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Título:
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ADP-ribosyltransferases: plastic tools for inactivating protein and small molecular weight targets
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Autores:
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Koch-Nolte, Friedrich ;
Reche, Pedro A ;
Haag, Friedrich ;
Bazan, Fernando
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Tipo de documento:
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texto impreso
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Editorial:
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Elsevier, 2001
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Dimensiones:
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application/pdf
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Nota general:
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info:eu-repo/semantics/openAccess
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Idiomas:
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Palabras clave:
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Estado = Publicado
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Materia = Ciencias Biomédicas: Biología: Evolución
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Materia = Ciencias: Informática: Bioinformática
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Materia = Ciencias Biomédicas: Biología: Biología molecular
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Tipo = Artículo
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Resumen:
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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.
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En línea:
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https://eprints.ucm.es/id/eprint/9343/1/14.Nolte_Reche_etal_JBiotech_2001.pdf
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