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Titolo:
HUMAN CD38 IS AN AUTHENTIC NAD(P)(+) GLYCOHYDROLASE
Autore:
BERTHELIER V; TIXIER JM; MULLERSTEFFNER H; SCHUBER F; DETERRE P;
Indirizzi:
HOP LA PITIE SALPETRIERE,CNRS,UA 625,LAB IMMUNOL CELLULAIRE,83 BLVD HOP F-75013 PARIS FRANCE HOP LA PITIE SALPETRIERE,CNRS,UA 625,LAB IMMUNOL CELLULAIRE F-75013 PARIS FRANCE FAC PHARM,CNRS,UA 1386,CHIM BIOORGAN LAB F-67400 ILLKIRCH GRAFFENS FRANCE
Titolo Testata:
Biochemical journal
, volume: 330, anno: 1998,
parte:, 3
pagine: 1383 - 1390
SICI:
0264-6021(1998)330:<1383:HCIAAN>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYCLIC ADP-RIBOSE; TRANSMEMBRANE GLYCOPROTEIN CD38; CALCIUM-MOBILIZING METABOLITE; LYMPHOCYTE ANTIGEN CD38; NAD+-GLYCOHYDROLASE; HUMAN ERYTHROCYTES; NAD(+) GLYCOHYDROLASE; ENZYMATIC-SYNTHESIS; CYCLASE ACTIVITY; OUTER SURFACE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
49
Recensione:
Indirizzi per estratti:
Citazione:
V. Berthelier et al., "HUMAN CD38 IS AN AUTHENTIC NAD(P)(+) GLYCOHYDROLASE", Biochemical journal, 330, 1998, pp. 1383-1390

Abstract

The leucoyte surface antigen CD38 has been shown to be an ecto-enzymewith multiple catalytic activities, It is principally a NAD(+) glycohydrolase that transforms NAD(+) into ADP-ribose and nicotinamide, CD38is also able to produce small amounts of cyclic ADP-ribose (ADP-ribosyl cyclase activity) and to hydrolyse this cyclic metabolite into ADP-ribose (cyclic ADP-ribose hydrolase activity), To classify CD38 among the enzymes that transfer the ADP-ribosyl moiety of NAD(+) to a variety of accepters, we have investigated its substrate specificity and some characteristics of its kinetic and molecular mechanisms. We find that CD38-catalysed cleavage of the nicotinamide-ribose bond results in the formation of an E . ADP-ribosyl intermediary complex, which is common to all reaction pathways; this intermediate reacts (1) with accepters such as water (hydrolysis), methanol (methanolysis) or pyridine (transglycosidation), and (2) intramolecularly, yielding cyclic ADP-ribose with a low efficiency. This reaction scheme is also followed when using nicotinamide guanine dinucleotide as an alternative substrate; in this case, however, the cyclization process is highly favoured. The results obtained here are not compatible with the prevailing model for the mode of action of CD38, according to which this enzyme produces first cyclic ADP-ribose which is then immediately hydrolysed into ADP-ribose (i.e. sequential ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities). We show instead that the cyclic metabolite was a reaction product of CD38 rather than an obligatory reaction intermediate during the glycohydrolase activity. Altogether our results lead to the conclusion that CD38 is an authentic 'classical' NAD(P)(+) glycohydrolase (EC 3.2.2.6).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 20:07:11