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Exploring a Streptomyces wax synthase using acyl-SNACs as donor substrates

The demand of fragrance and food industries for short/branched wax esters is increasing due to their rich scent and low toxicity. Wax synthase and acyl-CoA:diacylglycerol O-acyltransferase (WS/DGAT) are a family of bacterial enzymes capable of catalysing the production of wax esters. Here, we report...

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Detalles Bibliográficos
Autores principales: Casolari, Federica, Alrashdi, Saad, Carr, Reuben, Deng, Hai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: RSC 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10549239/
https://www.ncbi.nlm.nih.gov/pubmed/37799584
http://dx.doi.org/10.1039/d3cb00107e
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author Casolari, Federica
Alrashdi, Saad
Carr, Reuben
Deng, Hai
author_facet Casolari, Federica
Alrashdi, Saad
Carr, Reuben
Deng, Hai
author_sort Casolari, Federica
collection PubMed
description The demand of fragrance and food industries for short/branched wax esters is increasing due to their rich scent and low toxicity. Wax synthase and acyl-CoA:diacylglycerol O-acyltransferase (WS/DGAT) are a family of bacterial enzymes capable of catalysing the production of wax esters. Here, we report that a WS/DGAT from Streptomyces coelicolor is able to mediate the reactions between alcohol acceptors and synthetic acyl-donor mimics, acyl-SNACs. The enzyme displayed considerable substrate tolerance towards acyl-donors with structural diversity. Structural modelling-guided site directed mutagenesis resulted in a variant, L25F, the catalytic efficiency of which was improved toward aromatic, short-linear, and branched acyl-donors compared to the wild type.
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spelling pubmed-105492392023-10-05 Exploring a Streptomyces wax synthase using acyl-SNACs as donor substrates Casolari, Federica Alrashdi, Saad Carr, Reuben Deng, Hai RSC Chem Biol Chemistry The demand of fragrance and food industries for short/branched wax esters is increasing due to their rich scent and low toxicity. Wax synthase and acyl-CoA:diacylglycerol O-acyltransferase (WS/DGAT) are a family of bacterial enzymes capable of catalysing the production of wax esters. Here, we report that a WS/DGAT from Streptomyces coelicolor is able to mediate the reactions between alcohol acceptors and synthetic acyl-donor mimics, acyl-SNACs. The enzyme displayed considerable substrate tolerance towards acyl-donors with structural diversity. Structural modelling-guided site directed mutagenesis resulted in a variant, L25F, the catalytic efficiency of which was improved toward aromatic, short-linear, and branched acyl-donors compared to the wild type. RSC 2023-08-14 /pmc/articles/PMC10549239/ /pubmed/37799584 http://dx.doi.org/10.1039/d3cb00107e Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Casolari, Federica
Alrashdi, Saad
Carr, Reuben
Deng, Hai
Exploring a Streptomyces wax synthase using acyl-SNACs as donor substrates
title Exploring a Streptomyces wax synthase using acyl-SNACs as donor substrates
title_full Exploring a Streptomyces wax synthase using acyl-SNACs as donor substrates
title_fullStr Exploring a Streptomyces wax synthase using acyl-SNACs as donor substrates
title_full_unstemmed Exploring a Streptomyces wax synthase using acyl-SNACs as donor substrates
title_short Exploring a Streptomyces wax synthase using acyl-SNACs as donor substrates
title_sort exploring a streptomyces wax synthase using acyl-snacs as donor substrates
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10549239/
https://www.ncbi.nlm.nih.gov/pubmed/37799584
http://dx.doi.org/10.1039/d3cb00107e
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