Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Gus Cameron"'
Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme
Autor:
Daniel W. Watkins, Jonathan M. X. Jenkins, Katie J. Grayson, Nicola Wood, Jack W. Steventon, Kristian K. Le Vay, Matthew I. Goodwin, Anna S. Mullen, Henry J. Bailey, Matthew P. Crump, Fraser MacMillan, Adrian J. Mulholland, Gus Cameron, Richard B. Sessions, Stephen Mann, J. L. Ross Anderson
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017)
Catalytic mechanisms of enzymes are well understood, but achieving diverse reaction chemistries in re-engineered proteins can be difficult. Here the authors show a highly efficient and thermostable artificial enzyme that catalyzes a diverse array of
Externí odkaz:
https://doaj.org/article/872155373e0341fa822353dc3be89d1d
Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme
Autor:
J. L. Ross Anderson, Adrian J. Mulholland, Daniel W. Watkins, Jack W. Steventon, Richard B. Sessions, Henry J. Bailey, Fraser MacMillan, Jonathan M. X. Jenkins, Matthew Goodwin, Anna Mullen, Matthew P. Crump, Kristian Le Vay, Gus Cameron, Stephen Mann, Nicola Wood, Katie J. Grayson
Publikováno v:
Nature Communications
Watkins, D W, Jenkins, J M X, Grayson, K J, Wood, N, Steventon, J W, Le Vay, K, Goodwin, M I, Mullen, A S, Bailey, H J, Crump, M P, MacMillan, F, Mulholland, A J, Cameron, G, Sessions, R B, Mann, S & Anderson, J L R 2017, ' Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme ', Nature Communications, vol. 8, 358 . https://doi.org/10.1038/s41467-017-00541-4
Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017)
Watkins, D W, Jenkins, J M X, Grayson, K J, Wood, N, Steventon, J W, Le Vay, K, Goodwin, M I, Mullen, A S, Bailey, H J, Crump, M P, MacMillan, F, Mulholland, A J, Cameron, G, Sessions, R B, Mann, S & Anderson, J L R 2017, ' Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme ', Nature Communications, vol. 8, 358 . https://doi.org/10.1038/s41467-017-00541-4
Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017)
Although catalytic mechanisms in natural enzymes are well understood, achieving the diverse palette of reaction chemistries in re-engineered native proteins has proved challenging. Wholesale modification of natural enzymes is potentially compromised
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c10b296ef11faca1cd395758080bef3
https://pubmed.ncbi.nlm.nih.gov/28842561
https://pubmed.ncbi.nlm.nih.gov/28842561
Autor:
Jan Frayne, Apirat Chaikuad, Gus Cameron, Anthony R. Clarke, Wyatt W. Yue, R Al-Mokhtar, Udo Oppermann, Naeem Shafqat, R L Brady
Publikováno v:
The Biochemical journal. 435(2)
hGAPDS (human sperm-specific glyceraldehyde-3-phosphate dehydrogenase) is a glycolytic enzyme essential for the survival of spermatozoa, and constitutes a potential target for non-hormonal contraception. However, enzyme characterization of GAPDS has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d16f6b8893a544cced985e01d19d98e3
http://ora.ox.ac.uk/objects/uuid:c8fe78b2-cfa8-45ee-b4a4-847bf74ba9a8
http://ora.ox.ac.uk/objects/uuid:c8fe78b2-cfa8-45ee-b4a4-847bf74ba9a8
Sperm glyceraldehyde-3-phosphate dehydrogenase has been shown to be a successful target for a non-hormonal contraceptive approach, but the agents tested to date have had unacceptable side effects. Obtaining the structure of the sperm-specific isoform
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9f0ac4e0c65d054e953740e51852e4f
https://europepmc.org/articles/PMC2755679/
https://europepmc.org/articles/PMC2755679/
Publikováno v:
FEBS letters. 583(17)
The folding mechanism and stability of dimeric formate dehydrogenase from Candida methylica was analysed by exposure to denaturing agents and to heat. Equilibrium denaturation data yielded a dissociation constant of about 10 −13 M for assembly of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6899bf6b64352d5496f31555ec5e3e6c
https://pubmed.ncbi.nlm.nih.gov/19647736
https://pubmed.ncbi.nlm.nih.gov/19647736