On the Purification and Mechanism of Action of 5-Aminoimidazole-4-carboxamide-Ribonucleotide Transformylase from Chicken Liver

W. Thomas Mueller, Stephen J. Benkovic

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59 Scopus citations

Abstract

The transformylase from chicken liver catalyzing the formylation of 5-aminoimidazole-4-carboxamide ribonucleotide through the agency of 10-formyltetrahydrofolate has been purified to apparent homogeneity. Inosinicase activity copurifies. This transformylase is not further activated kinetically by the presence of the trifunctional protein in contrast to the glycinamide ribonucleotide transformylase. The enzyme exhibits a > 1000-fold preference for the naturally occurring 10-formyltetrahydrofolate cofactor and a sequential reaction pattern. A reinvestigation of the chemical structure of the formylated ribotide product employing 13C and 1H NMR indicated that the imidazole ring remained intact upon formylation, consistent with the originally proposed structure.

Original languageEnglish (US)
Pages (from-to)337-344
Number of pages8
JournalBiochemistry
Volume20
Issue number2
DOIs
StatePublished - Jan 1981

All Science Journal Classification (ASJC) codes

  • Biochemistry

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