Iterative Methylations Resulting in the Biosynthesis of the t-Butyl Group Catalyzed by a B12-Dependent Radical SAM Enzyme in Cystobactamid Biosynthesis. Chapter

abstract

• B12-dependent radical SAM enzymes that can perform methylations on sp3 carbon centers are important for functional diversity and regulation of biological activity in several nonribosomal peptides. Detailed studies on these enzymes are hindered by the complexity of the substrates and low levels of expression of active enzymes. CysS can catalyze iterative methylations of a methoxybenzene moiety during the biosynthesis of the cystobactamids. Here, we describe the overexpression, purification, substrate identification, and mechanism of this enzyme.

authors

• Begley, Tadhg

altmetric score

• 1

author list (cited authors)

• Wang, Y., Schnell, B., Mller, R., & Begley, T. P.

citation count

• 9

complete list of authors

• Wang, Yuanyou||Schnell, Bastien||Müller, Rolf||Begley, Tadhg P

Book Title

• RADICAL SAM ENZYMES

publication date

• January 2018

publisher

• Elsevier  Publisher

published in

• METHODS IN ENZYMOLOGY  Journal

keywords

• Anisoles
• B(12)-dependent Radical Sam Methyltransferase
• Bacterial Proteins
• Biocatalysis
• Biosynthetic Pathways
• Cyss
• Cystobactamid
• Enzyme Assays
• Esters
• Free Radicals
• Iterative Radical Methylation
• Mechanism
• Methylation
• Methyltransferases
• Myxococcales
• Nitro Compounds
• Recombinant Proteins
• Reconstitution
• S-adenosylmethionine
• Tert-butyl
• Vitamin B 12

PubMed Central ID

• 30097093

Digital Object Identifier (DOI)

• 10.1016/bs.mie.2018.05.018

International Standard Book Number (ISBN) 13

• 9780128127940

start page

• 199

end page

• 216

volume

• 606

URL

• http://dx.doi.org/10.1016/bs.mie.2018.05.018