Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Karl M. Erixon"'
Publikováno v:
Chem. Commun.. :960-962
Replacement of the thiazolium ring of thiamine pyrophosphate with a triazole gives extremely potent inhibitors of pyruvate decarboxylase from Z. mobilis, with K(I) values down to 20 pM; this system was used to explore pyrophosphate mimics and several
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5361b61ab3c0ed83cd707017e694f3c5
https://doi.org/10.1039/b615861g
https://doi.org/10.1039/b615861g
Autor:
Piotr Neumann, Finian J. Leeper, Ronald Kluger, Karl M. Erixon, Stefan Lüdtke, Ralf Ficner, Kai Tittmann
Publikováno v:
Nature chemistry. 5(9)
It is recognized widely that enzymes promote reactions by providing a pathway that proceeds through a transition state of lower energy. In principle, further rate enhancements could be achieved if intermediates are prevented from relaxing to their lo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f46bf8c67adf8f798b728c9ae9e1beb0
https://pubmed.ncbi.nlm.nih.gov/23965678
https://pubmed.ncbi.nlm.nih.gov/23965678
Publikováno v:
Biochemistry
Pyruvate decarboxylase (PDC) uses thiamine diphosphate as an essential cofactor to catalyze the formation of acetaldehyde on the pathway of ethanol synthesis. Here we report the crystallographic image of a prereaction intermediate of a bacterial pyru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::724de999cf92e9d0751fd23a1d5e082b
https://pubmed.ncbi.nlm.nih.gov/20099870
https://pubmed.ncbi.nlm.nih.gov/20099870
Publikováno v:
Organicbiomolecular chemistry. 6(19)
Novel triazole-based pyrophosphate analogues of thiamine pyrophosphate (TPP) have been synthesised and tested for inhibition of pyruvate decarboxylase (PDC) from Zymomonas mobilis. The thiazolium ring of thiamine was replaced by a triazole in an effi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08de13472a1044e423746b7172df91c4
https://pubmed.ncbi.nlm.nih.gov/19082157
https://pubmed.ncbi.nlm.nih.gov/19082157
Autor:
Finian J. Leeper, Elena Cressina, Kwasi Agyei-Owusu, Alison G. Smith, Chris Abell, Karl M. Erixon, Liuhong Chen, Jason Micklefield, Neil Dixon
Publikováno v:
Organic & Biomolecular Chemistry. 10:5924
The Escherichia coli thiM riboswitch forms specific contacts with its natural ligand, thiamine pyrophosphate (TPP or thiamine diphosphate), allowing it to generate not only nanomolar binding affinity, but also a high degree of discrimination against
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da298b1d33874eee96b08f1cef2c41cd
https://doi.org/10.1039/c2ob07116a
https://doi.org/10.1039/c2ob07116a
Publikováno v:
Chemical Communications; Feb2007, Vol. 2007 Issue 9, p960-962, 3p