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JBC, Vol. 253, Issue 12, 4242-4244, Jun, 1978
I. K. Dev and R. J. Harvey
Glycinamide ribotide transformylase from Escherichia coli was obtained free
of N5,N10-methenyltetrahydrofolate cyclohydrolase activity by
DEAE-cellulose chromatography. In reaction mixtures containing this enzyme
preparation in potassium maleate buffer, pH 7.2, no detectable
interconversion of N5,N10-methenyltetrahydrofolate occurred. Upon addition
of glycinamide ribotide, N-formylglycinamide ribotide was formed when
N10-formyltetrahydrofolate was present; no formylation occurred in the
presence of N5,N10-methenyltetrahydrofolate. A method for the synthesis and
purification of glycinamide ribotide is presented.
N10-Formyltetrahydrofolate is the formyl donor for glycinamide ribotide transformylase in Escherichia coli
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