PMID:3530323
| Citation |
Schrimsher, JL, Schendel, FJ, Stubbe, J and Smith, JM (1986) Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli. Biochemistry 25:4366-71 |
|---|---|
| Abstract |
Aminoimidazole ribonucleotide (AIR) synthetase has been purified 15-fold to apparent homogeneity 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 Mr 38,500. 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 [18O]formylglycinamide ribonucleotide to Pi. |
| Links | |
| Keywords |
Amino Acids/analysis; Carbon-Nitrogen Ligases; Escherichia coli/enzymology; Kinetics; Ligases/isolation & purification; Ligases/metabolism; Macromolecular Substances; Magnetic Resonance Spectroscopy; Molecular Weight; Oxygen Isotopes |
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