Institute for Genomic Biology, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.
Biochemistry. 2014 Jul 1;53(25):4087-9. doi: 10.1021/bi500683x. Epub 2014 Jun 20.
The d-mannonate dehydratase (ManD) subgroup of the enolase superfamily contains members with varying catalytic activities (high-efficiency, low-efficiency, or no activity) that dehydrate d-mannonate and/or d-gluconate to 2-keto-3-deoxy-d-gluconate [Wichelecki, D. J., et al. (2014) Biochemistry 53, 2722-2731]. Despite extensive in vitro characterization, the in vivo physiological role of a ManD has yet to be established. In this study, we report the in vivo functional characterization of a high-efficiency ManD from Caulobacter crescentus NA1000 (UniProt entry B8GZZ7) by in vivo discovery of its essential role in d-glucuronate metabolism. This in vivo functional annotation may be extended to ~50 additional proteins.
烯醇酶超家族的 d-甘露糖酸盐脱水酶（ManD）亚组包含具有不同催化活性（高效、低效或无活性）的成员，这些成员可将 d-甘露糖酸盐和/或 d-葡萄糖酸盐脱水为 2-酮-3-脱氧-d-葡萄糖酸[Wichelecki, D. J., et al. (2014) Biochemistry 53, 2722-2731]。尽管已经进行了广泛的体外表征，但 ManD 的体内生理作用尚未确定。在这项研究中，我们通过体内发现其在 d-葡萄糖醛酸代谢中的必需作用，报道了来自新月柄杆菌 NA1000 的高效 ManD（UniProt 条目 B8GZZ7）的体内功能特征。这种体内功能注释可能会扩展到大约 50 个其他蛋白质。
