Substrate specificity of plant nitrilase complexes is affected by their helical twist

  • Nitrilases are oligomeric, helix-forming enzymes from plants, fungi and bacteria that are involved in the metabolism of various natural and artificial nitriles. These biotechnologically important enzymes are often specific for certain substrates, but directed attempts at modifying their substrate specificities by exchanging binding pocket residues have been largely unsuccessful. Thus, the basis for their selectivity is still unknown. Here we show, based on work with two highly similar nitrilases from the plant \(\textit {Capsella rubella}\), that modifying nitrilase helical twist, either by exchanging an interface residue or by imposing a different twist, without altering any binding pocket residues, changes substrate preference. We reveal that helical twist and substrate size correlate and when binding pocket residues are exchanged between two nitrilases that show the same twist but different specificities, their specificities change. Based on these findings we propose that helical twist influences the overall size of the binding pocket.

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Metadaten
Author:Jeremy D. WoodwardGND, Inga TrompetterGND, Trevor SewellGND, Markus PiotrowskiORCiDGND
URN:urn:nbn:de:hbz:294-64414
DOI:https://doi.org/10.1038/s42003-018-0186-4
Parent Title (English):Communications biology
Document Type:Article
Language:English
Date of Publication (online):2019/05/20
Date of first Publication:2018/11/02
Publishing Institution:Ruhr-Universität Bochum, Universitätsbibliothek
Tag:Open Access Fonds
Electron microscopy; Hydrolases; Natural variation in plants
Volume:1
First Page:186-1
Last Page:186-10
Note:
Communications biology, Bd. 1.2018, Artikelnummer 186
Note:
Article Processing Charge funded by the Deutsche Forschungsgemeinschaft (DFG) and the Open Access Publication Fund of Ruhr-Universität Bochum.
Institutes/Facilities:Lehrstuhl für Pflanzenphysiologie, Arbeitsgruppe Pflanzliche Zellphysiologie und Molekularbiologie
Dewey Decimal Classification:Naturwissenschaften und Mathematik / Biowissenschaften, Biologie, Biochemie
open_access (DINI-Set):open_access
faculties:Fakultät für Biologie und Biotechnologie
Licence (English):License LogoCreative Commons - CC BY 4.0 - Attribution 4.0 International