Enzymological properties of poly(ADP-ribose)polymerase: characterization of automodification sites and NADase activity
| Autor: | Jean Lagueux, Luc Ménard, Guy G. Poirier, Yvan Desmarais |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Glycoside Hydrolases
Polymers Poly ADP ribose polymerase Biophysics Biochemistry NAD+ Nucleosidase Structural Biology Animals Binding site Molecular Biology Chromatography High Pressure Liquid Polymerase chemistry.chemical_classification Binding Sites biology Phosphoric Diester Hydrolases NAD+ ADP-Ribosyltransferase Molecular biology Kinetics Enzyme chemistry Phosphodiesterase I ADP-ribosylation biology.protein Cattle Electrophoresis Polyacrylamide Gel NAD+ kinase Poly(ADP-ribose) Polymerases Binding domain |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1078:179-186 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/0167-4838(91)99007-f |
| Popis: | We have characterized the effect of poly(ADP-ribose) polymerase automodification on the enzyme's activities, which include poly(ADP-ribose) synthesis and NADase activity. The apparent Km of the enzyme for NAD+ during polymer synthesis is higher than the one measured for alternate NADase activity. Furthermore, we have found that there are 28 automodification sites, in contrast to the 15 sites (postulated to be on the 15 glutamic acids) reported to be present in the automodification domain. For the first time, we show that some of these acceptor sites are outside the reported automodification domain (15 kDa); we demonstrate automodification in the NAD+ binding domain (55.2 kDa) and the DNA binding domain (42.5 kDa). We have analyzed the relationship between the number of sites modified on poly(ADP-ribose) polymerase and its effect on the polymerization activity and its alternate NADase activity. Automodification greatly altered both enzyme activities, decreasing both polymer synthesis and alternate NADase activity. |
| Databáze: | OpenAIRE |
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