Subhadra Dalwani, Rik K. Wierenga, Enzymes of the crotonase superfamily: Diverse assembly and diverse function, Current Opinion in Structural Biology, Volume 82, 2023, 102671, ISSN 0959-440X, https://doi.org/10.1016/j.sbi.2023.102671
Enzymes of the crotonase superfamily : diverse assembly and diverse function
|Author:||Dalwani, Subhadra1; Wierenga, Rik K.1|
1Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, FI-90014, Finland
|Online Access:||PDF Full Text (PDF, 1.5 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe20231109143683
|Publish Date:|| 2023-11-09
The crotonase fold is generated by a framework of four repeats of a ββα-unit, extended by two helical regions. The active site of crotonase superfamily (CS) enzymes is located at the N-terminal end of the helix of the third repeat, typically being covered by a C-terminal helix. A major subset of CS-enzymes catalyzes acyl-CoA-dependent reactions, allowing for a diverse range of acyl-tail modifications. Most of these enzymes occur as trimers or hexamers (dimers of trimers), but monomeric forms are also observed. A common feature of the active sites of CS-enzymes is an oxyanion hole, formed by two peptide-NH hydrogen bond donors, which stabilises the negatively charged thioester oxygen atom of the reaction intermediate. Structural properties and possible use of these enzymes for biotechnological applications are discussed.
Current opinion in structural biology
|Type of Publication:||
A2 Review article in a scientific journal
|Field of Science:||
1182 Biochemistry, cell and molecular biology
This research was funded by the Academy of Finland, grant 339894.
|Academy of Finland Grant Number:||
339894 (Academy of Finland Funding decision)
© 2023 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).