| IED ID | IndEnz0007000380 |
| Enzyme Type ID | catalase000380 |
| Protein Name |
L-amino-acid oxidase DrLAO LAAO EC 1.4.3.2 |
| Gene Name | |
| Organism | Daboia russelii (Russel's viper) (Vipera russelii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Viperinae (vipers) Daboia Daboia russelii (Russel's viper) (Vipera russelii) |
| Enzyme Sequence | MNVFFMFSLLFLATLGSCADDKNPLEECFREDDYEEFLEIAKNGLKKTSNPKHIVIVGAGMSGLSAAYVLAGAGHKVTVLEASERPGGRVRTHRNVKEGWYANLGPMRVPEKHRIIREYIRKFGLKLNEFVQETENGWYFIKNIRKRVGEVKKDPGLLKYPVKPSEAGKSAGQLYQESLGKAVEELKRTNCSYILNKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDQLPTSMYRAIEESVHFKARVIKIQQNAEKVTVTYQTTQKNLLLETADYVIVCTTSRAARRITFKPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIQGGKSTTDLPSRFIYYPNHNFTTGVGVIIAYGIGDDANFFQALNLNECADIVFNDLSSIHQLPKKDLQTFCYPSIIQKWSLDKYAMGAITTFTPYQFQHFSEALTAPVGRIFFAGEYTANAHGWIDSTIKSGLTAARDVNRASEL |
| Enzyme Length | 504 |
| Uniprot Accession Number | G8XQX1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 89; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 108; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 241; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 279; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 390; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 475; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:21802487}; CATALYTIC ACTIVITY: Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:21802487}; CATALYTIC ACTIVITY: Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:21802487}; CATALYTIC ACTIVITY: Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:21802487}; CATALYTIC ACTIVITY: Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; Evidence={ECO:0000269|PubMed:21802487}; CATALYTIC ACTIVITY: Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:21802487}; |
| DNA Binding | |
| EC Number | 1.4.3.2 |
| Enzyme Function | 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 (PubMed:21802487). Is highly active on L-Tyr followed by L-Phe, L-Met, L-Leu, L-Trp, and weakly active on L-Ile, L-Arg, L-Val, L-Lys, and L-Ala (PubMed:21802487). Inhibits ADP- and collagen-induced platelet aggregation (PubMed:21802487). This inhibition is inhibited by catalase, indicating the importance of generated H(2)O(2) for the inhibitory effect (PubMed:21802487). 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 (By similarity). In vivo, this enzyme induces a rapid, substantial and reversible increase in the paw volume of mice (edema) (PubMed:21802487). In addition, myofibrosis, and inflammatory cell infiltration on the paw tissue are also observed (PubMed:21802487). {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:21802487}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 61..62; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 81..82; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 105..108; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 482..487; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382 |
| Features | Binding site (6); Chain (1); Disulfide bond (2); Glycosylation (2); Mutagenesis (3); Nucleotide binding (4); Region (1); Signal peptide (1) |
| Keywords | Cytolysis;Direct protein sequencing;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Hemolysis;Hemostasis impairing toxin;Oxidoreductase;Platelet aggregation inhibiting toxin;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21802487}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:21802487 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,888 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.081 mM for L-Tyr (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0.142 mM for L-Phe (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0.373 mM for L-Met (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0.318 mM for L-Trp (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=0.490 mM for L-Leu (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=1.40 mM for L-Ile (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=12.20 mM for L-Arg (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=13.92 mM for L-Val (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=64.00 mM for L-Lys (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; KM=116.48 mM for L-Ala (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:21802487}; |
| Metal Binding | |
| Rhea ID | RHEA:13781; RHEA:60996; RHEA:61240; RHEA:61244; RHEA:61236; RHEA:61248 |
| Cross Reference Brenda |