Purification and Characterization of Aminoimidazole Ribonucleotide Synthetase from Escherichia coli

J. L. Schrimsher, F. J. Schendel, J. Stubb, J. M. Smith

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35 Scopus citations

Abstract

Aminoimidazole ribonucleotide (AIR) synthetase has been purified 15-fold to apparent ho-mogeneity from Escherichia coli which contains a multicopy plasmid containing the purM, AIR synthetase, gene. The protein is a dimer composed of two identical subunits of Mr38 500. The N-terminal sequence, amino acid composition, and steady-state kinetics of the protein have been determined. AIR synthetase has been shown to catalyze the transfer of the formyl oxygen of [180]formylglycinamide ribonucleotide to Pi.

Original languageEnglish (US)
Pages (from-to)4366-4371
Number of pages6
JournalBiochemistry
Volume25
Issue number15
DOIs
StatePublished - Jul 1986
Externally publishedYes

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