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A mechanistic study of the non-oxidative decarboxylation catalyzed by the radical S-adenosyl-L-methionine enzyme BlsE involved in blasticidin S biosynthesis

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Abstract

Decarboxylation is a fundamentally important reaction in biology and involves highly diverse mechanisms. Here we report a mechanistic study of the non-oxidative decarboxylation catalyzed by BlsE, a radical S-adenosyl-L-methionine (SAM) enzyme involved in blasticidin S biosynthesis. Through a series of biochemical analysis with isotopically labeled reagents, we show that the BlsE-catalyzed reaction is initiated by the 5′-deoxyadenosyl (dAdo) radical-mediated hydrogen abstraction from a sugar carbon of the substrate cytosylglucuronic acid (CGA), and does not involve a carboxyl radical as has been proposed for 4-hydroxyphenylacetate decarboxylase (HPAD). Our study reveals that BlsE represents a mechanistically new type of radical-based decarboxylase.

Graphical abstract: A mechanistic study of the non-oxidative decarboxylation catalyzed by the radical S-adenosyl-l-methionine enzyme BlsE involved in blasticidin S biosynthesis

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Publication details

The article was received on 02 Jun 2017, accepted on 26 Jun 2017 and first published on 26 Jun 2017


Article type: Communication
DOI: 10.1039/C7CC04286H
Citation: Chem. Commun., 2017, Advance Article
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    A mechanistic study of the non-oxidative decarboxylation catalyzed by the radical S-adenosyl-L-methionine enzyme BlsE involved in blasticidin S biosynthesis

    L. Liu, X. Ji, Y. Li, W. Ji, T. Mo, W. Ding and Q. Zhang, Chem. Commun., 2017, Advance Article , DOI: 10.1039/C7CC04286H

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