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Dihydrofolate reductase and thymidylate synthase in plants: an open problem
Author(s) -
Cella Rino,
Parisi Bruno
Publication year - 1993
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.1399-3054.1993.tb01366.x
Subject(s) - thymidylate synthase , dihydrofolate reductase , enzyme , biochemistry , atp synthase , biology , genetics , fluorouracil , chemotherapy
This review deals with recent findings in the purification and characterization of dihydrofolate reductase (DHFR) and thymidylate synthase (TS) in plants. The few enzymes purified, which differ remarkably in regard to their structure. kinetic and molecular properties and subcellular location are described. The response of DHFRs to antifolic agents and the analysis of resistance mechanisms in isolated cell lines is also reported. Problems opened by recent studies of the enzymes isolated from plants are outlined.