Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Jonathan D. Tyzack"'
Autor:
Nehad Noby, Rachel L. Johnson, Jonathan D. Tyzack, Amira M. Embaby, Hesham Saeed, Ahmed Hussein, Sherine N. Khattab, Pierre J. Rizkallah, D. Dafydd Jones
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 9, p 4703 (2022)
Cold active esterases have gained great interest in several industries. The recently determined structure of a family IV cold active esterase (EstN7) from Bacillus cohnii strain N1 was used to expand its substrate range and to probe its commercially
Externí odkaz:
https://doaj.org/article/c84c2e55ae7a489fbd5916ac8cbcd1fe
Autor:
António J. M. Ribeiro, Ioannis G. Riziotis, Jonathan D. Tyzack, Neera Borkakoti, Janet M. Thornton
Publikováno v:
Biophysical Reviews. 14:1273-1280
Enzyme reactions take place in the active site through a series of catalytic steps, which are collectively termed the enzyme mechanism. The catalytic step is thereby the individual unit to consider for the purposes of building new enzyme mechanisms
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13a83832075e262de30ee1e70b5714f2
https://doi.org/10.1007/s12551-022-01022-9
https://doi.org/10.1007/s12551-022-01022-9
Autor:
Antonio J. M. Ribeiro, Ioannis G. Riziotis, Jonathan D. Tyzack, Neera Borkakoti, Janet M. Thornton
A rich literature dedicated to understanding the reaction mechanisms of hundreds of enzymes has emerged over time from the works of experimental and computational researchers. This body of information can now be the starting point for an entirely nov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::611933cdc7fa6c733a9a5764113dd611
https://doi.org/10.1101/2022.09.05.506575
https://doi.org/10.1101/2022.09.05.506575
Autor:
Janet M. Thornton, António J. M. Ribeiro, Jonathan D. Tyzack, Neera Borkakoti, Gemma L. Holliday
Publikováno v:
Journal of Biological Chemistry. 295:314-324
The catalytic residues of an enzyme comprise the amino acids located in the active center responsible for accelerating the enzyme-catalyzed reaction. These residues lower the activation energy of reactions by performing several catalytic functions. D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3241124be47c85a01bac317a9d7e09a
https://doi.org/10.1074/jbc.rev119.006289
https://doi.org/10.1074/jbc.rev119.006289
Autor:
Jonathan D Tyzack
Publikováno v:
Reference Module in Biomedical Sciences
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::82862be2e118118344bcd6282075151a
https://doi.org/10.1016/b978-0-12-820472-6.00067-0
https://doi.org/10.1016/b978-0-12-820472-6.00067-0
Publikováno v:
The FEBS Journal. 287:4128-4140
Pseudoenzymes are proteins that are evolutionary related to enzymes but lack relevant catalytic activity. They are usually evolved from enzymatic ancestors that have lost their catalytic activities. The loss of catalytic function is one extreme among
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5af58df82809a814278975aa1f88ad70
https://doi.org/10.1111/febs.15142
https://doi.org/10.1111/febs.15142
Autor:
Joseph Onwubiko, Lukáš Pravda, António J. M. Ribeiro, Andrew R. Leach, Venkatesh Muthukrishnan, Rossana Zaru, Maria Jesus Martin, Sameer Velanker, Keeva Cochrane, Jonathan D. Tyzack, Janet M. Thornton, Claire O'Donovan, Sandra Orchard
Publikováno v:
The FEBS journalReferences. 289(19)
Enzymes play essential roles in all life processes and are used extensively in the biomedical and biotechnological fields. However, enzyme-related information is spread across multiple resources making its retrieval time-consuming. In response to thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab3947a58f92d6e4c584481069f9779c
https://pubmed.ncbi.nlm.nih.gov/34437766
https://pubmed.ncbi.nlm.nih.gov/34437766
Publikováno v:
ACS Synthetic Biology. 8:2494-2506
Transform-MinER (Transforming Molecules in Enzyme Reactions) is a web application facilitating the exploration of chemical biosynthetic space, guiding the user toward promising start points for enzyme design projects or directed evolution experiments
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e38be359be000e5526f4ea86f69793fc
https://doi.org/10.1021/acssynbio.9b00105
https://doi.org/10.1021/acssynbio.9b00105
Autor:
Harry Jubb, Aleksandras Gutmanas, Radka Svobodová, Stephen Anyango, Sreenath Nair, Manjeet Kumar, Jonathan D. Tyzack, Leandro G Radusky, Toby J. Gibson, Liang-Chin Huang, Luis Serrano, Eloy Villasclaras Fernandez, Sameer Velankar, Petr Škoda, Michael J.E. Sternberg, Mark N. Wass, Fábio Madeira, Christine A. Orengo, Rishabh Jain, Stuart A. MacGowan, Patrizio Di Micco, Sayoni Das, Emmanuel D. Levy, Natarajan Kannan, John M. Berrisford, Tom L. Blundell, Janet M. Thornton, Radoslav Krivak, Christos C. Kannas, Lukáš Pravda, Bissan Al-Lazikani, Jose M. Dana, Abhik Mukhopadhyay, David R. Armstrong, Saqib Mir, Mihaly Varadi, Franca Fraternali, Karel Berka, Mallur S. Madhusudhan, Jake E McGreig, Mandar Deshpande, Neera Borkakoti, Luca Parca, António J. M. Ribeiro, Ian Sillitoe, Henry J Martell, Manuela Helmer-Citterich, Sucharita Dey, David Hoksza, Gulzar Singh, Jaroslav Koča, Typhaine Paysan-Lafosse, Geoffrey J. Barton, Alfonso Valencia, Wim F. Vranken
Publikováno v:
Nucleic Acids Research
D353
D344
D353
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The Protein Data Bank in Europe-Knowledge Base (PDBe-KB, https://pdbe-kb.org) is a community-driven, collaborative resource for literature-derived, manually curated and computationally predicted structural and functional annotations of macromolecular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa27c0dd4bcd59db90b1d8c5a0ca1042
http://europepmc.org/articles/PMC6943075
http://europepmc.org/articles/PMC6943075
Autor:
Jonathan D. Tyzack, Johannes Kirchmair
Publikováno v:
Chemical Biology and Drug Design
Chemical Biology & Drug Design
Chemical Biology & Drug Design
In this review, we present important, recent developments in the computational prediction of cytochrome P450 (CYP) metabolism in the context of drug discovery. We discuss in silico models for the various aspects of CYP metabolism prediction, includin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b779ae7fc715dc2ecc6f0edd9f0729d
https://doi.org/10.1111/cbdd.13445
https://doi.org/10.1111/cbdd.13445