Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles

Description

Yes / Studies on the substrate selectivity of recombinant ferrous-iron- and 2-oxoglutarate-dependent proline hydroxylases (PHs) reveal that they can catalyse the production of dihydroxylated 5-, 6-, and 7-membered ring products, and can accept bicyclic substrates. Ring-substituted substrate analogues (such hydroxylated and fluorinated prolines) are accepted in some cases. The results highlight the considerable, as yet largely untapped, potential for amino acid hydroxylases and other 2OG oxygenases in biocatalysis.

Links & Downloads

1. Smart TJ, Hamed RB, Claridge TDW et al (2020) Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles. Bioorganic Chemistry. 94: 103386.
2. http://hdl.handle.net/10454/17659
3. https://doi.org/10.1016/j.bioorg.2019.103386

Tags

2-Oxoglutarate oxygenases

Amino acid oxidation

Biocatalysis

L-proline

Proline hydroxylase

Additional Fields

Identifer	oai:union.ndltd.org:BRADFORD/oai:bradscholars.brad.ac.uk:10454/17659
Date	17 February 2020
Creators	Smart, T.J., Hamed, Refaat B., Claridge, T.D.W., Schofield, C.J.
Source Sets	Bradford Scholars
Language	English
Detected Language	English
Type	Article, Published version
Rights	(c) 2020 The Authors. This is an Open Access article distributed under the Creative Commons CC-BY license (https://creativecommons.org/licenses/by/4.0/)