy similarity1
    Binding sitei279FAD; via amide nitrogen and carbonyl oxygenBy similarity1
    Binding sitei390SubstrateBy similarity1
    Binding sitei475FADBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi61 – 62FADBy similarity2
    Nucleotide bindingi81 – 82FADBy similarity2
    Nucleotide bindingi105 – 108FADBy similarity4
    Nucleotide bindingi482 – 487FADBy similarity6

    GO - Molecular functioni

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

    GO - Biological processi

    Keywordsi

    Molecular functionHemostasis impairing toxin, Oxidoreductase, Platelet aggregation inhibiting toxin, Toxin
    Biological processCytolysis, Hemolysis
    LigandFAD, 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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi241H → A: Shows high reactivity toward L-Arg, but does not induce change toward L-Leu, L-Phe and L-Met. 1 Publication1
    Mutagenesisi241H → N: No change in activity. 1 Publication1
    Mutagenesisi241H → S: Shows middle reactivity toward L-Arg and L-Phe, but does not induce change toward L-Leu, and L-Met. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 181 PublicationAdd BLAST18
    ChainiPRO_500082564819 – 504L-amino-acid oxidaseAdd BLAST486

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi28 ↔ 191By similarity
    Glycosylationi190N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi349 ↔ 430By similarity
    Glycosylationi379N-linked (GlcNAc...) asparagineSequence analysis1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.By similarity

    GO - Molecular functioni

    • protein dimerization activity Source: UniProtKB

    Structurei

    3D structure databases

    SMRiG8XQX1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni482 – 483Substrate bindingBy similarity2

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.50.50.60. 1 hit.
    InterProiView protein in InterPro
    IPR002937. Amino_oxidase.
    IPR036188. FAD/NAD-bd_sf.
    PfamiView protein in Pfam
    PF01593. Amino_oxidase. 1 hit.
    SUPFAMiSSF51905. SSF51905. 2 hits.

    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

    G8XQX1: 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.

    Similar proteinsi

    Entry informationi

    Entry nameiOXLA_DABRR
    AccessioniPrimary (citable) accession number: G8XQX1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2012
    Last sequence update: February 22, 2012
    Last modified: October 25, 2017
    This is version 22 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families