English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Chemistry of AdoMet‐dependent methyltransferases.

Klimasauskas, S., & Lukinavicius, G. (2008). Chemistry of AdoMet‐dependent methyltransferases. Wiley Encyclopedia of Chemical Biology. doi:10.1002/9780470048672.wecb335.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0001-E4A2-6 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-E4A6-2
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Klimasauskas, S., Author
Lukinavicius, G.1, Author              
Affiliations:
1Laboratory of Chromatin Labeling and Imaging, Max Planck Institute for Biophysical Chemistry, Max Planck Society, ou_2616691              

Content

show
hide
Free keywords: -
 Abstract: S‐adenosyl‐L‐methionine is a high energy compound and is the major source of methyl groups for a myriad of biologic transmethylation reactions. These highly specific single‐carbon transfers onto diverse nucleophilic centers in biomolecules are catalyzed by methyltransferase enzymes and play important regulatory and structural roles in the cell. Here we discuss the chemical mechanism of the methylation reactions, including structural features of the methylsulfonium center in the cofactor molecule, enzyme‐assisted activation of diverse nucleophilic targets by deprotonation or covalent catalysis, and spatial constraints of the reaction.

Details

show
hide
Language(s): eng - English
 Dates: 2008-05-15
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/9780470048672.wecb335
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Wiley Encyclopedia of Chemical Biology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: -