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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
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. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions (By similarity).By similarity

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=0.63 mM for L-Leu1 Publication
  2. KM=0.24 mM for L-Met1 Publication
  3. KM=0.05 mM for L-Phe1 Publication
  4. KM=0.08 mM for L-Trp1 Publication

    pH dependencei

    Optimum pH is 9.0.1 Publication

    Temperature dependencei

    Thermostable.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891FAD2 Publications
    Binding sitei108 – 1081Substrate
    Binding sitei241 – 2411Substrate
    Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygen2 Publications
    Binding sitei390 – 3901Substrate
    Binding sitei475 – 4751FAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi61 – 622FAD2 Publications
    Nucleotide bindingi81 – 822FAD2 Publications
    Nucleotide bindingi105 – 1084FAD2 Publications
    Nucleotide bindingi482 – 4876FAD2 Publications
    Nucleotide bindingi482 – 4832Substrate

    GO - Molecular functioni

    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

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    SABIO-RKP81382.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase (EC:1.4.3.2)
    Short name:
    LAAO
    Short name:
    LAO
    OrganismiCalloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
    Taxonomic identifieri8717 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCalloselasma

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18182 PublicationsAdd
    BLAST
    Chaini19 – 516498L-amino-acid oxidasePRO_0000001707Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 1911 Publication
    Glycosylationi190 – 1901N-linked (GlcNAc...)1 Publication
    Disulfide bondi349 ↔ 4301 Publication
    Glycosylationi379 – 3791N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    PTM databases

    UniCarbKBiP81382.

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.3 Publications

    Structurei

    Secondary structure

    1
    516
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 294Combined sources
    Helixi34 – 4310Combined sources
    Beta strandi53 – 575Combined sources
    Helixi61 – 7313Combined sources
    Beta strandi76 – 805Combined sources
    Beta strandi82 – 876Combined sources
    Beta strandi92 – 954Combined sources
    Turni96 – 994Combined sources
    Beta strandi100 – 1056Combined sources
    Helixi114 – 1229Combined sources
    Beta strandi127 – 1304Combined sources
    Beta strandi137 – 1415Combined sources
    Beta strandi144 – 1474Combined sources
    Helixi148 – 1536Combined sources
    Helixi155 – 1584Combined sources
    Helixi164 – 1663Combined sources
    Helixi171 – 1788Combined sources
    Helixi180 – 1889Combined sources
    Helixi191 – 1988Combined sources
    Beta strandi200 – 2023Combined sources
    Helixi203 – 2097Combined sources
    Helixi215 – 22410Combined sources
    Helixi228 – 2303Combined sources
    Helixi235 – 24511Combined sources
    Beta strandi251 – 2544Combined sources
    Helixi260 – 2689Combined sources
    Helixi269 – 2724Combined sources
    Beta strandi273 – 2764Combined sources
    Beta strandi278 – 2847Combined sources
    Beta strandi289 – 2946Combined sources
    Beta strandi296 – 2983Combined sources
    Beta strandi302 – 3109Combined sources
    Helixi314 – 3174Combined sources
    Beta strandi320 – 3245Combined sources
    Helixi328 – 3369Combined sources
    Beta strandi342 – 35110Combined sources
    Helixi353 – 3575Combined sources
    Beta strandi361 – 3688Combined sources
    Beta strandi372 – 3743Combined sources
    Beta strandi385 – 3928Combined sources
    Helixi393 – 3975Combined sources
    Turni398 – 4014Combined sources
    Helixi404 – 41916Combined sources
    Helixi423 – 4297Combined sources
    Beta strandi430 – 4378Combined sources
    Helixi438 – 4403Combined sources
    Turni442 – 4443Combined sources
    Beta strandi446 – 4494Combined sources
    Helixi455 – 46410Combined sources
    Beta strandi470 – 4723Combined sources
    Helixi475 – 4773Combined sources
    Beta strandi478 – 4825Combined sources
    Helixi484 – 50320Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F8RX-ray2.00A/B/C/D19-516[»]
    1F8SX-ray2.00A/B/C/D/E/F/G/H19-516[»]
    2IIDX-ray1.80A/B/C/D19-516[»]
    ProteinModelPortaliP81382.
    SMRiP81382. Positions 22-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81382.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG005729.

    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.

    P81382-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNVFFMFSLL FLAALGSCAD DRNPLAECFQ ENDYEEFLEI ARNGLKATSN
    60 70 80 90 100
    PKHVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERPGGRV RTYRNEEAGW
    110 120 130 140 150
    YANLGPMRLP EKHRIVREYI RKFDLRLNEF SQENDNAWYF IKNIRKKVGE
    160 170 180 190 200
    VKKDPGLLKY PVKPSEAGKS AGQLYEESLG KVVEELKRTN CSYILNKYDT
    210 220 230 240 250
    YSTKEYLIKE GDLSPGAVDM IGDLLNEDSG YYVSFIESLK HDDIFAYEKR
    260 270 280 290 300
    FDEIVDGMDK LPTAMYRDIQ DKVHFNAQVI KIQQNDQKVT VVYETLSKET
    310 320 330 340 350
    PSVTADYVIV CTTSRAVRLI KFNPPLLPKK AHALRSVHYR SGTKIFLTCT
    360 370 380 390 400
    TKFWEDDGIH GGKSTTDLPS RFIYYPNHNF TNGVGVIIAY GIGDDANFFQ
    410 420 430 440 450
    ALDFKDCADI VFNDLSLIHQ LPKKDIQSFC YPSVIQKWSL DKYAMGGITT
    460 470 480 490 500
    FTPYQFQHFS DPLTASQGRI YFAGEYTAQA HGWIDSTIKS GLRAARDVNL
    510
    ASENPSGIHL SNDNEL
    Length:516
    Mass (Da):58,221
    Last modified:January 23, 2002 - v2
    Checksum:i5F9435718B3A3BDE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281C → E AA sequence (PubMed:8080286).Curated
    Sequence conflicti33 – 331D → N AA sequence (PubMed:8080286).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ271725 mRNA. Translation: CAB71136.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ271725 mRNA. Translation: CAB71136.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F8RX-ray2.00A/B/C/D19-516[»]
    1F8SX-ray2.00A/B/C/D/E/F/G/H19-516[»]
    2IIDX-ray1.80A/B/C/D19-516[»]
    ProteinModelPortaliP81382.
    SMRiP81382. Positions 22-504.
    ModBaseiSearch...
    MobiDBiSearch...

    PTM databases

    UniCarbKBiP81382.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    HOVERGENiHBG005729.

    Enzyme and pathway databases

    SABIO-RKP81382.

    Miscellaneous databases

    EvolutionaryTraceiP81382.

    Family and domain databases

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

    Publicationsi

    1. "L-amino-acid oxidase from Malayan pit viper Calloselasma rhodostoma: comparative sequence analysis and characterization of active and inactive forms of the enzyme."
      Macheroux P., Seth O., Bollschweiler C., Schwarz M., Kurfuerst M., Au L.-C., Ghisla S.
      Eur. J. Biochem. 268:1679-1686(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-33.
      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 19-38, SUBUNIT.
      Tissue: Venom.
    3. "Molecular cloning, expression and purification of L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma."
      Kommoju P.R., Macheroux P., Ghisla S.
      Protein Expr. Purif. 52:89-95(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: EXPRESSION OF ACTIVE RECOMBINANT LAAO.
    4. "L-amino acid oxidase from Vipera lebetina venom: isolation, characterization, effects on platelets and bacteria."
      Tonismagi K., Samel M., Trummal K., Ronnholm G., Siigur J., Kalkkinen N., Siigur E.
      Toxicon 48:227-237(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    5. "The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site."
      Pawelek P.D., Cheah J., Coulombe R., Macheroux P., Ghisla S., Vrielink A.
      EMBO J. 19:4204-4215(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-516 IN COMPLEX WITH FAD, DISULFIDE BONDS, GLYCOSYLATION AT ASN-190 AND ASN-379.
      Tissue: Venom.
    6. "Crystal structure of LAAO from Calloselasma rhodostoma with an L-phenylalanine substrate: insights into structure and mechanism."
      Moustafa I.M., Foster S., Lyubimov A.Y., Vrielink A.
      J. Mol. Biol. 364:991-1002(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-516 IN COMPLEX WITH FAD AND SUBSTRATE L-PHE.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_CALRH
    AccessioniPrimary (citable) accession number: P81382
    Secondary accession number(s): Q9I849
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 23, 2002
    Last modified: January 7, 2015
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.