Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand

• Published in: Bioscience, biotechnology, and biochemistry Vol. 69; no. 6; pp. 1120 - 1129
• Main Authors: Toyama, H. (Yamaguchi Univ. (Japan). Faculty of Agriculture), Soemphol, W, Moonmangmee, D, Adachi, O, Matsushita, K
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.06.2005; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: acetic acid bacteria; Amino Acid Sequence; AMINO ACID SEQUENCES; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Base Sequence; Biological and medical sciences; Conserved Sequence; CYTOCHROME C; FAD; Flavin-Adenine Dinucleotide - chemistry; Fundamental and applied biological sciences. Psychology; Gluconobacter; Gluconobacter - enzymology; Gluconobacter frateurii; HEAT TOLERANCE; L-Iditol 2-Dehydrogenase - chemistry; L-Iditol 2-Dehydrogenase - metabolism; Membrane Proteins - chemistry; Membrane Proteins - metabolism; MOLECULAR CLONING; Molecular Sequence Data; Oxidation-Reduction; OXIDOREDUCTASES; PSEUDOMONACEAE; PURIFICATION; QUINOLINES; QUINONES; Sequence Alignment; Sequence Homology, Amino Acid; SORBITOL; Sorbitol - metabolism; sorbitol dehydrogenase; Thailand; Thailand; Asia; Acetobacteraceae; Cytochrome c; sorbitol dehydrogenase; Enzyme; FAD; Bacteria; L-Iditol 2-dehydrogenase; Membrane; Oxidoreductases; Gluconobacter; Acetic acid bacteria
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.69.1120

There are two types of membrane-bound D-sorbitol dehydrogenase (SLDH) reported: PQQ-SLDH, having pyrroloquinoline quinone (PQQ), and FAD-SLDH, containing FAD and heme c as the prosthetic groups. FAD-SLDH was purified and characterized from the PQQ-SLDH mutant strain of a thermotolerant Gluco-nobacter frateurii, having molecular mass of 61.5kDa, 52kDa, and 22kDa. The enzyme properties were quite similar to those of the enzyme from mesophilic G. oxydans IFO 3254. This enzyme was shown to be inducible by D-sorbitol, but not PQQ-SLDH. The oxidation product of FAD-SLDH from D-sorbitol was identified as L-sorbose. The cloned gene of FAD-SLDH had three open reading frames (sldSLC) corresponding to the small, the large, and cytochrome c sub-units of FAD-SLDH respectively. The deduced amino acid sequences showed high identity to those from G. oxydans IFO 3254: SldL showed to other FAD-enzymes, and SldC having three heme c binding motives to cytochrome c sub-units of other membrane-bound dehydrogenases.