PMID: 3756144Jul 29, 1986Paper

Isolation of a multifunctional protein with aminoimidazole ribonucleotide synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase activities: characterization of aminoimidazole ribonucleotide synthetase

Biochemistry
J L SchrimsherJ Stubbe

Abstract

5-Aminoimidazole ribonucleotide (AIR) synthetase, glycinamide ribonucleotide (GAR) synthetase, and GAR transformylase activities from chicken liver exist on a single polypeptide of Mr 110,000 [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 330,000, 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 beta-FGAM and beta-AIR are reported.

Citations

Jan 1, 1992·Progress in Biophysics and Molecular Biology·G Wächtershäuser
Mar 20, 2003·Plant Physiology·Danica Erin GogginPenelope Mary Collina Smith
Oct 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·M P GroziakN J Leonard
Sep 1, 1987·The Journal of Experimental Zoology·J W CampbellD D Smith
Jun 1, 1993·Journal of Bacteriology·P Nygaard, J M Smith
Jan 8, 2003·The Journal of Organic Chemistry·Mark McLaughlinHenry Rapoport

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