Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme
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 substrate oxidations coupled to the reduction of H...
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Nature Portfolio
2017
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oai:doaj.org-article:872155373e0341fa822353dc3be89d1d2021-12-02T14:42:20ZConstruction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme10.1038/s41467-017-00541-42041-1723https://doaj.org/article/872155373e0341fa822353dc3be89d1d2017-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00541-4https://doaj.org/toc/2041-1723Catalytic 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 substrate oxidations coupled to the reduction of H2O2.Daniel W. WatkinsJonathan M. X. JenkinsKatie J. GraysonNicola WoodJack W. SteventonKristian K. Le VayMatthew I. GoodwinAnna S. MullenHenry J. BaileyMatthew P. CrumpFraser MacMillanAdrian J. MulhollandGus CameronRichard B. SessionsStephen MannJ. L. Ross AndersonNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-9 (2017) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q 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 Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme |
| description |
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 substrate oxidations coupled to the reduction of H2O2. |
| format |
article |
| author |
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 |
| author_facet |
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 |
| author_sort |
Daniel W. Watkins |
| title |
Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme |
| title_short |
Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme |
| title_full |
Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme |
| title_fullStr |
Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme |
| title_full_unstemmed |
Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme |
| title_sort |
construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme |
| publisher |
Nature Portfolio |
| publishDate |
2017 |
| url |
https://doaj.org/article/872155373e0341fa822353dc3be89d1d |
| work_keys_str_mv |
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1718389698911535104 |