PMID:9452430
| Citation |
O'Handley, SF, Frick, DN, Dunn, CA and Bessman, MJ (1998) Orf186 represents a new member of the Nudix hydrolases, active on adenosine(5')triphospho(5')adenosine, ADP-ribose, and NADH. J. Biol. Chem. 273:3192-7 |
|---|---|
| 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. |
| Links | |
| Keywords |
Adenosine Diphosphate Ribose/metabolism; Amino Acid Sequence; Animals; Cloning, Molecular; Dinucleoside Phosphates/metabolism; Humans; Hydrolases/genetics; Hydrolases/metabolism; Molecular Sequence Data; NAD/metabolism; Pyrophosphatases/genetics; Pyrophosphatases/isolation & purification; Pyrophosphatases/metabolism; Sequence Homology, Amino Acid; Substrate Specificity |
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