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G8XQX1 (OXLA_DABRR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=DrLAO
Short name=LAAO
EC=1.4.3.2
OrganismDaboia russelii (Russel's viper) (Vipera russelii)
Taxonomic identifier31159 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeDaboia

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Miscellaneous

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

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.081 mM for L-Tyr (at pH 7.5 and 25 degrees Celsius) Ref.1

KM=0.142 mM for L-Phe (at pH 7.5 and 25 degrees Celsius)

KM=0.373 mM for L-Met (at pH 7.5 and 25 degrees Celsius)

KM=0.318 mM for L-Trp (at pH 7.5 and 25 degrees Celsius)

KM=0.490 mM for L-Leu (at pH 7.5 and 25 degrees Celsius)

KM=1.40 mM for L-Ile (at pH 7.5 and 25 degrees Celsius)

KM=12.20 mM for L-Arg (at pH 7.5 and 25 degrees Celsius)

KM=13.92 mM for L-Val (at pH 7.5 and 25 degrees Celsius)

KM=64.00 mM for L-Lys (at pH 7.5 and 25 degrees Celsius)

KM=116.48 mM for L-Ala (at pH 7.5 and 25 degrees Celsius)

Mass spectrometry

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.1
Chain19 – 504486L-amino-acid oxidase
PRO_5000825648

Regions

Nucleotide binding61 – 622FAD By similarity
Nucleotide binding81 – 822FAD By similarity
Nucleotide binding105 – 1084FAD By similarity
Nucleotide binding482 – 4876FAD By similarity
Nucleotide binding482 – 4832Substrate By similarity

Sites

Binding site891FAD By similarity
Binding site1081Substrate By similarity
Binding site2411Substrate By similarity
Binding site2791FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3901Substrate By similarity
Binding site4751FAD By similarity

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation3791N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 191 By similarity
Disulfide bond349 ↔ 430 By similarity

Experimental info

Mutagenesis2411H → A: Shows high reactivity toward L-Arg, but does not induce change toward L-Leu, L-Phe and L-Met. Ref.1
Mutagenesis2411H → N: No change in activity. Ref.1
Mutagenesis2411H → S: Shows middle reactivity toward L-Arg and L-Phe, but does not induce change toward L-Leu, and L-Met. Ref.1

Sequences

Sequence LengthMass (Da)Tools
G8XQX1 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: 938FBF23BBAA7681

FASTA50456,888
        10         20         30         40         50         60 
MNVFFMFSLL FLATLGSCAD DKNPLEECFR EDDYEEFLEI AKNGLKKTSN PKHIVIVGAG 

        70         80         90        100        110        120 
MSGLSAAYVL AGAGHKVTVL EASERPGGRV RTHRNVKEGW YANLGPMRVP EKHRIIREYI 

       130        140        150        160        170        180 
RKFGLKLNEF VQETENGWYF IKNIRKRVGE VKKDPGLLKY PVKPSEAGKS AGQLYQESLG 

       190        200        210        220        230        240 
KAVEELKRTN CSYILNKYDT YSTKEYLIKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK 

       250        260        270        280        290        300 
HDDIFAYEKR FDEIVGGMDQ LPTSMYRAIE ESVHFKARVI KIQQNAEKVT VTYQTTQKNL 

       310        320        330        340        350        360 
LLETADYVIV CTTSRAARRI TFKPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIQ 

       370        380        390        400        410        420 
GGKSTTDLPS RFIYYPNHNF TTGVGVIIAY GIGDDANFFQ ALNLNECADI VFNDLSSIHQ 

       430        440        450        460        470        480 
LPKKDLQTFC YPSIIQKWSL DKYAMGAITT FTPYQFQHFS EALTAPVGRI FFAGEYTANA 

       490        500 
HGWIDSTIKS GLTAARDVNR ASEL 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU663622 mRNA. Translation: ACF70483.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002937. Amino_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOXLA_DABRR
AccessionPrimary (citable) accession number: G8XQX1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: February 22, 2012
Last modified: April 16, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families