Ontology highlight
ABSTRACT:
PROVIDER: PRJNA579878 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR10353325_1.fastq.gz | Fastqsanger.gz | |||
| SRR10353325_2.fastq.gz | Fastqsanger.gz | |||
| SRR10353326_1.fastq.gz | Fastqsanger.gz | |||
| SRR10353326_2.fastq.gz | Fastqsanger.gz |
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Project description:Medium- and branched-chain diols and amino alcohols are important industrial solvents, polymer building blocks, cosmetics and pharmaceutical ingredients, yet biosynthetically challenging to produce. Here, we present a novel approach utilising a modular polyketide synthase (PKS) platform for the efficient production of these compounds. This platform takes advantage of a versatile loading module from the rimocidin PKS and NADPH-dependent terminal thioreductases (TRs), previously untapped in engineered PKSs. Reduction of the terminal aldehyde with specific alcohol dehydrogenases enables production of diols, oxidation enables production of hydroxy acids, and transamination with specific transaminases enables production of various amino alcohols. Furthermore, replacement of the malonyl-coenzyme A (CoA)–specific acyltransferase (AT) in the extension module with methyl- or ethylmalonyl-CoA–specific ATs enables production of branched-chain diols and amino alcohols. In total, we demonstrated production of nine 1,3-diols (including the difficult-to-produce insect repellent and cosmetic ingredient 2-ethyl-1,3-hexanediol), six amino alcohols, and two carboxylic acids using our PKS platform in Streptomyces albus. Finally, tuning production of the PKS acyl-CoA substrates enabled production of high titers of specific diols and amino alcohols (1 g/L diol titer in shake flasks), demonstrating high tunability and efficiency of the platform.
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Project description:Postoperative insulin resistance refers to the phenomenon that the body’s glucose uptake stimulated by insulin is reduced due to stress effects such as trauma or the inhibitory effect of insulin on liver glucose output is weakened after surgery.
There is a clear link between postoperative insulin resistance and poor perioperative prognosis. Therefore, exploring interventions to reduce postoperative stress insulin resistance, stabilize postoperative blood glucose, and reduce postoperative complications are clinical problems that need to be solved urgently. In recent years, research on branched-chain amino acids and metabolic diseases has become a hot spot. Studies have found that in the rat model, preoperatively given a high branched-chain amino acid diet can inhibit postoperative insulin resistance and stabilize blood glucose levels. This research plan is to try to add branched-chain amino acids before surgery to observe the occurrence of postoperative insulin resistance in patients.
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Project description:Modular polyketide synthases (PKSs) have been proposed as promising megasynthases for retrobiosynthesis because of their fitness for rational carbon skeleton design. However, over the last three decades, all engineered PKSs produce carboxylic acids via terminal thioesterase (TE), which significantly narrows available chemical scope. We proposed the possibility of expanding PKS chemical diversity via terminal thioreductase (TR) engineering, and comprehensively characterised PKS TRs as NADPH-dependent enzymes to terminate polyketides with aldehyde. These aldehyde products can be readily converted to industrially valuable alcohols and amines, demonstrated by an engineered rimocidin PKS-TR producing 1,3-butanediol, 1,3-pentanediol, and 1,3-hexanediol with a total titer of 1008 mg/L in Streptomyces albus, or producing 554 mg/L 1-amino-3-alcohols via post-PKS transamination, both in shake flasks. Furthermore, efficient control of the product profile was achieved by coenzyme A (CoA) substrate regulation, as elevating butyryl-CoA level resulted in 1,3-hexanediol product ratio increased from 11% to 77%. We also demonstrated that PKS-TR can produce biosynthetically challenging branched-chain diols, culminating in production of 166 mg/L branched-chain 2-methyl-1,3-diols via acyltransferase exchange.
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