메뉴 건너뛰기




Volumn 183, Issue 1, 2000, Pages 55-61

Gene cloning, nucleotide sequence and biochemical properties of a cytoplasmic cyclomaltodextrinase (neopullulanase) from Alicyclobacillus acidocaldarius, reclassification of a group of enzymes

Author keywords

Amylase family; Alicyclobacillus acidocaldarius; Amylopullulanase; Cyclomaltodextrinase; Neopullulanase; Sub cellular location

Indexed keywords

AMYLASE; BACTERIAL ENZYME; CYCLOMALTODEXTRINASE; NEOPULLULANASE; POLYSACCHARIDE; PULLULAN; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

EID: 0033978303     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(99)00630-8     Document Type: Article
Times cited : (55)

References (30)
  • 1
    • 0030778420 scopus 로고    scopus 로고
    • α-Amylase family: Molecular biology and evolution
    • Janeěek S. α-Amylase family: molecular biology and evolution. Progr. Biophys. Mol. Biol. 67:1997;67-97.
    • (1997) Progr. Biophys. Mol. Biol. , vol.67 , pp. 67-97
    • Janeěek, S.1
  • 2
    • 0028580701 scopus 로고
    • Purification, properties and structural aspects of a thermoacidophilic α-amylase from Alicyclobacillus acidocaldarius ATCC27009. Insight into acidostability of proteins
    • Schwermann B., Pfau K., Liliensiek B., Schleyer M., Fischer T., Bakker E.P. Purification, properties and structural aspects of a thermoacidophilic α-amylase from Alicyclobacillus acidocaldarius ATCC27009. Insight into acidostability of proteins. Eur. J. Biochem. 226:1994;981-991.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 981-991
    • Schwermann, B.1    Pfau, K.2    Liliensiek, B.3    Schleyer, M.4    Fischer, T.5    Bakker, E.P.6
  • 3
    • 0031279756 scopus 로고    scopus 로고
    • Acidostable and acidophilic proteins: The example of the α-amylase from Alicyclobacillus acidocaldarius
    • Matzke J., Schwermann B., Bakker E.P. Acidostable and acidophilic proteins: the example of the α-amylase from Alicyclobacillus acidocaldarius. Comp. Biochem. Physiol. 118A:1997;475-479.
    • (1997) Comp. Biochem. Physiol. , vol.118 , pp. 475-479
    • Matzke, J.1    Schwermann, B.2    Bakker, E.P.3
  • 4
    • 0030276148 scopus 로고    scopus 로고
    • Biochemical identification of a lipoprotein with maltose-binding activity in the thermoacidophilic Gram-positive bacterium Alicyclobacillus acidocaldarius
    • Herrmann A., Schlösser A., Schmid R., Schneider E. Biochemical identification of a lipoprotein with maltose-binding activity in the thermoacidophilic Gram-positive bacterium Alicyclobacillus acidocaldarius. Res. Microbiol. 147:1996;733-737.
    • (1996) Res. Microbiol. , vol.147 , pp. 733-737
    • Herrmann, A.1    Schlösser, A.2    Schmid, R.3    Schneider, E.4
  • 5
    • 0024382861 scopus 로고
    • Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus
    • Kuriki T., Imanaka T. Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus. J. Gen. Microbiol. 135:1989;1521-1528.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 1521-1528
    • Kuriki, T.1    Imanaka, T.2
  • 6
    • 0026757347 scopus 로고
    • Structure of the gene encoding cyclomaltodextrinase from Clostridium thermohydrosulfuricum 39E and characterization of the enzyme purified from Escherichia coli
    • Podkovyrov S.M., Zeikus J.G. Structure of the gene encoding cyclomaltodextrinase from Clostridium thermohydrosulfuricum 39E and characterization of the enzyme purified from Escherichia coli. J. Bacteriol. 174:1992;5400-5405.
    • (1992) J. Bacteriol. , vol.174 , pp. 5400-5405
    • Podkovyrov, S.M.1    Zeikus, J.G.2
  • 7
    • 0026828477 scopus 로고
    • Nucleotide sequence of a gene that encodes a neopullulanase from an alkalophilic Bacillus
    • Igarashi K., Ara K., Saeki K., Ozaki K., Kawai S., Ito S. Nucleotide sequence of a gene that encodes a neopullulanase from an alkalophilic Bacillus. Biosci. Biotech. Biochem. 56:1992;514-516.
    • (1992) Biosci. Biotech. Biochem. , vol.56 , pp. 514-516
    • Igarashi, K.1    Ara, K.2    Saeki, K.3    Ozaki, K.4    Kawai, S.5    Ito, S.6
  • 8
    • 0027189835 scopus 로고
    • Cloning and sequence analysis of the cyclomaltodextrinase gene from Bacillus sphaericus and expression in Escherichia coli cells
    • Oguma T., Matsuyama A., Nimuchi M., Nakano E. Cloning and sequence analysis of the cyclomaltodextrinase gene from Bacillus sphaericus and expression in Escherichia coli cells. Appl. Microbiol. Biotechnol. 39:1993;197-203.
    • (1993) Appl. Microbiol. Biotechnol. , vol.39 , pp. 197-203
    • Oguma, T.1    Matsuyama, A.2    Nimuchi, M.3    Nakano, E.4
  • 10
    • 0029919677 scopus 로고    scopus 로고
    • Genetics of a novel starch utilisation pathway present in Klebsiella oxytoca
    • Fiedler G., Pajatsch M., Böck A. Genetics of a novel starch utilisation pathway present in Klebsiella oxytoca. J. Mol. Biol. 256:1996;279-291.
    • (1996) J. Mol. Biol. , vol.256 , pp. 279-291
    • Fiedler, G.1    Pajatsch, M.2    Böck, A.3
  • 11
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • Kunst F., Ogasawara N., Moszer I., et al. The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature. 390:1997;249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3
  • 12
    • 0032053544 scopus 로고    scopus 로고
    • Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose
    • Cha H., Yoon H.-G., Kim Y.-W., Lee H.-S., Kim J.-W., Kweon K.-S., Oh B.-H., Park K.-H. Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose. Eur. J. Biochem. 253:1998;251-262.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 251-262
    • Cha, H.1    Yoon, H.-G.2    Kim, Y.-W.3    Lee, H.-S.4    Kim, J.-W.5    Kweon, K.-S.6    Oh, B.-H.7    Park, K.-H.8
  • 13
    • 0032942009 scopus 로고    scopus 로고
    • Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain
    • Kim T.-J., Kim M.-J., Kim B.-C., Kim J.-C., Cheong T.-K., Kim J.-W., Park K.-H. Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain. Appl. Environ. Microbiol. 65:1999;1644-1651.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1644-1651
    • Kim, T.-J.1    Kim, M.-J.2    Kim, B.-C.3    Kim, J.-C.4    Cheong, T.-K.5    Kim, J.-W.6    Park, K.-H.7
  • 14
    • 0002485280 scopus 로고
    • Bacillus acidocaldarius sp. nov., an acidophilic thermophilic spore-forming bacterium
    • Darland G., Brock T.D. Bacillus acidocaldarius sp. nov., an acidophilic thermophilic spore-forming bacterium. J. Gen. Microbiol. 67:1971;9-15.
    • (1971) J. Gen. Microbiol. , vol.67 , pp. 9-15
    • Darland, G.1    Brock, T.D.2
  • 15
    • 0021736478 scopus 로고
    • In vivo evidence for the role of the ε subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli
    • Klionsky D.J. In vivo evidence for the role of the ε subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli. J. Bacteriol. 160:1984;1055-1060.
    • (1984) J. Bacteriol. , vol.160 , pp. 1055-1060
    • Klionsky, D.J.1
  • 16
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequence of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequence of the M13mp18 and pUC19 vectors. Gene. 33:1985;103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 17
    • 0002088351 scopus 로고
    • Synthesis of bacteriophage and plasmid-encoded polypeptides in minicells.
    • (Pühler, A. and Timmis, K.N., Eds.), Springer, Berlin
    • Reeve, J. (1984) Synthesis of bacteriophage and plasmid-encoded polypeptides in minicells. In: Advanced Molecular Genetics (Pühler, A. and Timmis, K.N., Eds.), pp. 212-223. Springer, Berlin.
    • (1984) In: Advanced Molecular Genetics , pp. 212-223
    • Reeve, J.1
  • 18
    • 0028093146 scopus 로고
    • Direct detection of pullulanase activity in electrophoretic polyacrylamide gels
    • Furegon L., Curioni A., Peruffo A.D.B. Direct detection of pullulanase activity in electrophoretic polyacrylamide gels. Anal. Biochem. 221:1994;200-201.
    • (1994) Anal. Biochem. , vol.221 , pp. 200-201
    • Furegon, L.1    Curioni, A.2    Peruffo, A.D.B.3
  • 19
    • 0001614498 scopus 로고
    • Exoamylase activity in vacuoles isolated from pea and wheat leaf protoplasts
    • Ziegler P., Beck E. Exoamylase activity in vacuoles isolated from pea and wheat leaf protoplasts. Plant Physiol. 82:1986;1119-1121.
    • (1986) Plant Physiol. , vol.82 , pp. 1119-1121
    • Ziegler, P.1    Beck, E.2
  • 20
    • 0002761512 scopus 로고
    • The α-amylases
    • (Radley, J.A., Ed.), Chapman and Hall, London
    • Robyt, J.F. and Whelan, W.J. (1968) The α-amylases. In: Starch and its derivatives (Radley, J.A., Ed.), pp. 430-476. Chapman and Hall, London.
    • (1968) In: Starch and Its Derivatives , pp. 430-476
    • Robyt, J.F.1    Whelan, W.J.2
  • 23
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson W.R., Lipman D.J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:1988;2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 24
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through weighting, positive-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through weighting, positive-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 25
    • 0030203863 scopus 로고    scopus 로고
    • TREEVIEW: An application to display phylogenetic trees on personal computer
    • Page R.M.D. TREEVIEW: an application to display phylogenetic trees on personal computer. Comput. Appl. Biosci. 12:1996;357-358.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.M.D.1
  • 26
    • 0033574502 scopus 로고    scopus 로고
    • Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution
    • Kamitori S., Kondo S., Okuyama K., Yokota T., Shimura Y., Tonozuka T., Sakano Y. Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution. J. Mol. Biol. 287:1999;907-921.
    • (1999) J. Mol. Biol. , vol.287 , pp. 907-921
    • Kamitori, S.1    Kondo, S.2    Okuyama, K.3    Yokota, T.4    Shimura, Y.5    Tonozuka, T.6    Sakano, Y.7
  • 27
    • 0027257462 scopus 로고
    • Sequencing of the amylopullulanase (apu) gene of Thermoanaerobacter ethanolycus 39E and identification of the active site by site-directed mutagenesis
    • Mathupula S.P., Lowe S.E., Podkovyrov S.M., Zeikus J.G. Sequencing of the amylopullulanase (apu) gene of Thermoanaerobacter ethanolycus 39E and identification of the active site by site-directed mutagenesis. J. Biol. Chem. 268:1993;16332-16344.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16332-16344
    • Mathupula, S.P.1    Lowe, S.E.2    Podkovyrov, S.M.3    Zeikus, J.G.4
  • 29
    • 0029089389 scopus 로고
    • Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVAI and TVAII, from Thermoactinomyces vulgaris R-47
    • Tonozuka T., Mogi S., Shimura Y., Ibuka A., Sakai H., Matsuzawa H., Sakano Y., Ohta T. Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVAI and TVAII, from Thermoactinomyces vulgaris R-47. Biochim. Biophys. Acta. 1252:1995;35-42.
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 35-42
    • Tonozuka, T.1    Mogi, S.2    Shimura, Y.3    Ibuka, A.4    Sakai, H.5    Matsuzawa, H.6    Sakano, Y.7    Ohta, T.8
  • 30
    • 0022670999 scopus 로고
    • Comparison of amino acid sequences of eleven different α-amylases
    • Nakajima R., Imanaka T., Aiba S. Comparison of amino acid sequences of eleven different α-amylases. Appl. Microbiol. Biotechnol. 23:1986;231-237.
    • (1986) Appl. Microbiol. Biotechnol. , vol.23 , pp. 231-237
    • Nakajima, R.1    Imanaka, T.2    Aiba, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.