Abstract
The majority of the mono(ADP-ribosyl) transferases identified to date in animal tissues (1–5) are characterized by their specific modification of the guanidinium group of arginine residues. In contrast, poly(ADP-ribose) polymerase is known only to modify carboxylate groups on protein acceptors, i.e., glutamate (6–9), carboxy-terminal lysine (8) and aspartate (10). Both classes of enzymes have identical substrate stereospecificity in which the β-configuration of the anomeric carbon of NAD+ is converted to the α-configuration in the product (11, 12). No major differences between these two classes of enzymes in substrate structural requirements have been documented. The present study identifies a difference in behavior of an NAD+:arginine mono(ADP-ribosyl) transferase from turkey erythrocytes (2) and poly(ADP-ribose) polymerase from calf thymus (13) toward 2′dNAD+ as a substrate.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Moss, J., Vaughan, M. (1978) Proc Natl Acad Sci USA 75: 3621–3624
Moss, J., Stanley, S.J., Watkins, P.A. (1980) J Biol Chem 258: 5838–5840
Yost, D., Moss, J. (1983) J Biol Chem 258: 4946–4929
Tanigawa, Y., Tsuchiya, M., Imai, Y., Shimoyama, M. (1984) J Biol Chem 259: 2022–2029
Soman, G., Miehelson, I.R., Louis, C.F., Graves, D.J. (1984) Biochem Biophys Res Commun 120: 973–980
Riquelme, P.T., Burzio, L.O., Koide, S.S. (1979) J Biol Chem 254: 3018–3028
Burzio, L.O., Riquelme, P.T., Koide, S.S. (1979) J Biol Chem 245: 3029–3037
Ogata, N., Ueda, K., Hayaishi, O. (1980) J Biol Chem 255: 7610–7615
Ogata, N., Ueda, K., Kagamiyama, H., Hayaishi, O. (1980) J Biol Chem 255: 7616–7620
Suzuki, H., Quesada, P., Farina, F., Leone, E. (1986) J Biol Chem 261: 6048–6055
Ferro, A.M., Oppenheimer, N.J. (1978) Proc Natl Acad Sci USA 75: 809–813
Moss, J., Stanley, S.J., Oppenheimer, N.J. (1979) J Biol Chem 254: 8891–8894
Niedergang, C.P., Okasaki, N., Mandel, M. (1979) Eur J Biochem 102: 43–57
Alvarez-Gonzalez, R., Juarez-Salinas, H., Jacobson, E.L., Jacobson, M.K. (1983) Anal Biochem 135: 69–77
Jacobson, M.K., Payne, D.M., Alvarez-Gonzalez, R., Juarez-Salinas, H., Sims, J.L., Jacobson, EX. (1984) Methods Enzymol 106: 483–494
Zahradka, P., Ebisuzaki, K. (1984) Eur J Biochem 142: 503–509
Suhadolnik, R.J., Baur, R., Lichtenwalner, D.M., Uematsu, T., Roberts, J.H., Sudhakar, S., Smulson, M. (1977) J Biol Chem 252: 4134–4144
Lichtenwalner, D.M., Suhadolnik, R.J. (1979) Biochem 18: 3749–3755
Suhadolnik, R.J. (1982) ADP-ribosylation reactions: Biology and Medicine. O. Hayaishi, K. Uda (eds.), Academic Press, Inc. New York, pp. 65–75.
Hilz, H., Koch, R., Fanick, W., Klapproth, K., Adamietz, P. (1984) Proc Natl. Acad Sci USA 81: 3929–3933
Ikejima, M., Gill, D.M. (1985) Biochem 24: 5039–5045
Moss, J., Jacobson, M.K., Stanley, S.J. (1985) Proc Natl Acad Sci USA 82: 5603–5607
Moss, J., Oppenheimer, N.J., West, R.E., Stanley, S.J. (1986) Biochem 25: 5408–5414
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1989 Springer-Verlag New York Inc.
About this chapter
Cite this chapter
Alvarez-Gonzalez, R., Moss, J., Niedergang, C., Althaus, F.R. (1989). In Vitro ADP-Ribosylation Utilizing 2′Deoxy-NAD+ as a Substrate. In: Jacobson, M.K., Jacobson, E.L. (eds) ADP-Ribose Transfer Reactions. Springer, New York, NY. https://doi.org/10.1007/978-1-4615-8507-7_9
Download citation
DOI: https://doi.org/10.1007/978-1-4615-8507-7_9
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4615-8509-1
Online ISBN: 978-1-4615-8507-7
eBook Packages: Springer Book Archive