Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Nicola J Blackmore"'
Publikováno v:
PLoS ONE, Vol 12, Iss 6, p e0180052 (2017)
The first enzyme of the shikimate pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS), adopts a range of distinct allosteric regulation mechanisms in different organisms, related to different quaternary assemblies. DAH7PS from Myco
Externí odkaz:
https://doaj.org/article/93f98f379d744f8892b1f92d772dbbc2
Publikováno v:
PLoS ONE, Vol 11, Iss 4, p e0152723 (2016)
Chirality plays a major role in recognition and interaction of biologically important molecules. The enzyme 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase (DAH7PS) is the first enzyme of the shikimate pathway, which is responsible for the synth
Externí odkaz:
https://doaj.org/article/d658f69c05514076b876cf40606e920d
Publikováno v:
Journal of Biological Chemistry. 295:6252-6262
Allostery exploits the conformational dynamics of enzymes by triggering a shift in population ensembles toward functionally distinct conformational or dynamic states. Allostery extensively regulates the activities of key enzymes within biosynthetic p
Publikováno v:
J Biol Chem
Allostery exploits the conformational dynamics of enzymes by triggering a shift in population ensembles toward functionally distinct conformational or dynamic states. Allostery extensively regulates the activities of key enzymes within biosynthetic p
Autor:
Melissa N. Webby, Ali Reza Nazmi, Emily J. Parker, Nicola J. Blackmore, Geoffrey B. Jameson, Richard D. Hutton, Edward N. Baker
Publikováno v:
Journal of Biological Chemistry. 290:18187-18198
Allostery, where remote ligand binding alters protein function, is essential for the control of metabolism. Here, we have identified a highly sophisticated allosteric response that allows complex control of the pathway for aromatic amino acid biosynt
Publikováno v:
PLoS ONE
PLoS ONE, Vol 12, Iss 6, p e0180052 (2017)
PLoS ONE, Vol 12, Iss 6, p e0180052 (2017)
The first enzyme of the shikimate pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS), adopts a range of distinct allosteric regulation mechanisms in different organisms, related to different quaternary assemblies. DAH7PS from Myco
Publikováno v:
PLoS ONE
PLoS ONE, Vol 11, Iss 4, p e0152723 (2016)
PLoS ONE, Vol 11, Iss 4, p e0152723 (2016)
Chirality plays a major role in recognition and interaction of biologically important molecules. The enzyme 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase (DAH7PS) is the first enzyme of the shikimate pathway, which is responsible for the synth
Autor:
Richard D. Hutton, Celia J. Webby, Geoffrey B. Jameson, Nicola J. Blackmore, Emily J. Parker, Edward N. Baker, Heather M. Baker, Wanting Jiao
Publikováno v:
Journal of Biological Chemistry. 285:30567-30576
The shikimate pathway, responsible for aromatic amino acid biosynthesis, is required for the growth of Mycobacterium tuberculosis and is a potential drug target. The first reaction is catalyzed by 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase
Autor:
Nicola J, Blackmore, Ali Reza, Nazmi, Richard D, Hutton, Melissa N, Webby, Edward N, Baker, Geoffrey B, Jameson, Emily J, Parker
Publikováno v:
The Journal of biological chemistry. 290(29)
Allostery, where remote ligand binding alters protein function, is essential for the control of metabolism. Here, we have identified a highly sophisticated allosteric response that allows complex control of the pathway for aromatic amino acid biosynt
Autor:
Wanting Jiao, Geoffrey B. Jameson, Edward N. Baker, Richard D. Hutton, Nicola J. Blackmore, Sebastian Reichau, Emily J. Parker
Publikováno v:
Journal of molecular biology. 425(9)
3-Deoxy-d-arabino-heptulosonate 7-phosphate synthase (DAH7PS) catalyzes the first step in the shikimate pathway, the pathway responsible for the biosynthesis of the aromatic amino acids Trp, Phe, and Tyr. Unlike many other organisms that produce up t