Molybdopterin Biosynthesis: Trapping an Unusual Purine Ribose Adduct in the MoaA-Catalyzed Reaction

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• 作者：Angad P. Mehta ; Sameh H. Abdelwahed ; Tadhg P. Begley
• 刊名：The Journal of the American Chemical Society
• 出版年：2013
• 出版时间：July 31, 2013
• 年：2013
• 卷：135
• 期：30
• 页码：10883-10885
• 全文大小：260K
• 年卷期：v.135,no.30(July 31, 2013)
• ISSN：1520-5126

文摘

MoaA/MoaC catalyze a remarkable rearrangement reaction in which guanosine-5鈥?triphosphate (GTP) is converted to cyclic pyranopterin monophosphate (cPMP). In this reaction, the C8 of GTP is inserted between the C2鈥?and the C3鈥?carbons of the GTP ribose. Previous experiments with GTP isotopomers demonstrated that the ribose C3鈥?hydrogen atom is abstracted by the adenosyl radical. This led to a novel mechanistic proposal involving an intermediate with a bond between the C8 of guanine and C3鈥?of the ribose. This paper describes the use of 2鈥?3鈥?dideoxyGTP to trap this intermediate.