Isolation of a Multifunctional Protein with Aminoimidazole Ribonucleotide Synthetase, Glycinamide Ribonucleotide Synthetase, and Glycinamide Ribonucleotide Transformylase Activities: Characterization of Aminoimidazole Ribonucleotide Synthetase

J. L. Schrimsher, F. J. Schendel, J. Stubbe

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Abstract

5-Aminoimidazole ribonucleotide (AIR) synthetase, glycinamide ribonucleotide (GAR) synthetase, and GAR transformylase activities from chicken liver exist on a single polypeptide of Mr110000 [Daubner, C. S., Schrimsher, J. L., Schendel, F. J., Young, M., Henikoff, S., Patterson, D., Stubbe, J., & Benkovic, S. J. (1985) Biochemistry 24, 7059–7062]. Details of copurification of these three activities through four chromatographic steps are reported. The ratios of these activities remain constant throughout the purification. AIR synthetase has an absolute requirement for K+ for activity and under these conditions has apparent molecular weights of 330000, determined by Sephadex G-200 chromatography, and 133 000, determined by sucrose density gradient ultracentrifugation. Incubation of 18O-labeled formylglycinamidine ribonucleotide (FGAM) with AIR synthetase results in stoichiometric production of AIR, ADP, and [18O]Pi. NMR spectra of β-FGAM and β-AIR are reported.

Original languageEnglish (US)
Pages (from-to)4356-4365
Number of pages10
JournalBiochemistry
Volume25
Issue number15
DOIs
StatePublished - Jul 1986

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