Abstract
Over the past 10 years, considerable progress has been made in our understanding of the mechanistic enzymology of the Radical-SAM enzymes. It is now clear that these enzymes appear to be involved in a remarkably wide range of chemically challenging reactions. This review article highlights mechanistic and structural aspects of the methylthiotransferases (MTTases) sub-class of the Radical-SAM enzymes. The mechanism of methylthio insertion, now observed to be performed by three different enzymes is an exciting unsolved problem. This article is part of a Special Issue entitled: Radical SAM enzymes and Radical Enzymology.
Copyright © 2011 Elsevier B.V. All rights reserved.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
Amino Acid Sequence
-
Bacterial Proteins / chemistry
-
Bacterial Proteins / metabolism
-
Biocatalysis
-
Escherichia coli Proteins / chemistry
-
Escherichia coli Proteins / metabolism
-
Free Radicals / chemistry
-
Free Radicals / metabolism
-
Humans
-
Iron-Sulfur Proteins / chemistry
-
Iron-Sulfur Proteins / metabolism*
-
Methyltransferases / chemistry
-
Methyltransferases / metabolism*
-
Models, Molecular
-
Molecular Sequence Data
-
Phylogeny
-
Protein Structure, Tertiary
-
Ribosomal Proteins / chemistry
-
Ribosomal Proteins / metabolism
-
S-Adenosylmethionine / chemistry
-
S-Adenosylmethionine / metabolism*
-
Sulfurtransferases / chemistry
-
Sulfurtransferases / metabolism*
Substances
-
Bacterial Proteins
-
Escherichia coli Proteins
-
Free Radicals
-
Iron-Sulfur Proteins
-
Ribosomal Proteins
-
RpsL protein, E coli
-
S-Adenosylmethionine
-
Methyltransferases
-
Sulfurtransferases