2026-06-28T20:24:47Zhttps://docta.ucm.es/rest/oai/request

oai:docta.ucm.es:20.500.14352/582502024-06-07T16:06:25Zcom_20.500.14352_14col_20.500.14352_15

ADP-ribosyltransferases: plastic tools for inactivating protein and small molecular weight targets Reche Gallardo, Pedro Antonio Koch-Nolte, Friedrich Haag, Friedrich Bazan, Fernando ADP-ribosyltransferases (ADPRTs) form an interesting class of enzymes with well-established roles as potent bacterial toxins and metabolic regulators. ADPRTs catalyze the transfer of the ADP-ribose moiety from NAD(+) onto specific substrates including proteins. ADP-ribosylation usually inactivates the function of the target. ADPRTs have become adapted to function in extra- and intracellular settings. Regulation of ADPRT activity can be mediated by ligand binding to associated regulatory domains, proteolytic cleavage, disulphide bond reduction, and association with other proteins. Crystallisation has revealed a conserved core set of elements that define an unusual minimal scaffold of the catalytic domain with remarkably plastic sequence requirements--only a single glutamic acid residue critical to catalytic activity is invariant. These inherent properties of ADPRTs suggest that the ADPRT catalytic fold is an attractive, malleable subject for protein design. 2023-06-20T17:26:46Z 2023-06-20T17:26:46Z 2023-06-20T17:26:46Z 2001 journal article https://hdl.handle.net/20.500.14352/58250 1873-4863 eng open access Elsevier