ArticleAMB Express2019
In vitro reconstitution and characterisation of the oxidative D-xylose pathway for production of organic acids and alcohols.
Article in AMB Express, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Metabolic Engineering of Komagataella phaffii and Process Optimization for Biosynthesis of 1,2,4-Butanetriol From Xylose.Biotechnology journal · 2025Article
- Co-utilization of glucose and xylose for the production of poly-β-hydroxybutyrate (PHB) by Sphingomonas sanxanigenens NX02.Microbial cell factories · 2023Article
- Structure and function of aldopentose catabolism enzymes involved in oxidative non-phosphorylative pathways.Biotechnology for biofuels and bioproducts · 2022Review
- Recent progress in the microbial production of xylonic acid.World journal of microbiology & biotechnology · 2022Review
- Three-dimensional structure of xylonolactonase from Caulobacter crescentus: A mononuclear iron enzyme of the 6-bladed β-propeller hydrolase family.Protein science : a publication of the Protein Society · 2022Article
- Xylonolactonase fromBiochemistry · 2021Article
- Characterization of highly active 2-keto-3-deoxy-L-arabinonate and 2-keto-3-deoxy-D-xylonate dehydratases in terms of the biotransformation of hemicellulose sugars to chemicals.Applied microbiology and biotechnology · 2020Article
- A combined experimental and modelling approach for the Weimberg pathway optimisation.Nature communications · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The oxidative D-xylose pathway, i.e. Dahms pathway, can be utilised to produce from cheap biomass raw material useful chemical intermediates. In vitro metabolic pathways offer a fast way to study the rate-limiting steps and find the most suitable enzymes for each reaction. We have constructed here in vitro multi-enzyme cascades leading from D-xylose or D-xylonolactone to ethylene glycol, glycolic acid and lactic acid, and use simple spectrophotometric assays for the read-out of the efficiency of these pathways. Based on our earlier results, we focussed particularly on the less studied xylonolactone ring opening (hydrolysis) reaction. The bacterial Caulobacter crescentus lactonase (Cc XylC), was shown to be a metal-dependent enzyme clearly improving the formation of D-xylonic acid at pH range from 6 to 8. The following dehydration reaction by the ILVD/EDD family D-xylonate dehydratase is a rate-limiting step in the pathway, and an effort was made to screen for novel enolase family D-xylonate dehydratases, however, no suitable replacing enzymes were found for this reaction. Concerning the oxidation of glycolaldehyde to glycolic acid, several enzyme candidates were also tested. Both Escherichia coli aldehyde dehydrogenase (Ec AldA) and Azospirillum brasilense α-ketoglutarate semialdehyde dehydrogenase (Ab AraE) proved to be suitable enzymes for this reaction.
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