Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase sgtam

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Montavon, T. J.
  • Christianson, C. V.
  • Festin, G. M.
  • Shen, Ben
  • Bruner, S. D.

publication date

  • May 2008

journal

  • Bioorganic & Medicinal Chemistry Letters  Journal

abstract

  • The synthesis and evaluation of two classes of inhibitors for SgTAM, a 4-methylideneimidazole-5-one (MIO) containing tyrosine aminomutase, are described. A mechanism-based strategy was used to design analogs that mimic the substrate or product of the reaction and form covalent interactions with the enzyme through the MIO prosthetic group. The analogs were characterized by measuring inhibition constants and X-ray crystallographic structural analysis of the co-complexes bound to the aminomutase, SgTAM.

subject areas

  • Crystallography, X-Ray
  • Drug Design
  • Enzyme Inhibitors
  • Epoxy Compounds
  • Imidazoles
  • Intramolecular Transferases
  • Molecular Structure
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0960-894X

Digital Object Identifier (DOI)

  • 10.1016/j.bmcl.2007.11.046

PubMed ID

  • 18078753
scroll to property group menus

Additional Document Info

start page

  • 3099

end page

  • 3102

volume

  • 18

issue

  • 10

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support