2-酮葡萄糖酸激酶来自 H16：纯化、特性分析及其底物特异性研究。
2-Ketogluconate Kinase from H16: Purification, Characterization, and Exploration of Its Substrate Specificity.
机构信息
Université Clermont Auvergne, CNRS, SIGMA Clermont, Institut de Chimie de Clermont-Ferrand, 63000 Clermont-Ferrand, France.
University of Stuttgart, Institute of Microbiology, D-70569 Stuttgart, Germany.
出版信息
Molecules. 2019 Jun 28;24(13):2393. doi: 10.3390/molecules24132393.
We have cloned, overexpressed, purified, and characterized a 2-ketogluconate kinase (2-dehydrogluconokinase, EC 2.7.1.13) from 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.
我们已经从 H16 中克隆、过表达、纯化并鉴定了一种 2-酮葡萄糖酸激酶（2-脱水葡萄糖酸激酶，EC 2.7.1.13）。对其底物特异性的探索表明，三种结构与天然底物（2-酮-d-葡萄糖酸）相近的酮酸（2-酮-3-脱氧-d-葡萄糖酸、2-酮-d-古洛糖酸和 2-酮-3-脱氧-d-古洛糖酸）能够以低于或与 2-酮葡萄糖酸相当的效率进行磷酸化，这可以从测量的动力学常数值中看出。还测定了十一种不同链长和立体化学的醛糖和酮糖，但它们都不是底物。2-酮葡萄糖酸 6-磷酸以制备规模合成，并首次得到了充分的表征。
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