On June 8, 2022, Yang, Hua; Yan, Ruxue; Li, Yue; Lu, Zhaoxin; Bie, Xiaomei; Zhao, Haizhen; Lu, Fengxia; Chen, Meirong published an article.Computed Properties of 585-88-6 The title of the article was Structure-function analysis of a quinone-dependent dehydrogenase capable of deoxynivalenol detoxification. And the article contained the following:
The pyrroloquinoline quinone (PQQ)-dependent dehydrogenase DepA detoxifies deoxynivalenol (DON) by converting the C3-OH into a keto group. Herein, two crystal structures of DepA and its complex with PQQ were determined, together with biochem. evidence confirming the interactions of DepA with PQQ and DON and revealing a unique tyrosine residue important for substrate selection. Furthermore, four loops over the active site essential for DepA activity were identified, of which three loops were stabilized by PQQ, and the fourth loop invisible in both structures was considered important for binding DON, together constituting a lid for the active site. Preliminary engineering of the loop showed its potential for enzyme improvement. This study provides structural insights into how a PQQ-dependent dehydrogenase is equipped with the function of DON conversion and for the first time shows the necessity of a lid structure for PQQ-dependent dehydrogenase activity, laying foundation for structure-based design to enhance catalysis efficiency. The experimental process involved the reaction of SweetPearlR P300 DC Maltitol(cas: 585-88-6).Computed Properties of 585-88-6
The Article related to pyrroloquinoline quinone dependent dehydrogenase depa devosia structure deoxynivalenol detoxification, devosia pqq dependent dehydrogenase depa structure deoxynivalenol detoxification, crystal structure, deoxynivalenol, enzyme engineering, quinone-dependent dehydrogenase, substrate specificity and other aspects.Computed Properties of 585-88-6
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