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Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea.
- Source :
- Life (2075-1729); Nov2020, Vol. 10 Issue 11, p280, 1p
- Publication Year :
- 2020
-
Abstract
- β-lactam antibiotics have a well-known activity which disturbs the bacterial cell wall biosynthesis and may be cleaved by β-lactamases. However, these drugs are not active on archaea microorganisms, which are naturally resistant because of the lack of β-lactam target in their cell wall. Here, we describe that annotation of genes as β-lactamases in Archaea on the basis of homologous genes is a remnant of identification of the original activities of this group of enzymes, which in fact have multiple functions, including nuclease, ribonuclease, β-lactamase, or glyoxalase, which may specialized over time. We expressed class B β-lactamase enzyme from Methanosarcina barkeri that digest penicillin G. Moreover, while weak glyoxalase activity was detected, a significant ribonuclease activity on bacterial and synthetic RNAs was demonstrated. The β-lactamase activity was inhibited by β-lactamase inhibitor (sulbactam), but its RNAse activity was not. This gene appears to have been transferred to the Flavobacteriaceae group especially the Elizabethkingia genus, in which the expressed gene shows a more specialized activity on thienamycin, but no glyoxalase activity. The expressed class C-like β-lactamase gene, from Methanosarcina sp., also shows hydrolysis activity on nitrocefin and is more closely related to DD-peptidase enzymes. Our findings highlight the need to redefine the nomenclature of β-lactamase enzymes and the specification of multipotent enzymes in different ways in Archaea and bacteria over time. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 20751729
- Volume :
- 10
- Issue :
- 11
- Database :
- Complementary Index
- Journal :
- Life (2075-1729)
- Publication Type :
- Academic Journal
- Accession number :
- 147275250
- Full Text :
- https://doi.org/10.3390/life10110280