Enzymes of the crotonase superfamily : diverse assembly and diverse function
Dalwani, Subhadra; Wierenga, Rik K. (2023-08-04)
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
© 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/).
https://creativecommons.org/licenses/by/4.0/
https://urn.fi/URN:NBN:fi-fe20231109143683
Tiivistelmä
Abstract
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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