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 pteroylmonoglutamates. contained low levels of a B-independent, pteroylpolyglutamate-specific methionine synthetase. Its methylene-tetrahydrofolate reductase also functioned more effectively with pteroylpolyglutamate substrates.


Article metrics loading...

Loading full text...

Full text loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error