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MUTANTS OF THE FORMYLTETRAHYDROFOLATE INTERCONVERSION PATHWAY OF SACCHAROMYCES CEREVISIAE
K. Q. McKenzie 1 and Elizabeth W. Jones 2
1 Case Western Reserve University, Cleveland, Ohio
2 Carnegie-Mellon University, Pittsburgh, Pennsylvania
Thirteen mutants of Saccharomyces cerevisiae that lack one or more of the three enzyme activities of the pathway for interconversion of tetrahydrofolate coenzymes at the formate level of oxidation have been isolated. They do not require adenine. All fail to complement mutations in the ade3 locus. Mutations that greatly reduce activity for one enzyme also reduce activity for the other two interconversion enzymes. The three enzyme activities cochromatograph on TEAE-cellulose columns. A mutation that eliminates synthetase activity also alters the chromatographic behavior of the remaining cyclohydrolase and dehydrogenase activities. It is suggested that the three activities reside in an enzyme complex encoded by the ade3 locus.
Submitted on October 19, 1976Revised on January 13, 1977
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