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

Chem Commun (Camb). 2017 Aug 8;53(64):8952-8955. doi: 10.1039/c7cc04286h.

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.

MeSH terms

  • Bacterial Proteins / metabolism*
  • Biocatalysis
  • Decarboxylation
  • Glucuronic Acid / chemistry
  • Glucuronic Acid / metabolism
  • Glucuronosyltransferase / metabolism*
  • Nucleosides / biosynthesis
  • Nucleosides / chemistry
  • Streptomyces / enzymology

Substances

  • Bacterial Proteins
  • Nucleosides
  • blasticidin S
  • Glucuronic Acid
  • cytosine-UDP-glucuronosyltransferase
  • Glucuronosyltransferase