PMID:10508786

Citation	Li, C, Kappock, TJ, Stubbe, J, Weaver, TM and Ealick, SE (1999) X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution. Structure 7:1155-66
Abstract	The purine biosynthetic pathway in procaryotes enlists eleven enzymes, six of which use ATP. Enzymes 5 and 6 of this pathway, formylglycinamide ribonucleotide (FGAR) amidotransferase (PurL) and aminoimidazole ribonucleotide (AIR) synthetase (PurM) utilize ATP to activate the oxygen of an amide within their substrate toward nucleophilic attack by a nitrogen. AIR synthetase uses the product of PurL, formylglycinamidine ribonucleotide (FGAM) and ATP to make AIR, ADP and P(i).
Links	PubMed
Keywords	Adenosine Triphosphate/metabolism; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Carbon-Nitrogen Ligases/chemistry; Carbon-Nitrogen Ligases/isolation & purification; Carbon-Nitrogen Ligases/metabolism; Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor; Crystallization; Crystallography, X-Ray; Dimerization; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins; Ligases; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Folding; Purines/biosynthesis; Sequence Alignment; Sequence Homology, Amino Acid; Sulfates/metabolism
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