β-Lactam antibiotic-degrading enzymes from non-pathogenic marine organisms: a potential threat to human health

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
Manfredi MiraulaNataša Mitić

Abstract

Metallo-β-lactamases (MBLs) are a family of Zn(II)-dependent enzymes that inactivate most of the commonly used β-lactam antibiotics. They have emerged as a major threat to global healthcare. Recently, we identified two novel MBL-like proteins, Maynooth IMipenemase-1 (MIM-1) and Maynooth IMipenemase-2 (MIM-2), in the marine organisms Novosphingobium pentaromativorans and Simiduia agarivorans, respectively. Here, we demonstrate that MIM-1 and MIM-2 have catalytic activities comparable to those of known MBLs, but from the pH dependence of their catalytic parameters it is evident that both enzymes differ with respect to their mechanisms, with MIM-1 preferring alkaline and MIM-2 acidic conditions. Both enzymes require Zn(II) but activity can also be reconstituted with other metal ions including Co(II), Mn(II), Cu(II) and Ca(II). Importantly, the substrate preference of MIM-1 and MIM-2 appears to be influenced by their metal ion composition. Since neither N. pentaromativorans nor S. agarivorans are human pathogens, the precise biological role(s) of MIM-1 and MIM-2 remains to be established. However, due to the similarity of at least some of their in vitro functional properties to those of known MBLs, MIM-1 and MIM-2 may provide essen...Continue Reading

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Citations

Jan 12, 2017·Scientific Reports·Chun-Feng D HouDavid L Ollis
Jul 28, 2017·Metallomics : Integrated Biometal Science·Marcelo Monteiro PedrosoGerhard Schenk
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Oct 26, 2016·Chemistry : a European Journal·Christopher SelleckGerhard Schenk
Jul 27, 2021·Antimicrobial Agents and Chemotherapy·Liam A WilsonGerhard Schenk

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