Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism. Issue 72 (11th August 2020)
- Record Type:
- Journal Article
- Title:
- Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism. Issue 72 (11th August 2020)
- Main Title:
- Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism
- Authors:
- Chang, Yu-Yung
Hagawa, Sora
Hsu, Chun-Hua - Abstract:
- Abstract : Two is better than one: thermophilic N α-acetyltransferase SsArd1 develops a strategy to adapt to higher temperatures for water-mediated catalysis. Abstract : The common mechanism of N -acetyltransferases (NATs) is a water-mediated catalysis, which is not conducive to thermophilic acetyltransferases. The crystal structure of SsArd1 shows an ordered catalytic water molecule in a trap formed by the residues H88 and E127. Structure-guided mutagenesis, kinetic studies and MD simulation indicated that the turnover rates of H88A, E127A and H88A/E127A mutants were low, but that of the H88E/E127H mutant could be restored to the level of the wild type.
- Is Part Of:
- Chemical communications. Volume 56:Issue 72(2020)
- Journal:
- Chemical communications
- Issue:
- Volume 56:Issue 72(2020)
- Issue Display:
- Volume 56, Issue 72 (2020)
- Year:
- 2020
- Volume:
- 56
- Issue:
- 72
- Issue Sort Value:
- 2020-0056-0072-0000
- Page Start:
- 10537
- Page End:
- 10540
- Publication Date:
- 2020-08-11
- Subjects:
- Chemistry -- Periodicals
540 - Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/cc ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d0cc04305b ↗
- Languages:
- English
- ISSNs:
- 1359-7345
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3139.350000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 14252.xml