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Article Abstract
RohQ from the azomycin biosynthetic pathway catalyzes a spontaneous cyclodehydration to form 2-aminoimidazole. Here we report the structure and mechanism of RohQ and use a serendipitously bound imidazole to pinpoint active site residues. We propose that catalysis occurs at the dimeric interface using two key aspartic acid residues for proton transfer steps to accelerate 3 × 10-fold intramolecular cyclization of a guanidino group and aldehyde, releasing water. Our work expands our understanding of emerged enzymes and provides the first structural and mechanistic view of a yet-unexplored protein family.
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