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... > Enzymes and Coenzymes > Enzymes > Transferases > Glycosyltransferases > Pentosyltransferases > ADP Ribose Transferases

Terme préférentiel

ADP Ribose Transferases  

Type

  • mesh:Descriptor

Définition

  • Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains. Enzymes that catalyze the transfer of one ADP-ribose moiety from NAD+ to an amino acid residue in specific protein substrates. This reaction is catalyzed by prokaryotic and eukaryotic enzymes. Mono-ADP-ribosylation is a mechanism of action common to several bacterial toxins. An enzyme that catalyzes the transfer of the ADP-ribose moiety from NAD+ or NADP+ to specific protein substrates with arginine, arginine-type compounds, agmatine, or guanidine as acceptors. This mono-ADP-ribosylation reaction is the mechanism of action common to several bacterial toxins affecting profound changes in cellular metabolism, such as activation of adenylate cyclase, regulation of protein synthesis at the level of elongation factor 2, and ion transport across biological membranes. An enzyme that catalyze the transfer of ADP-RIBOSE from NAD+ to an amino acid residue in a specific protein substrate. This reaction is catalyzed by both mono(ADP-ribose) transferases as well as POLY(ADP-RIBOSE) POLYMERASES. When the term NAD+ ADP-Ribosyltransferase refers to EC 2.4.2.30 it is referring to POLY(ADP-RIBOSE) POLYMERASES.

Concept générique

Concepts spécifiques

Concepts associés

Synonyme(s)

  • 81457-93-4 (CAS RN)
  • ADP Ribose Transferase
  • ADP-Ribosyltransferase
  • ADPRT
  • ADPRTs
  • ARTase
  • ARTases
  • ART Transferase
  • ART Transferases

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Traductions

URI

http://data.loterre.fr/ark:/67375/JVR-J72RJJQG-0

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RDF/XML TURTLE JSON-LD Date de création 02/07/2002, dernière modification le 14/04/2017