Pub. Date : 1997 Feb 14
PMID : 9020087
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Lysine 129 of CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase) participates in the binding of ATP to inhibit the cyclic ADP-ribose hydrolase. | Adenosine Triphosphate | CD38 molecule | Homo sapiens |
| 2 | CD38 catalyzes not only the formation of cyclic ADP-ribose (cADPR) from NAD+ but also the hydrolysis of cADPR to ADP-ribose (ADPR), and ATP inhibits the hydrolysis (Takasawa, S., Tohgo, A., Noguchi, N., Koguma, T., Nata, K., Sugimoto, T., Yonekura, H., and Okamoto, H. (1993) J. Biol. | Adenosine Triphosphate | CD38 molecule | Homo sapiens |
| 3 | In the present study, using purified recombinant CD38, we showed that the cADPR hydrolase activity of CD38 was inhibited by ATP in a competitive manner with cADPR. | Adenosine Triphosphate | CD38 molecule | Homo sapiens |
| 4 | In the present study, using purified recombinant CD38, we showed that the cADPR hydrolase activity of CD38 was inhibited by ATP in a competitive manner with cADPR. | Adenosine Triphosphate | CD38 molecule | Homo sapiens |
| 5 | To identify the binding site for ATP and/or cADPR, we labeled the purified CD38 with FSBA. | Adenosine Triphosphate | CD38 molecule | Homo sapiens |
| 6 | These results indicate that Lys-129 of CD38 participates in cADPR binding and that ATP competes with cADPR for the binding site, resulting in the inhibition of the cADPR hydrolase activity of CD38. | Adenosine Triphosphate | CD38 molecule | Homo sapiens |