University of Oulu

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,

Enzymes of the crotonase superfamily : diverse assembly and diverse function

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Author: Dalwani, Subhadra1; Wierenga, Rik K.1
Organizations: 1Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, FI-90014, Finland
Format: article
Version: published version
Access: open
Online Access: PDF Full Text (PDF, 1.5 MB)
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Language: English
Published: Elsevier, 2023
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.

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Series: Current opinion in structural biology
ISSN: 0959-440X
ISSN-E: 1879-033X
ISSN-L: 0959-440X
Volume: 82
Article number: 102671
DOI: 10.1016/
Type of Publication: A2 Review article in a scientific journal
Field of Science: 1182 Biochemistry, cell and molecular biology
Funding: This research was funded by the Academy of Finland, grant 339894.
Academy of Finland Grant Number: 339894
Detailed Information: 339894 (Academy of Finland Funding decision)
Copyright information: © 2023 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (