Docking domain-mediated subunit interactions in natural product megasynth(et)ases

Polyketide synthase (PKS) and non-ribosomal peptide synthetase (NRPS) multienzymes produce numerous high value metabolites. The protein subunits which constitute these megasynth(et)ases must undergo ordered self-assembly to ensure correct organisation of catalytic domains for the biosynthesis of a g...

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Autores principales: Smith, Helen G, Beech, Matthew J, Lewandowski, Józef R, Challis, Gregory L, Jenner, Matthew
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2021
Materias:
Natural Products
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9113145/
https://www.ncbi.nlm.nih.gov/pubmed/33640957
http://dx.doi.org/10.1093/jimb/kuab018
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author Smith, Helen G
Beech, Matthew J
Lewandowski, Józef R
Challis, Gregory L
Jenner, Matthew
author_facet Smith, Helen G
Beech, Matthew J
Lewandowski, Józef R
Challis, Gregory L
Jenner, Matthew
author_sort Smith, Helen G
collection PubMed
description Polyketide synthase (PKS) and non-ribosomal peptide synthetase (NRPS) multienzymes produce numerous high value metabolites. The protein subunits which constitute these megasynth(et)ases must undergo ordered self-assembly to ensure correct organisation of catalytic domains for the biosynthesis of a given natural product. Short amino acid regions at the N- and C-termini of each subunit, termed docking domains (DDs), often occur in complementary pairs, which interact to facilitate substrate transfer and maintain pathway fidelity. This review details all structurally characterised examples of NRPS and PKS DDs to date and summarises efforts to utilise DDs for the engineering of biosynthetic pathways.
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spelling pubmed-91131452022-06-08 Docking domain-mediated subunit interactions in natural product megasynth(et)ases Smith, Helen G Beech, Matthew J Lewandowski, Józef R Challis, Gregory L Jenner, Matthew J Ind Microbiol Biotechnol Natural Products Polyketide synthase (PKS) and non-ribosomal peptide synthetase (NRPS) multienzymes produce numerous high value metabolites. The protein subunits which constitute these megasynth(et)ases must undergo ordered self-assembly to ensure correct organisation of catalytic domains for the biosynthesis of a given natural product. Short amino acid regions at the N- and C-termini of each subunit, termed docking domains (DDs), often occur in complementary pairs, which interact to facilitate substrate transfer and maintain pathway fidelity. This review details all structurally characterised examples of NRPS and PKS DDs to date and summarises efforts to utilise DDs for the engineering of biosynthetic pathways. Oxford University Press 2021-02-26 /pmc/articles/PMC9113145/ /pubmed/33640957 http://dx.doi.org/10.1093/jimb/kuab018 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of Society of Industrial Microbiology and Biotechnology. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Natural Products
Smith, Helen G
Beech, Matthew J
Lewandowski, Józef R
Challis, Gregory L
Jenner, Matthew
Docking domain-mediated subunit interactions in natural product megasynth(et)ases
title Docking domain-mediated subunit interactions in natural product megasynth(et)ases
title_full Docking domain-mediated subunit interactions in natural product megasynth(et)ases
title_fullStr Docking domain-mediated subunit interactions in natural product megasynth(et)ases
title_full_unstemmed Docking domain-mediated subunit interactions in natural product megasynth(et)ases
title_short Docking domain-mediated subunit interactions in natural product megasynth(et)ases
title_sort docking domain-mediated subunit interactions in natural product megasynth(et)ases
topic Natural Products
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9113145/
https://www.ncbi.nlm.nih.gov/pubmed/33640957
http://dx.doi.org/10.1093/jimb/kuab018
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AT challisgregoryl dockingdomainmediatedsubunitinteractionsinnaturalproductmegasynthetases
AT jennermatthew dockingdomainmediatedsubunitinteractionsinnaturalproductmegasynthetases

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