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Open AccessArticle

2-Ketogluconate Kinase from Cupriavidus necator H16: Purification, Characterization, and Exploration of Its Substrate Specificity

1
Université Clermont Auvergne, CNRS, SIGMA Clermont, Institut de Chimie de Clermont-Ferrand, 63000 Clermont–Ferrand, France
2
University of Stuttgart, Institute of Microbiology, D-70569 Stuttgart, Germany
*
Authors to whom correspondence should be addressed.
Molecules 2019, 24(13), 2393; https://doi.org/10.3390/molecules24132393
Received: 7 June 2019 / Revised: 21 June 2019 / Accepted: 27 June 2019 / Published: 28 June 2019
(This article belongs to the Special Issue Carbohydrates in Synthesis)
We have cloned, overexpressed, purified, and characterized a 2-ketogluconate kinase (2-dehydrogluconokinase, EC 2.7.1.13) from Cupriavidus necator (Ralstonia eutropha) H16. Exploration of its substrate specificity revealed that three ketoacids (2-keto-3-deoxy-d-gluconate, 2-keto-d-gulonate, and 2-keto-3-deoxy-d-gulonate) with structures close to the natural substrate (2-keto-d-gluconate) were successfully phosphorylated at an efficiency lower than or comparable to 2-ketogluconate, as depicted by the measured kinetic constant values. Eleven aldo and keto monosaccharides of different chain lengths and stereochemistries were also assayed but not found to be substrates. 2-ketogluconate-6-phosphate was synthesized at a preparative scale and was fully characterized for the first time. View Full-Text
Keywords: 2-ketogluconate; 2-ketogluconate kinase; 2-ketogulonate; 2-keto-3-deoxygluconate; Cupriavidus necator; biocatalysis; monosaccharides phosphate 2-ketogluconate; 2-ketogluconate kinase; 2-ketogulonate; 2-keto-3-deoxygluconate; Cupriavidus necator; biocatalysis; monosaccharides phosphate
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Sánchez-Moreno, I.; Trachtmann, N.; Ilhan, S.; Hélaine, V.; Lemaire, M.; Guérard-Hélaine, C.; Sprenger, G.A. 2-Ketogluconate Kinase from Cupriavidus necator H16: Purification, Characterization, and Exploration of Its Substrate Specificity. Molecules 2019, 24, 2393.

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