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Thymidine Phosphorylation in Arachis hypogaea by Combined Activities of Adenosine Triphosphate Phosphohydrolase and Nucleoside Phosphotransferase
Author(s) -
MULLIN BETH C.,
FITES ROGER C.
Publication year - 1978
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1978.tb04103.x
Subject(s) - thymidine , phosphotransferase , biochemistry , adenosine triphosphate , thymidine kinase , nucleoside , arachis hypogaea , chemistry , adenosine , adenosine monophosphate , enzyme , biology , dna , virus , virology , herpes simplex virus , agronomy
Extracts from hypocotyls of germinating peanuts ( Arachis hypogaea L.) stimulated the formation of thymidine monophosphate from thymidine and adenosine triphosphate in the presence of magnesium ions. Such extracts were incapable of incorporating isotopic phosphorus from gamma‐labelled adenosine triphosphate into thymidine during the synthesis of thymidine monophosphate but were competent in transferring phosphorus from alpha‐labelled adenosine triphosphate to thymidine. The apparent thymidine kinase activity thus appeared to result from the combined activities of an adenosine triphosphatase (adenosine triphosphate pyrophosphohydrolase, E. C. 3.6.1.3) and a nucleoside phosphotransferase (E. C. 2.7.1.77). The latter two enzymes could be largely separated by using DEAE‐Sephadex chromatography.