Structural insight into glucose dehydrogenase from the thermoacidophilic archaeon Thermoplasma volcanium. (1st May 2014)

• Record Type: Journal Article
• Authors: Kanoh, Yoshitaka; Uehara, Seiichiroh; Iwata, Hideyuki; Yoneda, Kazunari; Ohshima, Toshihisa; Sakuraba, Haruhiko
• Is Part Of: Acta crystallographica. Volume 70:Part 5(2014:May)
• Page Start: 1271
• Page End: 1280
• Publication Date: 2014-05-01
• Subjects: Biomolecules -- Structure -- Periodicals; Physical biochemistry -- Periodicals; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; 572
• DOI: 10.1107/S1399004714002363
• Languages: English
• ISSNs: 0907-4449

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Glucose dehydrogenase from the thermoacidophilic archaeon <italic>Thermoplasma volcanium</italic> (tvGlcDH) is highly active towards D‐glucose and D‐galactose, but does not utilize aldopentoses such as D‐xylose as substrates. In the present study, the crystal structures of substrate/cofactor‐free tvGlcDH and of a tvGlcDH T277F mutant in a binary complex with NADP and in a ternary complex with D‐glucose and nicotinic acid adenine dinucleotide phosphate, an NADP analogue, were determined at resolutions of 2.6, 2.25 and 2.33 Å, respectively. The overall structure of each monomer showed notable similarity to that of the enzyme from <italic>Sulfolobus solfataricus</italic> (ssGlcDH‐1), which accepts a broad range of C5 and C6 sugars as substrates. However, the amino‐acid residues of tvGlcDH involved in substrate binding markedly differed from those of ssGlcDH‐1. Structural comparison revealed that a decreased number of interactions between the C3‐hydroxyl group of the sugar and the enzyme are likely to be responsible for the lack of reactivity of tvGlcDH towards D‐xylose.</p> </abstract>