Dual RNase and ?-lactamase Activity of a Single Enzyme Encoded in Archaea.

ABSTRACT: ?-lactam antibiotics have a well-known activity which disturbs the bacterial cell wall biosynthesis and may be cleaved by ?-lactamases. However, these drugs are not active on archaea microorganisms, which are naturally resistant because of the lack of ?-lactam target in their cell wall. Here, we describe that annotation of genes as ?-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, ?-lactamase, or glyoxalase, which may specialized over time. We expressed class B ?-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 ?-lactamase activity was inhibited by ?-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 ?-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 ?-lactamase enzymes and the specification of multipotent enzymes in different ways in Archaea and bacteria over time.

SUBMITTER: Diene SM 

PROVIDER: S-EPMC7697635 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature