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MipLAAO, a new L-amino acid oxidase from the redtail coral snake Micrurus mipartitus

L-amino acid oxidases (LAAOs) are ubiquitous enzymes in nature. Bioactivities described for these enzymes include apoptosis induction, edema formation, induction or inhibition of platelet aggregation, as well as antiviral, antiparasite, and antibacterial actions. With over 80 species, Micrurus snake...

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Autores principales: Rey-Suárez, Paola, Acosta, Cristian, Torres, Uday, Saldarriaga-Córdoba, Mónica, Lomonte, Bruno, Núñez, Vitelbina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5995095/
https://www.ncbi.nlm.nih.gov/pubmed/29900074
http://dx.doi.org/10.7717/peerj.4924
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author Rey-Suárez, Paola
Acosta, Cristian
Torres, Uday
Saldarriaga-Córdoba, Mónica
Lomonte, Bruno
Núñez, Vitelbina
author_facet Rey-Suárez, Paola
Acosta, Cristian
Torres, Uday
Saldarriaga-Córdoba, Mónica
Lomonte, Bruno
Núñez, Vitelbina
author_sort Rey-Suárez, Paola
collection PubMed
description L-amino acid oxidases (LAAOs) are ubiquitous enzymes in nature. Bioactivities described for these enzymes include apoptosis induction, edema formation, induction or inhibition of platelet aggregation, as well as antiviral, antiparasite, and antibacterial actions. With over 80 species, Micrurus snakes are the representatives of the Elapidae family in the New World. Although LAAOs in Micrurus venoms have been predicted by venom gland transcriptomic studies and detected in proteomic studies, no enzymes of this kind have been previously purified from their venoms. Earlier proteomic studies revealed that the venom of M. mipartitus from Colombia contains ∼4% of LAAO. This enzyme, here named MipLAAO, was isolated and biochemically and functionally characterized. The enzyme is found in monomeric form, with an isotope-averaged molecular mass of 59,100.6 Da, as determined by MALDI-TOF. Its oxidase activity shows substrate preference for hydrophobic amino acids, being optimal at pH 8.0. By nucleotide sequencing of venom gland cDNA of mRNA transcripts obtained from a single snake, six isoforms of MipLAAO with minor variations among them were retrieved. The deduced sequences present a mature chain of 483 amino acids, with a predicted pI of 8.9, and theoretical masses between 55,010.9 and 55,121.0 Da. The difference with experimentally observed mass is likely due to glycosylation, in agreement with the finding of three putative N-glycosylation sites in its amino acid sequence. A phylogenetic analysis of MmipLAAO placed this new enzyme within the clade of homologous proteins from elapid snakes, characterized by the conserved Serine at position 223, in contrast to LAAOs from viperids. MmipLAAO showed a potent bactericidal effect on S. aureus (MIC: 2 µg/mL), but not on E. coli. The former activity could be of interest to future studies assessing its potential as antimicrobial agent.
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spelling pubmed-59950952018-06-13 MipLAAO, a new L-amino acid oxidase from the redtail coral snake Micrurus mipartitus Rey-Suárez, Paola Acosta, Cristian Torres, Uday Saldarriaga-Córdoba, Mónica Lomonte, Bruno Núñez, Vitelbina PeerJ Biochemistry L-amino acid oxidases (LAAOs) are ubiquitous enzymes in nature. Bioactivities described for these enzymes include apoptosis induction, edema formation, induction or inhibition of platelet aggregation, as well as antiviral, antiparasite, and antibacterial actions. With over 80 species, Micrurus snakes are the representatives of the Elapidae family in the New World. Although LAAOs in Micrurus venoms have been predicted by venom gland transcriptomic studies and detected in proteomic studies, no enzymes of this kind have been previously purified from their venoms. Earlier proteomic studies revealed that the venom of M. mipartitus from Colombia contains ∼4% of LAAO. This enzyme, here named MipLAAO, was isolated and biochemically and functionally characterized. The enzyme is found in monomeric form, with an isotope-averaged molecular mass of 59,100.6 Da, as determined by MALDI-TOF. Its oxidase activity shows substrate preference for hydrophobic amino acids, being optimal at pH 8.0. By nucleotide sequencing of venom gland cDNA of mRNA transcripts obtained from a single snake, six isoforms of MipLAAO with minor variations among them were retrieved. The deduced sequences present a mature chain of 483 amino acids, with a predicted pI of 8.9, and theoretical masses between 55,010.9 and 55,121.0 Da. The difference with experimentally observed mass is likely due to glycosylation, in agreement with the finding of three putative N-glycosylation sites in its amino acid sequence. A phylogenetic analysis of MmipLAAO placed this new enzyme within the clade of homologous proteins from elapid snakes, characterized by the conserved Serine at position 223, in contrast to LAAOs from viperids. MmipLAAO showed a potent bactericidal effect on S. aureus (MIC: 2 µg/mL), but not on E. coli. The former activity could be of interest to future studies assessing its potential as antimicrobial agent. PeerJ Inc. 2018-06-08 /pmc/articles/PMC5995095/ /pubmed/29900074 http://dx.doi.org/10.7717/peerj.4924 Text en ©2018 Rey-Suárez et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited.
spellingShingle Biochemistry
Rey-Suárez, Paola
Acosta, Cristian
Torres, Uday
Saldarriaga-Córdoba, Mónica
Lomonte, Bruno
Núñez, Vitelbina
MipLAAO, a new L-amino acid oxidase from the redtail coral snake Micrurus mipartitus
title MipLAAO, a new L-amino acid oxidase from the redtail coral snake Micrurus mipartitus
title_full MipLAAO, a new L-amino acid oxidase from the redtail coral snake Micrurus mipartitus
title_fullStr MipLAAO, a new L-amino acid oxidase from the redtail coral snake Micrurus mipartitus
title_full_unstemmed MipLAAO, a new L-amino acid oxidase from the redtail coral snake Micrurus mipartitus
title_short MipLAAO, a new L-amino acid oxidase from the redtail coral snake Micrurus mipartitus
title_sort miplaao, a new l-amino acid oxidase from the redtail coral snake micrurus mipartitus
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5995095/
https://www.ncbi.nlm.nih.gov/pubmed/29900074
http://dx.doi.org/10.7717/peerj.4924
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