Phosphorylation of cytokinin by adenosine kinase from wheat germ |
| |
Authors: | Chen C M Eckert R L |
| |
Institution: | Science Division, University of Wisconsin-Parkside, Kenosha, Wisconsin 53140. |
| |
Abstract: | Adenosine kinase was partially purified from wheat germ. This enzyme preparation, which was devoid of adenine phosphoribosyltransferase and nearly free of adenosine deaminase but contained adenylate kinase, rapidly phosphorylated adenosine and a cytokinin, N6-(δ2-isopentenyl)adenosine. Electrophoretic analysis indicated that only N6-(δ2-isopentenyl)adenosine-monophosphate was formed from the cytokinin while about 55% AMP, 45% ADP, and a trace of ATP were formed from adenosine. The biosynthesized nucleoside monophosphates were quantitatively hydrolyzed to the corresponding nucleosides by 5′-nucleotidase and the isopentenyl side chain of the phosphorylated cytokinin was not cleaved. The enzyme did not catalyze phosphorylation of inosine. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|