Molecular Characterization of an Intracellular β-N-Acetylglucosaminidase Involved in the Chitin Degradation System of Streptomyces thermoviolaceus OPC-520
スポンサーリンク
概要
- 論文の詳細を見る
We purified and characterized an intracellular β-N-acetylglucosaminidase (NagC) from a cytoplasmic fraction of Streptomyces thermoviolaceus OPC-520. The molecular mass of NagC was estimated to be 60 kDa by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH and temperature of the enzyme were 6.0 and 50 °C respectively. Purified NagC hydrolyzed chitin oligosaccharides from N,N′-diacetylchitobiose (GlcNAc)2 to chitopentaose (GlcNAc)5, hydrolyzed N,N′-diacetylchitobiose especially rapidly, and showed a tendency to decrease with increases in the degree of polymerization. But, NagC didn’t hydrolyze chitohexaose (GlcNAc)6. The gene encoding NagC was cloned and sequenced. The open reading frame of nagC encoded a protein of 564 amino acids with a calculated molecular mass of 62,076 Da. The deduced amino acid sequence of NagC showed homology with several β-N-acetylglucosaminidases belonging to glycosyl hydrolase family 20. The expression plasmid coding for NagC was constructed in Escherichia coli. The recombinant enzyme showed pH and temperature optima and substrate specificity similar to those of the native enzyme. The gene arrangement near the nagC gene of S. thermoviolaceus OPC-520 was compared with that of S. coelicolor A3(2). Three genes, which appear to constitute an ABC transport system for sugar, were missing in the vicinity of the nagC gene.
- 社団法人 日本農芸化学会の論文
- 2004-06-23
著者
-
Inamori Yoshihiko
Department Of Microbiology Osaka University Of Pharmaceutical Sciences
-
Kubota Takahiro
Department Of Physiology Ii Osaka Medical College
-
Kubota Takahiro
Department Of Drug Metabolism And Biopharmaceutics Faculty Of Pharmacy Chiba Institute Of Science
-
YASUDA Masahide
Department of Applied Chemistry, Faculty of Engineering, Miyazaki University
-
MIYAMOTO Katsushiro
Department of Microbiology, Osaka University of Pharmaceutical Sciences
-
TSUJIBO Hiroshi
Department of Microbiology, Osaka University of Pharmaceutical Sciences
-
Yoshimura M
Department Of Microbiology Osaka University Of Pharmaceutical Sciences
-
Tsujibo H
Department Of Microbiology Osaka University Of Pharmaceutical Sciences
-
Miyamoto K
Central Research Laboratories Osaka University Of Pharmaceutical Sciences
-
Yasuda Masahide
Department Of Applied Chemistry Faculty Of Engineering Miyazaki University
-
Inamori Yoshihiko
Department Of Microbiology Osaka College Of Pharmacy
-
Kubota Takahiro
Department Of Microbiology Osaka University Of Pharmaceutical Sciences
-
YASUDA Masahide
Depariment of Hygienic Chemistry, Osaka College of Pharmacy
関連論文
- Molecular Cloning of the Gene Encoding a Novel β-N-Acetylhexosaminidase from a Marine Bacterium, Alteromonas sp. Strain O-7, and Characterization of the Cloned Enzyme(Biochemistry & Molecular Biology)
- Molecular Cloning of the Gene Encoding an Outer-Membrane-Associated β-N-Acetylglucosaminidase Involved in Chitin Degradation System of Alteromonas sp. Strain O-7
- Association of troglitazone-induced liver injury with mutation of the cytochrome P450 2C19 gene
- Isolation of immunosuppressive phospholipids from marine bacteria
- Production of Angiotensin-Converting Enzyme Inhibitors from Baker's Yeast Glyceraldehyde-3-phosphate Dehydrogenase
- Bacillus stearothermophilus Glyceraldehyde-3-phosphate Dehydrogenase as a Source of Angiotensin-converting Enzyme Inhibitors(Biological Chemistry)
- Utilization of Proteinase K-Treated Cells as Lipopolysaccharide Antigens for the Serodiagnosis of Helicobacter pylori Infections
- Cloning and Nucleotide Sequence of the Gene Encoding a Serine Proteinase Inhibitor Named Marinostatin from a Marine Bacterium, Alteromonas sp. Strain B-10-31
- Infiltration of H-2^d-Specific Cytotoxic Macrophage with Unique Morphology into Rejection Site of Allografted Meth A (H-2^d) Tumor Cells in C57BL/6 (H-2^b) Mice
- One-Loop Path Integral of the Open Superstring