Show simple item record

dc.contributor.authorLohans, C.T.*
dc.contributor.authorWang, D.Y.*
dc.contributor.authorWang, J.*
dc.contributor.authorHamed, Refaat B.*
dc.contributor.authorSchofield, C.J.*
dc.date.accessioned2019-05-03T13:00:46Z
dc.date.available2019-05-03T13:00:46Z
dc.date.issued2017-08-14
dc.identifier.citationLohans CT, Wang DY, Wang J et al (2017) Crotonases: Nature’s exceedingly convertible catalysts. ACS Catalysis. 7(10): 6587-6599.en_US
dc.identifier.urihttp://hdl.handle.net/10454/17010
dc.descriptionYesen_US
dc.description.abstractThe crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Many crotonases employ oxyanion hole-mediated stabilization of intermediates to catalyze the reaction of coenzyme A (CoA) thioester substrates (e.g., malonyl-CoA, α,β-unsaturated CoA esters) both with nucleophiles and, in the case of enolate intermediates, with varied electrophiles. Reactions of crotonases that proceed via a stabilized oxyanion intermediate include the hydrolysis of substrates including proteins, as well as hydration, isomerization, nucleophilic aromatic substitution, Claisen-type, and cofactor-independent oxidation reactions. The crotonases have a conserved fold formed from a central β-sheet core surrounded by α-helices, which typically oligomerizes to form a trimer or dimer of trimers. The presence of a common structural platform and mechanisms involving intermediates with diverse reactivity implies that crotonases have considerable potential for biocatalysis and synthetic biology, as supported by pioneering protein engineering studies on them. In this Perspective, we give an overview of crotonase diversity and structural biology and then illustrate the scope of crotonase catalysis and potential for biocatalysis.en_US
dc.description.sponsorshipBiotechnology and Biological Sciences Research Council, the Medical Research Council, and the Wellcome Trusten_US
dc.language.isoenen_US
dc.relation.isreferencedbyhttps://doi.org/10.1021/acscatal.7b01699en_US
dc.rights(c) 2017 ACS. This is the author accepted manuscript following peer-review version of the article. The final version is available online from ACS at: https://doi.org/10.1021/acscatal.7b01699.en_US
dc.subjectBiocatalysisen_US
dc.subjectCoenzyme Aen_US
dc.subjectCrotonasesen_US
dc.subjectEnolate intermediateen_US
dc.subjectHydrolaseen_US
dc.subjectOxyanion holeen_US
dc.subjectOxygenaseen_US
dc.subjectProteaseen_US
dc.subjectProtein engineeringen_US
dc.titleCrotonases: Nature’s exceedingly convertible catalystsen_US
dc.status.refereedYesen_US
dc.date.Accepted2017-08-14
dc.typeArticleen_US
dc.type.versionAccepted manuscripten_US
refterms.dateFOA2019-05-03T13:00:46Z


Item file(s)

Thumbnail
Name:
lohans_et_al_2017.pdf
Size:
18.37Mb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record