Ornithine monooxygenase and RNase J family beta-CASP ribonuclease. Can they be bacteriocins?

Authors

DOI:

https://doi.org/10.17268/sci.agropecu.2020.02.16

Keywords:

Ornithine monooxygenase, ribonucleases, bacteriocins, enzymes, antimicrobial properties.

References

Arosio, P.; Poli, M.; Gozzelino, R. 2020. Iron as therapeutic targets in human diseases Iron as Therapeutic Target in Human Diseases Volumen 2. Editorial MDPI AG. Barcelona, España. 440 pp.

BRENDA – The Comprehensive Enzyme Information System. 2020. Information on EC 1.14.13.195 - L-ornithine N5-monooxygenase (NADPH). Available in: https://www.brenda-enzymes.org/enzyme.php?ecno=1.14.13.195

Clouet-d’Orval, B.; Phung, D.K.; Langendijk-Genevaux, P. S.; et al. 2015. Universal RNA-degrading enzymes in Archaea: Prevalence, activities and functions of β-CASP ribonucleases. Biochimie 118: 278-285.

InterPro. 2020. Classification of protein families. InterPro 78.1. Available in:

https://www.ebi.ac.uk/interpro/entry/InterPro/IPR004613/

Kramer, J.; Özkaya, Ö.; Kümmerli, R. 2019. Bacterial siderophores in community and host interactions. Nature Reviews Microbiology 18: 152-163.

Kumariya, R.; Garsa, A.K.; Rajput, Y.S.; et al. 2019. Bacteriocins: Classification, synthesis, mechanism of action and resistance development in food spoilage causing bacteria. Microbial pathogenesis 128: 171-177.

Sánchez, H.; Ochoa, G.; Rojas, C.; et al. 2017. Aislamiento de péptidos inhibidores de bacterias a partir de bacterias ácido lácticas del tracto digestivo del lechón e identificación mediante prueba proteómica. Scientia Agropecuaria 8(4): 437-443.

UniProt Consortium. 2020. UniProtKB – Q51548 (PVDA_PSEAE). Available in: https://www.uniprot.org/uniprot/Q51548

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Published

2020-06-08

How to Cite

Alfaro, R. (2020). Ornithine monooxygenase and RNase J family beta-CASP ribonuclease. Can they be bacteriocins?. Scientia Agropecuaria, 11(2), 279. https://doi.org/10.17268/sci.agropecu.2020.02.16

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