ID   OXLA_NAJKA              Reviewed;          38 AA.
AC   P0C2D4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 12.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LAO;
DE            Short=K-LAO;
DE            EC=1.4.3.2;
DE   Flags: Fragment;
OS   Naja kaouthia (Monocled cobra) (Naja siamensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8649;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=11600144; DOI=10.1016/S0041-0101(01)00133-7;
RA   Sakurai Y., Takatsuka H., Yoshioka A., Matsui T., Suzuki M.,
RA   Titani K., Fujimura Y.;
RT   "Inhibition of human platelet aggregation by L-amino acid oxidase
RT   purified from Naja naja kaouthia venom.";
RL   Toxicon 39:1827-1833(2001).
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=1612186; DOI=10.1016/0020-711X(92)90105-A;
RA   Tan N.-H., Swaminathan S.;
RT   "Purification and properties of the L-amino acid oxidase from
RT   monocellate cobra (Naja naja kaouthia) venom.";
RL   Int. J. Biochem. 24:967-973(1992).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids. Is very active against L-
CC       Phe and L-Tyr, moderately active against L-Trp, L-Met, L-Leu, and
CC       L-Arg. Inhibits both agonist- and shear stress-induced platelet
CC       aggregation (SIPA) dose-dependently through the formation of
CC       hydrogen peroxide (H(2)O(2)). May induce apoptosis and hemorrhage.
CC       May have an antibacterial activity.
CC   -!- CATALYTIC ACTIVITY: An L-amino acid + H(2)O + O(2) = a 2-oxo acid
CC       + NH(3) + H(2)O(2).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5, unlike many other venom L-amino acid oxidase,
CC         is also stable in alkaline medium;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily.
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DR   HOVERGEN; P0C2D4; -.
DR   BRENDA; 1.4.3.2; 274888.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:EC.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Blood coagulation;
KW   Direct protein sequencing; FAD; Flavoprotein; Glycoprotein;
KW   Oxidoreductase; Secreted; Toxin.
FT   CHAIN         1    >38       L-amino-acid oxidase.
FT                                /FTId=PRO_0000273569.
FT   NON_TER      38     38
SQ   SEQUENCE   38 AA;  4514 MW;  D988B9FC32DDDE08 CRC64;
     DDRRSPLEEC FQQNDYEEFL EIAKNGLKKT XNPKHVXV
//