Escherichia coli QueD Is a 6-Carboxy-5,6,7,8-tetrahydropterin Synthase

• Published in: Biochemistry (Easton) Vol. 48; no. 11; pp. 2301 - 2303
• Main Authors: McCarty, Reid M, Somogyi, Árpád, Bandarian, Vahe
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 24-03-2009
• Subjects: Carbon-Oxygen Lyases - chemistry; Carbon-Oxygen Lyases - genetics; Carbon-Oxygen Lyases - metabolism; Escherichia coli; Escherichia coli - chemistry; Escherichia coli - enzymology; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Neopterin - analogs & derivatives; Neopterin - metabolism; Pteridines - metabolism
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi9001437

To elucidate the early steps required during biosynthesis of a broad class of 7-deazapurine-containing natural products, we have studied the reaction catalyzed by Escherichia coli QueD, a 6-pyruvoyl-5,6,7,8-tetrahydropterin synthase (PTPS) homologue possibly involved in queuosine biosynthesis. While mammalian PTPS homologues convert 7,8-dihydroneopterin triphosphate (H2NTP) to 6-pyruvoyltetrahydropterin (PPH4) in biopterin biosynthesis, E. coli QueD catalyzes the conversion of H2NTP to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4). E. coli QueD can also convert PPH4 and sepiapterin to CPH4, allowing a mechanism to be proposed.