Cloning, Sequence Analysis, and Expression of the Gene Encoding Sphingomonas paucimobilis FP2001 α-L-Rhamnosidase

Takeshi Miyata1, Nobuhiro Kashige1, Tomomitsu Satho1, Tadatoshi Yamaguchi2, Yoichi Aso3, Fumio Miake1
1Microbiology Laboratory, Faculty of Pharmaceutical Sciences, Fukuoka University, 8-19-1 Nanakuma, Johnan-ku, Fukuoka, 814-0180, Japan
2Department of Hygiene, School of Medicine, Miyazaki University, 5200 Kihara, Kiyotake, Miyazaki, 889-1692, Japan
3Laboratory of Protein Chemistry and Engineering, Department of Genetic Resources Technology, Faculty of Agriculture, Kyushu University, Fukuoka, 812-8581, Japan

Tóm tắt

Từ khóa


Tài liệu tham khảo

Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25:3389–3402

Bourbouze R, Percheron F, Courtois JE (1976) [alpha-L-Rhamnosidase from Fagopyrum esculentum: purification and some properties (translated from)]. Eur J Biochem 63:331–337

Eriksson U, Svenson SB, Lonngren J, Lindberg AA (1979) Salmonella phage glycanases: substrate specificity of the phage P22 endo-rhamnosidase. J Gen Virol 43:503–511

Hashimoto W, Miyake O, Nankai H, Murata K (2003) Molecular identification of an alpha-L-rhamnosidase from Bacillus sp strain GL1 as an enzyme involved in complete metabolism of gellan. Arch Biochem Biophys 415:235–244

Hashimoto W, Murata K (1998) alpha-L-rhamnosidase of Sphingomonas sp. R1 producing an unusual exopolysaccharide of sphingan. Biosci Biotechnol Biochem 62:1068–1074

Hashimoto W, Nankai H, Sato N, Kawai S, Murata K (1999) Characterization of alpha-L-rhamnosidase of Bacillus sp. GL1 responsible for the complete depolymerization of gellan. Arch Biochem Biophys 368:56–60

Imai R, Nagata Y, Fukuda M, Takagi M, Yano K (1991) Molecular cloning of a Pseudomonas paucimobilis gene encoding a 17-kilodalton polypeptide that eliminates HCl molecules from gamma-hexachlorocyclohexane. J Bacteriol 173:6811–6819

Jang IS, Kim DH (1996) Purification and characterization of alpha-L-rhamnosidase from Bacteroides JY-6, a human intestinal bacterium. Biol Pharm Bull 19:1546–1549

Miake F, Murata K, Kuroiwa A, Kumamoto T, Kuroda S, Terasawa T, Tone H, Watanabe K (1995) Characterization of Pseudomonas paucimobilis FP2001 which forms flagella depending upon the presence of rhamnose in liquid medium. Microbiol Immunol 39:437–442

Miake F, Satho T, Takesue H, Yanagida F, Kashige N, Watanabe K (2000) Purification and characterization of intracellular alpha-L-rhamnosidase from Pseudomonas paucimobilis FP2001. Arch Microbiol 173:65–70

Palleroni NJ (1984) Geneus I. Pseudomonas Migula 1894, 237AL (Nom. cons. Opin. 5, Jud Comm. 1952, 237). In: Kreig NR, Holt JG (eds). Bergey’s manual of systematic baceteriology, vol 1. Baltimore: The Williams & Willkins Co. p 141–199

Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press

Shine J, Dalgarno L (1974) The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci USA 71:1342–1346

Soria F, Ellenrieder G (2002) Thermal inactivation and product inhibition of Aspergillus terreus CECT 2663 alpha-L-rhamnosidase and their role on hydrolysis of naringin solutions. Biosci Biotechnol Biochem 66:1442–1449

Wosten MM (1998) Eubacterial sigma-factors. FEMS Microbiol Rev 22:127–150

Yanai T, Sato M (2000) Purification and characterization of an alpha-L-rhamnosidase from Pichia angusta X349. Biosci Biotechnol Biochem 64:2179–2185

Yu H, Gong J, Zhang C, Jin F (2002) Purification and characterization of ginsenoside-alpha-L-rhamnosidase. Chem Pharm Bull (Tokyo) 50:175–178

Zverlov VV, Hertel C, Bronnenmeier K, Hroch A, Kellermann J, Schwarz WH (2000) The thermostable alpha-L-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial alpha-L-rhamnoside hydrolase, a new type of inverting glycoside hydrolase. Mol Microbiol 35:173–179