1887

Abstract

Oxidation of 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate was the rate-limiting step in 5-methyltetrahydrofolate metabolism by . The limiting steps in the utilization of suboptimal levels of folate by were related to the ability of folates to function in purine and/or thymidylate biosynthesis. Folates with glutamate chains of up to at least seven residues were substrates for these biosynthetic enzymes, and comparisons of bacterial growth yields with transport rates for these folates indicated that the polyglutamates were more effective substrates in purine and thymidylate synthesis than the corresponding pteroylmonoglutamate contained low levels of a B-independent, pteroylpolyglutamate-specific methionine synthetase. Its methylene-tetrahydrofolate reductase also functioned more effectively with pteroylpolyglutamate substrates.

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/content/journal/micro/10.1099/00221287-103-2-261
1977-12-01
2021-10-24
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