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P81382 (OXLA_CALRH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismCalloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Taxonomic identifier8717 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Calloselasma

Protein attributes

Sequence length516 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, 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.

Catalytic activity

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

Cofactor

FAD.

Subunit structure

Homodimer; non-covalently linked. Ref.2

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.63 mM for L-Leu Ref.4

KM=0.24 mM for L-Met

KM=0.05 mM for L-Phe

KM=0.08 mM for L-Trp

pH dependence:

Optimum pH is 9.0.

Temperature dependence:

Thermostable.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.1 Ref.2
Chain19 – 516498L-amino-acid oxidase
PRO_0000001707

Regions

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

Sites

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

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...) Ref.5
Glycosylation3791N-linked (GlcNAc...) Ref.5
Disulfide bond28 ↔ 191 Ref.5
Disulfide bond349 ↔ 430 Ref.5

Experimental info

Sequence conflict281C → E AA sequence Ref.2
Sequence conflict331D → N AA sequence Ref.2

Secondary structure

1 ................................................................................................ 516
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81382 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 5F9435718B3A3BDE

FASTA51658,221
        10         20         30         40         50         60 
MNVFFMFSLL FLAALGSCAD DRNPLAECFQ ENDYEEFLEI ARNGLKATSN PKHVVIVGAG 

        70         80         90        100        110        120 
MAGLSAAYVL AGAGHQVTVL EASERPGGRV RTYRNEEAGW YANLGPMRLP EKHRIVREYI 

       130        140        150        160        170        180 
RKFDLRLNEF SQENDNAWYF IKNIRKKVGE VKKDPGLLKY PVKPSEAGKS AGQLYEESLG 

       190        200        210        220        230        240 
KVVEELKRTN CSYILNKYDT YSTKEYLIKE GDLSPGAVDM IGDLLNEDSG YYVSFIESLK 

       250        260        270        280        290        300 
HDDIFAYEKR FDEIVDGMDK LPTAMYRDIQ DKVHFNAQVI KIQQNDQKVT VVYETLSKET 

       310        320        330        340        350        360 
PSVTADYVIV CTTSRAVRLI KFNPPLLPKK AHALRSVHYR SGTKIFLTCT TKFWEDDGIH 

       370        380        390        400        410        420 
GGKSTTDLPS RFIYYPNHNF TNGVGVIIAY GIGDDANFFQ ALDFKDCADI VFNDLSLIHQ 

       430        440        450        460        470        480 
LPKKDIQSFC YPSVIQKWSL DKYAMGGITT FTPYQFQHFS DPLTASQGRI YFAGEYTAQA 

       490        500        510 
HGWIDSTIKS GLRAARDVNL ASENPSGIHL SNDNEL

« Hide

References

[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: 11248687] [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: 8080286] [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: 17127077] [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: 16828829] [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: 10944103] [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: 17046020] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-516 IN COMPLEX WITH FAD AND SUBSTRATE L-PHE.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ271725 mRNA. Translation: CAB71136.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP81382.
SMRP81382. Positions 22-504.
ModBaseSearch...

PTM databases

GlycoSuiteDBP81382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

Family and domain databases

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

Entry information

Entry nameOXLA_CALRH
AccessionPrimary (citable) accession number: P81382
Secondary accession number(s): Q9I849
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2002
Last modified: January 25, 2012
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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