Rare earth elements play a pivotal role in high-technology devices, are used as contrast agents for magnetic resonance imaging in clinical settings, are explored as drug carriers for tumor photodynamic therapy, and are used as fertilizers. From the biochemical viewpoint, they act not only as antagonists of Ca2+ but have been proposed as alternative to Ca2+ in metallo-enzymes, in particular in Ce3+-based methanol dehydrogenases (MDHs). Up to now, the analysis of protein sequence databases identified Ce3+-based MHDs only in Archea and Bacteria. Here, we report evidence that Ce3+-based MDHs are also present in higher organisms. These enzymes, identified in the parasite Plasmodium yoelii yoelii, in the spider Nephila clavipes, in the Tibetan antelope Pantholops hodgsonii, and in Homo sapiens, are encoded by intronless genes, thus representing a case of multiple, independent lateral gene transfer from Prokaryotes to Eukaryotes. The conservation of residues involved in the Ce3+ coordination, pyrroquinoline quinone cofactor recognition and in the structure stabilization suggests that these enzymes belong to the Ce3+-dependent MDH family, hitherto considered as exclusive of Prokaryotes. © 2018 IUBMB Life, 70(11):1067–1075, 2018.
De Simone, G., Polticelli, F., Aime, S., Ascenzi, P. (2018). Lanthanides-based catalysis in eukaryotes. IUBMB LIFE, 70(11), 1067-1075 [10.1002/iub.1933].
Lanthanides-based catalysis in eukaryotes
De Simone, Giovanna;Polticelli, Fabio;Ascenzi, Paolo
2018-01-01
Abstract
Rare earth elements play a pivotal role in high-technology devices, are used as contrast agents for magnetic resonance imaging in clinical settings, are explored as drug carriers for tumor photodynamic therapy, and are used as fertilizers. From the biochemical viewpoint, they act not only as antagonists of Ca2+ but have been proposed as alternative to Ca2+ in metallo-enzymes, in particular in Ce3+-based methanol dehydrogenases (MDHs). Up to now, the analysis of protein sequence databases identified Ce3+-based MHDs only in Archea and Bacteria. Here, we report evidence that Ce3+-based MDHs are also present in higher organisms. These enzymes, identified in the parasite Plasmodium yoelii yoelii, in the spider Nephila clavipes, in the Tibetan antelope Pantholops hodgsonii, and in Homo sapiens, are encoded by intronless genes, thus representing a case of multiple, independent lateral gene transfer from Prokaryotes to Eukaryotes. The conservation of residues involved in the Ce3+ coordination, pyrroquinoline quinone cofactor recognition and in the structure stabilization suggests that these enzymes belong to the Ce3+-dependent MDH family, hitherto considered as exclusive of Prokaryotes. © 2018 IUBMB Life, 70(11):1067–1075, 2018.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
