Analysis of Bacterial Glucose Dehydrogenase Homologs from Thermoacidophilic Archaeon Thermoplasma acidophilum : Finding and Characterization of Aldohexose Dehydrogenase

スポンサーリンク

概要

• 論文の詳細を見る

• The NADP+-preferring glucose dehydrogenase from thermoacidophilic archaeon Thermoplasma acidophilum has been characterized, and its crystal structure has been determined (Structure, 2:385-393, 1994). Its sequence and structure are not homologous to bacterial NAD(P)+-dependent glucose dehydrogenases, and its molecular weight is also quite defferent. On the other hand, three functionally unknown genes with homologies to bacterial NAD(P)+-dependent glucose dehydrogenases have been sequenced as part of the T. acidophilum genome project (gene names: Ta0191, Ta0747, and Ta0754 respectively). We expressed two genes of three, Ta0191 and Ta0754, in Escherichia coli, and purified the gene products to homogeneity. Dehydrogenase activities were thereby detected from the purified proteins. The Ta0754 gene product exhibited aldohexose dehydrogenase activity, and the Ta0191 gene product exhibited weak 2-deoxyglucose dehydrogenase activity. No aldohexose dehydrogenase gene has been isolated, while the enzyme was reported in 1968. This is the first report of the gene and primary structure. The purified Ta0754 gene product, designated AldT, was characterized. The enzyme AldT effectively catalyzed the oxidation of various aldohexoses, especially D-mannose. Lower activities on D-2-deoxyglucose, D-xylose, D-glucose, and D-fucose were detected although no activities were shown on other aldohexoses or additional sugars. As a cofactor, NAD+ was much more suitable for the activity than NADP+. The NAD+-preferring dehydrogenase most effectively reacting to D-mannose is for the first time. AldT was most active at pH 10 and above 70 °C, and completely stable up to 60 °C after incubation for 15 min. Other enzymatic properties were also investigated.

• 社団法人 日本農芸化学会の論文
• 2004-12-23

著者

• Tamura Tomohiro

  Research Institute of Genome-based Biofactory, AIST

• Tamura Tomohiro

  Lab. Of Molecular Environmental Microbiology Graduate School Of Agriculture Hokkaido Univ. Kita-9 Ni

• NISHIYA Yoshiaki

  Department of Biochemistry, Toyobo Co., Ltd.

• TAMURA Noriko

  Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and

• Tamura Tomohiro

  Research Institute Of Genome-based Biofactory Aist:laboratory Of Molecular Environmental Microbiolog

• Nishiya Yoshiaki

  Department Of Biochemistry Toyobo Co. Ltd.

関連論文

• Phylogenetic analysis of Rhodococcus erythropolis based on the variation of ribosomal proteins as observed by matrix-assisted laser desorption ionization-mass spectrometry without using genome information(METHODS)
• Three Types of Antibiotics Produced from Rhodococcus erythropolis Strains
• Structural insights into unique substrate selectivity of Thermoplasma acidophilum D-aldohexose dehydrogenase
• Analysis of Bacterial Glucose Dehydrogenase Homologs from Thermoacidophilic Archaeon Thermoplasma acidophilum : Finding and Characterization of Aldohexose Dehydrogenase
• A Novel Enzymatic Method for Measuring Mizoribine 5'-Monophosphate Levels in Serum(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
• Enzymatic Characterization of an Amine Oxidase from Arthrobacter sp. Used to Measure Phosphatidylethanolamine
• A Quinoline Antibiotic from Rhodococcus erythropolis JCM 6824
• Advances in the Development of Genetic Tools for the Genus Rhodococcus
• Homogeneous Enzymatic Assay for L-Cysteine with βC-S Lyase

スポンサーリンク