Catalysis of a New Ribose Carbon-Insertion Reaction by the Molybdenum Cofactor Biosynthetic Enzyme MoaA
| Autor: | Angad P. Mehta, Sameh H. Abdelwahed, David G. Hilmey, Tadhg P. Begley, Jeremiah Hanes, Petra Hänzelmann |
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| Rok vydání: | 2013 |
| Předmět: |
Spectrometry
Mass Electrospray Ionization Magnetic Resonance Spectroscopy Hydrolases Stereochemistry Ribose Coenzymes Guanosine triphosphate Hydrogen atom abstraction Biochemistry Article Catalysis chemistry.chemical_compound Biosynthesis Insertion reaction Metalloproteins Organic chemistry Pteridines Molybdopterin Carbon Models Chemical chemistry Guanosine Triphosphate Molybdenum cofactor Molybdenum Cofactors |
| Zdroj: | Biochemistry. 52:1134-1136 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi3016026 |
| Popis: | MoaA, a radical S-adenosylmethionine (SAM) enzyme, catalyzes the first step in molybdopterin biosynthesis. This reaction involves a complex rearrangement in which C8 of guanosine triphosphtate is inserted between the C2′ and the C3′ carbons of the ribose. This study identifies the site of initial hydrogen atom abstraction by the adenosyl radical and advances a mechanistic proposal for this unprecedented reaction. |
| Databáze: | OpenAIRE |
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