caa a22 4500 397494327 CHVBK 20180308164517.0 cr unu---uuuuu 161202e199501 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a124698 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a124698 Enzyme Properties of Aplysia ADP-Ribosyl Cyclase: Comparison with NAD Glycohydrolase of CD38 Antigen [Elektronische Daten] [Kiyoshi Inageda, Katsunobu Takahashi, Ken-ichi Tokita, Hiroshi Nishina, Yasunori Kanaho, Iwao Kukimoto, Kenji Kontani, Shin-ichi Hoshino, Toshiaki Katadat] An ecto-enzyme of NAD glycohydrolase (NADase) induced by retinoic acid in HL-60 cells is attributed to the molecule of CD38 antigen [Kontani, K., Nishina, H., Ohoka, Y., Takahashi, K., and Katada, T. (1993) J. Biol. Chem. 268, 16895-16898]. CD38 antigen has an amino acid sequence homologous to Aplysia ADP-ribosyl cyclase which generates cyclic adenosine diphosphoribose (cADPR) and nicotinamide (NA) from β-NAD+. On the basis of this sequence homology, we compared enzyme properties between CD38 NADase expressed as a fusion protein in Escherichia coli and ADP-ribosyl cyclase purified from the ovotestis of Aplysia kurodai. 1) β-NAD+ analogs, nicotinamide 1, N6-ethenoadenine dinucleotide, and nicotinamide hypoxanthine dinucleotide, did not serve as good substrates for the ADP-ribosyl cyclase, suggesting that the intact adenine ring of β-NAD+ was required for the cyclase-catalyzed reaction. On the other hand, CD38 NADase utilized the NAD analogs to form ADP-ribose and NA. 2) Kinetic analyses of the ADP-ribosyl cyclase reaction revealed that NA was first released from the substrate (β-NAD+)-enzyme complex, followed by the release of another product, cADPR, which was capable of interacting with the free enzyme. 3) The enzyme reaction catalyzed by the ADP-ribosyl cyclase was fully reversible; β-NAD+ could be formed from cADPR and NA with a velocity similar to that observed in the degradation of β-NAD+. However, CD38 NADase did not catalyze the reverse reaction to form β-NAD+ from ADP-ribose and NA. 4) The CD38 NADase activity was, but the ADP-ribosyl cyclase activity was not, inhibited by dithiothreitol. These results indicated that enzyme reactions catalyzed by Aplysia ADP-ribosyl cyclase and CD38 NADase were quite different from each other in terms of their substrate specificities, reversible reactions, and susceptibilities to dithiothreitol, though both enzymes cleaved the N-glycoside bond of β-NAD+ resulting in the liberation of NA. © 1995 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence ADP-ribosyl cyclase nationallicence CD38 antigen nationallicence cyclic ADP-ribose nationallicence NAD glycohydrolase nationallicence Inageda Kiyoshi Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227 aut Takahashi Katsunobu Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227 aut Tokita Ken-ichi Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227 aut Nishina Hiroshi Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227 aut Kanaho Yasunori Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227 aut Kukimoto Iwao Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113 aut Kontani Kenji Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113 aut Hoshino Shin-ichi Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113 aut Katadat Toshiaki Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113 aut The Journal of Biochemistry Oxford University Press 117/1(1995-01), 125-131 0021-924X 117:1<125 1995 117 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a124698 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a124698 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Inageda Kiyoshi Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227 aut NATIONALLICENCE 700 1- Takahashi Katsunobu Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227 aut NATIONALLICENCE 700 1- Tokita Ken-ichi Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227 aut NATIONALLICENCE 700 1- Nishina Hiroshi Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227 aut NATIONALLICENCE 700 1- Kanaho Yasunori Department of Life Science, Tokyo Institute of Technology Midori-ku, Yokohama 227 aut NATIONALLICENCE 700 1- Kukimoto Iwao Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Kontani Kenji Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Hoshino Shin-ichi Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Katadat Toshiaki Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 117/1(1995-01), 125-131 0021-924X 117:1<125 1995 117 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford