ArticleBioengineered2015
Characterization of D-xylonate dehydratase YjhG from Escherichia coli.
Article in Bioengineered, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- 2-Keto-3-deoxy-D-xylonate and 2-oxo-4-hydroxybutyrate as natural and artificial effectors of transcription factors regulating D-xylonate operons in E. coli.Applied microbiology and biotechnology · 2026Article
- Enzyme and cofactor engineering to increase d-xylonate dehydratase activity for improved d-1,2,4-butanetriol production from d-xylose.Synthetic and systems biotechnology · 2025Article
- Identification of gene targets regulated by the IclR-like regulator SL1344_3500 inJournal of bacteriology · 2025Article
- Metabolic engineering for microbial production of sugar acids.BMC biotechnology · 2025Review
- Article
- Progress in research on the biosynthesis of 1,2,4-butanetriol by engineered microbes.World journal of microbiology & biotechnology · 2024Review
- Structure and function of aldopentose catabolism enzymes involved in oxidative non-phosphorylative pathways.Biotechnology for biofuels and bioproducts · 2022Review
- Engineering microbial pathways for production of bio-based chemicals from lignocellulosic sugars: current status and perspectives.Biotechnology for biofuels · 2020Review
- Engineering Escherichia coli to grow constitutively on D-xylose using the carbon-efficient Weimberg pathway.Microbiology (Reading, England) · 2018Article
- The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family.Scientific reports · 2018Article
- Synthetic pathway optimization for improved 1,2,4-butanetriol production.Journal of industrial microbiology & biotechnology · 2016Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
D-xylonate dehydratase YjhG from Escherichia coli can convert D-xylonate into 2-keto-3-deoxy- D-xylonate (KDX), and is a key enzyme in the biosynthesis of 1,2,4-butanetriol and other chemicals. However, the biochemical properties of YjhG still remain unknown. In this study, the activity assay method for YjhG was established based on semicarbazide method, in which KDX reacts with semicarbazide reagent, and is further quantified by high-resolution mass spectrometry. The effect of reaction conditions on YjhG activity was determined in vitro using purified His-tagged YjhG protein. This enzyme showed maximal activity at 30°C and pH 8.0. Bivalent metal ions such as Mg(2+) and Mn(2+) activated, whereas Ni(2+) and Zn(2+) inhibited the activity of YjhG. Under optimal conditions, the Km and Vmax values were 4.88 mM and 78.62 μM l(-1)h(-1), respectively, when using D-xylonate as a substrate. Amino acids sequence alignments and catalytic properties analysis revealed that YjhG might be a member of IlvD/EDD family. Results obtained in this study may lay a foundation for further investigation on YjhG and will benefit its application in biosynthesis of related chemicals.
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