5ts5
From Proteopedia
Crystal structure of L-amino acid oxidase from Bothrops atrox
Structural highlights
FunctionOXLA_BOTAT 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:18804547). Shows high catalytic activity against L-Met, L-Leu, L-Phe, L-Trp, L-Tyr, L-Ile (PubMed:18804547). Shows no or weak activity on L-Cys, L-Val, L-Gln, L-Thr, L-Ser, L-Lys, L-Arg, L-Asn, L-Glu, L-Gly, L-Pro, L-Asp and L-His (PubMed:18804547). Induces platelet aggregation in platelet-rich plasma, probably due to hydrogen peroxide production, since catalase inhibits aggregation effect (PubMed:18804547). Induces moderate mouse paw edema (PubMed:18804547). Induces apoptosis and shows cytotoxicity against several cancer cell lines, which is inhibited by catalase (PubMed:18804547, PubMed:21300133). Shows hemolytic activity and antibacterial activities against both Gram-positive and Gram-negative bacteria (PubMed:21300133). Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (PubMed:21300133). Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage (with 50 ug of enzyme) (PubMed:18804547).[1] [2] Publication Abstract from PubMedL-amino acid oxidases (LAAOs) are dimeric flavoproteins that catalyze the deamination of L-amino acid to alpha-keto acid, producing ammonia and hydrogen peroxide. In this study, we report the crystal structure and molecular dynamics simulations of LAAO from the venom of Bothrops atrox (BatroxLAAO). BatroxLAAO presents several biological and pharmacological properties with promising biomedical applications. BatroxLAAO structure contains the highly conserved structural pattern of LAAOs comprising a FAD-binding domain, substrate-binding domain and helical domain, and a dimeric arrangement that can be stabilized by zinc. Also, molecular dynamics results show an asymmetric behavior, and a direct communication between FAD- and substrate-binding domains of counterpart subunits. These findings shed light on the structural role of dimerization to catalytic mechanism of SV-LAAOs. Crystal structure and molecular dynamics studies of L-amino acid oxidase from Bothrops atrox.,Feliciano PR, Rustiguel JK, Soares RO, Sampaio SV, Cristina Nonato M Toxicon. 2017 Mar 15;128:50-59. doi: 10.1016/j.toxicon.2017.01.017. Epub 2017 Jan, 27. PMID:28137621[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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