作者: Holly D. Doremus , Dale G. Blevins
DOI: 10.1104/PP.87.1.41
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摘要: A specific nucleoside diphosphatase was purified from the plant portion of soybean (Glycine max L.) root nodules. This enzyme is highly for nucleotide diphosphates; it unable to hydrolyze tri- and monophosphates or a variety other phosphorylated compounds. It will, however, any disphosphate tested. The pH optimum about 7.5; requires divalent cation activity; neither inhibited nor activated by metabolites appears that in vivo this would be very active, but its function not clear.