Structural and Mechanistic Studies on the HeLa and Chicken Liver Proteins That Catalyze Glycinamide Ribonucleotide Synthesis and Formylation and Aminoimidazole Ribonucleotide Synthesis

Susan Colette Daubner, Mark Young, R. Douglas Sammons, Lawrence F. Courtney, Stephen Benkovic

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

Glycinamide ribonucleotide (GAR) transformylase from HeLa cells has been purified 200-fold to apparent homogeneity with a procedure using two affinity resins. The activities glycinamide ribonucleotide synthetase and aminoimidazole ribonucleotide synthetase were found to copurify with GAR transformylase. Glycinamide ribonucleotide synthetase and GAR transformylase were separable only after exposure to chymotrypsin. Antibodies raised to pure L1210 cell GAR transformylase were able to precipitate the glycinamide ribonucleotide transformylase and GAR synthetase activities from HeLa and L1210 cells both in their native and in their proteolytically shortened forms. The compound N-10-(bromoacetyl)-5,8-di-deazafolate was found to inhibit formylation but to leave the ATP-requiring synthetase activities intact.

Original languageEnglish (US)
Pages (from-to)2951-2957
Number of pages7
JournalBiochemistry
Volume25
Issue number10
DOIs
StatePublished - Jan 1 1986

All Science Journal Classification (ASJC) codes

  • Biochemistry

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