| Literature DB >> 9193651 |
S Karsten1, J Schröder, C da Silva, D Kahlke, H G Thiele, F Koch-Noite, F Haag.
Abstract
Recombinant RT6 proteins of rat and mouse were analyzed for NAD-metabolizing, i.e. mono(ADP-ribosyl)transferase, NAD-glycohydrolase (NADase) and ADP-ribosyl cyclase activities. The results reveal surprising intra- as well as inter-species differences in enzyme activities. While mouse Rt6 proteins were found to be strong arginine-specific transferases, but comparatively weak NADases, the opposite held true for rat RT6, for which transferase activity could only be detected in the form of arginine-specific auto-ADP-ribosylation, displayed by RT6.2 but not by RT6.1. NADase activity of rat RT6 was not accompanied by production of cyclic ADPR (cADPR). Rat RT6 gained potent arginine-specific transferase activity by exchange of a single amino acid for the corresponding residue of the mouse proteins.Entities:
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Year: 1997 PMID： 9193651 DOI： 10.1007/978-1-4419-8632-0_21
Source DB: PubMed Journal: Adv Exp Med Biol ISSN： 0065-2598 Impact factor: 2.622