Structural analysis of fungus-derived FAD glucose dehydrogenase

Yoshida, Hiromi; Sakai, Genki; Mori, Kazushige; Kojima, Katsuhiro; Kamitori, Shigehiro; Sode, Koji

doi:10.1038/srep13498

Cited by 102 publications

(114 citation statements)

References 62 publications

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“…GOx has a homodimeric structure with a narrow active site pocket, resulting in a minimum distance of 13 Å between the protein surface and the FAD site [30,31]. In contrast, according to the crystal structure of FAD-GDH from Aspergillus flavus [32], this enzyme has a broader substrate-binding pocket than that of GOx, which allows easier access of redox molecules to the FAD site. The bimolecular rate constant of pyrroloquinoline quinone-dependent glucose dehydrogenase (PQQ-GDH) for a variety of quinones showed similar potential-dependent behavior, although PQQ-GDH exhibits potential-dependent activation-controlled as well as potential-independent diffusion-controlled regions [33].…”

Section: Resultsmentioning

confidence: 99%

Bimolecular Rate Constants for FAD-Dependent Glucose Dehydrogenase from Aspergillus terreus and Organic Electron Acceptors

Tsuruoka

Sadakane

Hayashi

et al. 2017

IJMS

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Abstract:The flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) from Aspergillus species require suitable redox mediators to transfer electrons from the enzyme to the electrode surface for the application of bioelectrical devices. Although several mediators for FAD-GDH are already in use, they are still far from optimum in view of potential, kinetics, sustainability, and cost-effectiveness. Herein, we investigated the efficiency of various phenothiazines and quinones in the electrochemical oxidation of FAD-GDH from Aspergillus terreus. At pH 7.0, the logarithm of the bimolecular oxidation rate constants appeared to depend on the redox potentials of all the mediators tested. Notably, the rate constant of each molecule for FAD-GDH was approximately 2.5 orders of magnitude higher than that for glucose oxidase from Aspergillus sp. The results suggest that the electron transfer kinetics is mainly determined by the formal potential of the mediator, the driving force of electron transfer, and the electron transfer distance between the redox active site of the mediator and the FAD, affected by the steric or chemical interactions. Higher k 2 values were found for ortho-quinones than for para-quinones in the reactions with FAD-GDH and glucose oxidase, which was likely due to less steric hindrance in the active site in the case of the ortho-quinones.

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Section: Resultsmentioning

confidence: 99%

Bimolecular Rate Constants for FAD-Dependent Glucose Dehydrogenase from Aspergillus terreus and Organic Electron Acceptors

Tsuruoka

Sadakane

Hayashi

et al. 2017

IJMS

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“…A 3D structural model of Botryotinia fuckeliana-derived GDH (Bf GDH) was generated based on the crystal structure of FAD-dependent glucose dehydrogenase derived from A. flavus (Af GDH, PDB ID: 4YNU) [28]. The amino acid sequences of GOx derived from A. niger (AnGOx, PDB ID: 1CF3) and of the GDHs were aligned using the multiple sequence alignment software ClustalW (http://www.clustal.org) [29].…”

Section: Identification Of the Appropriate Mutation Site By Comparingmentioning

confidence: 99%

Engineered Glucose Oxidase Capable of Quasi-Direct Electron Transfer after a Quick-and-Easy Modification with a Mediator

Suzuki

Lee

Loew

et al. 2020

IJMS

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Glucose oxidase (GOx) has been widely utilized for monitoring glycemic levels due to its availability, high activity, and specificity toward glucose. Among the three generations of electrochemical glucose sensor principles, direct electron transfer (DET)-based third-generation sensors are considered the ideal principle since the measurements can be carried out in the absence of a free redox mediator in the solution without the impact of oxygen and at a low enough potential for amperometric measurement to avoid the effect of electrochemically active interferences. However, natural GOx is not capable of DET. Therefore, a simple and rapid strategy to create DET-capable GOx is desired. In this study, we designed engineered GOx, which was made readily available for single-step modification with a redox mediator (phenazine ethosulfate, PES) on its surface via a lysine residue rationally introduced into the enzyme. Thus, PES-modified engineered GOx showed a quasi-DET response upon the addition of glucose. This strategy and the obtained results will contribute to the further development of quasi-DET GOx-based glucose monitoring dedicated to precise and accurate glycemic control for diabetic patient care.

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“…PDB ID: 1GAL [67] or 1CF3 [68]). Interestingly, a catalytically favourable conformation of the active-site histidine (henceforth denoted as the 'catalytic' conformation) was observed in a related glucose dehydrogenase from Aspergillus flavus (AfGDH), which was crystallized in complex with D-glucono-1,5-lactone product [69]. However, in the structure of the GOx from Penicillium amagasakiense (PaGOx), His516 is observed in a different conformation [68], in which its position geometrically prevents proton abstraction from the substrate (henceforth denoted as the 'non-catalytic' conformation; figure 3a).…”

Section: Glucose Oxidasementioning

confidence: 99%

Conformational dynamics and enzyme evolution

Petrović

Risso

Kamerlin

et al. 2018

J. R. Soc. Interface.

172

184

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Enzymes are dynamic entities, and their dynamic properties are clearly linked to their biological function. It follows that dynamics ought to play an essential role in enzyme evolution. Indeed, a link between conformational diversity and the emergence of new enzyme functionalities has been recognized for many years. However, it is only recently that state-ofthe-art computational and experimental approaches are revealing the crucial molecular details of this link. Specifically, evolutionary trajectories leading to functional optimization for a given host environment or to the emergence of a new function typically involve enriching catalytically competent conformations and/or the freezing out of non-competent conformations of an enzyme. In some cases, these evolutionary changes are achieved through distant mutations that shift the protein ensemble towards productive conformations. Multifunctional intermediates in evolutionary trajectories are probably multi-conformational, i.e. able to switch between different overall conformations, each competent for a given function. Conformational diversity can assist the emergence of a completely new active site through a single mutation by facilitating transition-state binding. We propose that this mechanism may have played a role in the emergence of enzymes at the primordial, progenote stage, where it was plausibly promoted by high environmental temperatures and the possibility of additional phenotypic mutations.

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Structural analysis of fungus-derived FAD glucose dehydrogenase

Cited by 102 publications

References 62 publications

Bimolecular Rate Constants for FAD-Dependent Glucose Dehydrogenase from Aspergillus terreus and Organic Electron Acceptors

Bimolecular Rate Constants for FAD-Dependent Glucose Dehydrogenase from Aspergillus terreus and Organic Electron Acceptors

Engineered Glucose Oxidase Capable of Quasi-Direct Electron Transfer after a Quick-and-Easy Modification with a Mediator

Conformational dynamics and enzyme evolution

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