Works (1)
Updated: July 11th, 2023 20:10
2006 journal article
Proximal cavity, distal histidine, and substrate hydrogen-bonding mutations modulate the activity of Amphitrite ornata dehaloperoxidase
BIOCHEMISTRY, 45(30), 9085–9094.
MeSH headings : Animals; Binding Sites / genetics; Hemoglobins; Histidine / chemistry; Histidine / genetics; Hydrogen Bonding; Mutagenesis, Site-Directed; Peroxidases / chemistry; Peroxidases / genetics; Peroxidases / metabolism; Phenylalanine / genetics; Polychaeta / enzymology; Polychaeta / genetics; Substrate Specificity / genetics; Tyrosine / genetics; Valine / genetics
TL;DR:
The role of tyrosine 38 (Y38), which hydrogen bonds to the hydroxyl group of the substrate, was probed and it was suggested that abolishing this hydrogen bond may open a pathway for the escape of the one-electron product, the phenoxy radical leading to polymeric products.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
14. Life Below Water
(OpenAlex)
Sources: Web Of Science, ORCID
Added: August 6, 2018
Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.
Certain data included herein are derived from the Web of Science© and InCites© (2024) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.
