English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
 Local TagsRelease HistoryDetailsSummary
  Characterizing active site conformational heterogeneity along the trajectory of an enzymatic phosphoryl transfer reaction

Zeymer, C., Werbeck, N. D., Zimmermann, S., Reinstein, J., & Hansen, D. F. (2016). Characterizing active site conformational heterogeneity along the trajectory of an enzymatic phosphoryl transfer reaction. Angewandte Chemie International Edition, 55(38), 11533-11537. doi:10.1002/anie.201606238.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-1F73-9 Version Permalink: https://hdl.handle.net/21.11116/0000-000A-1E58-3
Genre: Journal Article

Files

show Files
hide Files
:
AngewChemIntEd_55_2016_11533.pdf (Any fulltext), 3MB
 
File Permalink:
-
Name:
AngewChemIntEd_55_2016_11533.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
AngewChemIntEd_55_2016_11533_Suppl.pdf (Supplementary material), 2MB
 
File Permalink:
-
Name:
AngewChemIntEd_55_2016_11533_Suppl.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://onlinelibrary.wiley.com/doi/10.1002/anie.201606238/epdf (Any fulltext)
Description:
-
OA-Status:
Locator:
https://dx.doi.org/10.1002/anie.201606238 (Any fulltext)
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Zeymer, Cathleen1, Author           
Werbeck, Nicolas D., Author
Zimmermann, Sabine1, Author           
Reinstein, Jochen1, Author           
Hansen, D. Flemming, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: -
 Abstract: States along the phosphoryl transfer reaction catalyzed by the nucleoside monophosphate kinase UmpK were captured and changes in the conformational heterogeneity of conserved active site arginine side-chains were quantified by NMR spin-relaxation methods. In addition to apo and ligand-bound UmpK, a transition state analog (TSA) complex was utilized to evaluate the extent to which active site conformational entropy contributes to the transition state free energy. The catalytically essential arginine side-chain guanidino groups were found to be remarkably rigid in the TSA complex, indicating that the enzyme has evolved to restrict the conformational freedom along its reaction path over the energy landscape, which in turn allows the phosphoryl transfer to occur selectively by avoiding side reactions.

Details

show
hide
Language(s): eng - English
 Dates: 2016-06-272016-08-182016-08-182016-09-12
 Publication Status: Issued
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201606238
URI: https://www.ncbi.nlm.nih.gov/pubmed/27534930
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Angewandte Chemie International Edition
  Other : Angew. Chem., Int. Ed.
  Other : Angew. Chem. Int. Ed.
  Other : Angewandte Chemie, International Edition
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 55 (38) Sequence Number: - Start / End Page: 11533 - 11537 Identifier: ISSN: 1433-7851
CoNE: https://pure.mpg.de/cone/journals/resource/1433-7851