| dc.contributor.author | O'Handley, Suzanne | en_US |
| dc.contributor.author | Frick, David | en_US |
| dc.contributor.author | Dunn, Christopher | en_US |
| dc.contributor.author | Bessman, Maurice | en_US |
| dc.date.accessioned | 2006-07-19T19:50:22Z | en_US |
| dc.date.available | 2006-07-19T19:50:22Z | en_US |
| dc.date.issued | 1998-02-06 | en_US |
| dc.identifier.citation | Journal of Biological Chemistry 273N6 (1998) 3192-3197 | en_US |
| dc.identifier.issn | 1083-351X | en_US |
| dc.identifier.uri | http://hdl.handle.net/1850/2199 | en_US |
| dc.description.abstract | Orf186, a new member of the Nudix hydrolase family of genes, has been cloned and expressed, and the protein has been purified and identified as an enzyme highly specific for compounds of ADP. Its three major substrates are adenosine(5)triphospho(5)adenosine, ADP-ribose, and NADH, all implicated in a variety of cellular regulatory processes, supporting the notion that the function of the Nudix hydrolases is to monitor the concentrations of reactive nucleoside diphosphate derivatives and to help modulate their accumulation during cellular metabolism. | en_US |
| dc.description.sponsorship | This work was supported by National Institutes of Health Grant GM18649. | en_US |
| dc.format.extent | 35618 bytes | en_US |
| dc.format.mimetype | application/pdf | en_US |
| dc.language.iso | en_US | en_US |
| dc.publisher | The American Society for Biochemistry and Molecular Biology: Journal of Biological Chemistry | en_US |
| dc.subject | ADP | en_US |
| dc.subject | Hydrolases | en_US |
| dc.subject | Nudix | en_US |
| dc.title | Orf186 represents a new member of the nudix hydrolases, active on adenosine(5)triphospho(5)adenosine, ADP-ribose, and NADH | en_US |
| dc.type | Abstract | en_US |
| dc.identifier.url | http://dx.doi.org/10.1074/jbc.273.6.3192 | |
