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Volumn 99, Issue 1, 2005, Pages 48-54

Molecular identification of Sphingomonas sp. A1 alginate lyase (A1-IV′) as a member of novel polysaccharide lyase family 15 and implications in alginate lyase evolution

Author keywords

Alginate lyase; Evolution; Molecular diversity; Polysaccharide lyase family 15; Sphingomonas sp. A1

Indexed keywords

BACTERIA; CELLS; CYTOLOGY; ESCHERICHIA COLI; GENES; METABOLISM; POLYMERIZATION; POLYSACCHARIDES; STRAIN;

EID: 12444285375     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.99.48     Document Type: Article
Times cited : (41)

References (22)
  • 2
    • 0033759340 scopus 로고    scopus 로고
    • Alginate lyase: Review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications
    • Wong, T. Y., Preston, L. A., and Schiller, N. L.: Alginate lyase: review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications. Annu. Rev. Microbiol., 54, 289-340 (2000).
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 289-340
    • Wong, T.Y.1    Preston, L.A.2    Schiller, N.L.3
  • 3
    • 0032883510 scopus 로고    scopus 로고
    • Evidence for a novel Chlorella virus-encoded alginate lyase
    • Suda, K., Tanji, Y., Hori, K., and Unno, H.: Evidence for a novel Chlorella virus-encoded alginate lyase. FEMS Microbiol. Lett., 180, 45-53 (1999).
    • (1999) FEMS Microbiol. Lett. , vol.180 , pp. 45-53
    • Suda, K.1    Tanji, Y.2    Hori, K.3    Unno, H.4
  • 5
    • 0344737824 scopus 로고    scopus 로고
    • cDNA cloning of an alginate lyase from abalone, Haliotis discus hannai
    • Shimizu, E., Ojima, T., and Nishita, K.: cDNA cloning of an alginate lyase from abalone, Haliotis discus hannai. Carbohydr. Res., 338, 2841-2852 (2003).
    • (2003) Carbohydr. Res. , vol.338 , pp. 2841-2852
    • Shimizu, E.1    Ojima, T.2    Nishita, K.3
  • 7
    • 0033905713 scopus 로고    scopus 로고
    • Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate
    • Hashimoto, W., Miyake, O., Momma, K., Kawai, S., and Murata, K.: Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate. J. Bacteriol., 182, 4572-4577 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 4572-4577
    • Hashimoto, W.1    Miyake, O.2    Momma, K.3    Kawai, S.4    Murata, K.5
  • 8
    • 0027168719 scopus 로고
    • Bacterial alginate lyase gene: Nucleotide sequence and molecular route for the generation of alginate lyase species
    • Yonemoto, Y., Tanaka, H., Hisano, T., Sakaguchi, K., Abe, S., Yamashita, T., Kimura, A., and Murata, K.: Bacterial alginate lyase gene: nucleotide sequence and molecular route for the generation of alginate lyase species. J. Ferment. Bioeng., 75, 336-342 (1993).
    • (1993) J. Ferment. Bioeng. , vol.75 , pp. 336-342
    • Yonemoto, Y.1    Tanaka, H.2    Hisano, T.3    Sakaguchi, K.4    Abe, S.5    Yamashita, T.6    Kimura, A.7    Murata, K.8
  • 9
    • 0031783859 scopus 로고    scopus 로고
    • Sphingomonas sp. A1 lyase active on both poly-β-D-mannuronate and heteropolymeric regions in alginate
    • Hashimoto, W., Okamoto, M., Misano, T., Momma, K., and Murata, K.: Sphingomonas sp. A1 lyase active on both poly-β-D-mannuronate and heteropolymeric regions in alginate. J. Ferment. Bioeng., 86, 236-238 (1998).
    • (1998) J. Ferment. Bioeng. , vol.86 , pp. 236-238
    • Hashimoto, W.1    Okamoto, M.2    Misano, T.3    Momma, K.4    Murata, K.5
  • 10
    • 0034084571 scopus 로고    scopus 로고
    • Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases
    • Yoon, H.-J., Hashimoto, W., Miyake, O., Okamoto, M., Mikami, B., and Murata, K.: Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases. Protein Expr. Purif., 19, 84-90 (2000).
    • (2000) Protein Expr. Purif. , vol.19 , pp. 84-90
    • Yoon, H.-J.1    Hashimoto, W.2    Miyake, O.3    Okamoto, M.4    Mikami, B.5    Murata, K.6
  • 12
    • 0038532456 scopus 로고    scopus 로고
    • An exotype alginate lyase in Sphingomonas sp. A1: Overexpression in Escherichia coli, purification, and characterization of alginate lyase IV (A1-IV)
    • Miyake, O., Hashimoto, W., and Murata, K.: An exotype alginate lyase in Sphingomonas sp. A1: overexpression in Escherichia coli, purification, and characterization of alginate lyase IV (A1-IV). Protein Expr. Purif., 29, 33-41 (2003).
    • (2003) Protein Expr. Purif. , vol.29 , pp. 33-41
    • Miyake, O.1    Hashimoto, W.2    Murata, K.3
  • 13
    • 0033932250 scopus 로고    scopus 로고
    • A novel bacterial ATP-binding cassette transporter system that allows uptake of macromolecules
    • Momma, K., Okamoto, M., Mishima, Y., Mori, S., Hashimoto, W., and Murata, K.: A novel bacterial ATP-binding cassette transporter system that allows uptake of macromolecules. J. Bacteriol., 182, 3998-4004 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 3998-4004
    • Momma, K.1    Okamoto, M.2    Mishima, Y.3    Mori, S.4    Hashimoto, W.5    Murata, K.6
  • 14
    • 1942443159 scopus 로고    scopus 로고
    • Origin and diversity of alginate lyases of families PL-5 and -7 in Sphingomonas sp. strain A1
    • Miyake, O., Ochiai, A., Hashimoto, W., and Murata, K.: Origin and diversity of alginate lyases of families PL-5 and -7 in Sphingomonas sp. strain A1. J. Bacteriol., 186, 2891-2896 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 2891-2896
    • Miyake, O.1    Ochiai, A.2    Hashimoto, W.3    Murata, K.4
  • 15
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito, H. and Miura, K.: Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim. Biophys. Acta, 72, 619-629 (1963).
    • (1963) Biochim. Biophys. Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.2
  • 17
    • 78651113725 scopus 로고
    • The formation of 2-keto-3-deoxyheptonic acid in extracts of Escherichia coli B
    • Weissbach, A. and Hurwitz, J.: The formation of 2-keto-3-deoxyheptonic acid in extracts of Escherichia coli B. J. Biol. Chem., 234, 705-709 (1959).
    • (1959) J. Biol. Chem. , vol.234 , pp. 705-709
    • Weissbach, A.1    Hurwitz, J.2
  • 18
    • 0037604551 scopus 로고
    • Enzymes
    • Conn, E. E., Stumpe, P. K., Bruening, G., and Doi, R. H. (ed.) . John Wiley and Sons, New York
    • Conn, E. E., Stumpe, P. K., Bruening, G., and Doi, R. H.: Enzymes, p. 115-163. In Conn, E. E., Stumpe, P. K., Bruening, G., and Doi, R. H. (ed.), Outlines of biochemistry. John Wiley and Sons, New York (1987).
    • (1987) Outlines of Biochemistry , pp. 115-163
    • Conn, E.E.1    Stumpe, P.K.2    Bruening, G.3    Doi, R.H.4
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M.: A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 33947500127 scopus 로고
    • Thiobarbituric acid spray reagent for deoxy sugars and sialic acids
    • Warren, L.: Thiobarbituric acid spray reagent for deoxy sugars and sialic acids. Nature, 186, 237 (1960).
    • (1960) Nature , vol.186 , pp. 237
    • Warren, L.1
  • 22
    • 0029123664 scopus 로고
    • Effect of site-directed mutations on processing and activity of γ-glutamyltranspeptidase of Escherichia coli K-12
    • Hashimoto, W., Suzuki, H., Yamamoto, K., and Kumagai, H.: Effect of site-directed mutations on processing and activity of γ- glutamyltranspeptidase of Escherichia coli K-12. J. Biochem., 118, 75-80 (1995).
    • (1995) J. Biochem. , vol.118 , pp. 75-80
    • Hashimoto, W.1    Suzuki, H.2    Yamamoto, K.3    Kumagai, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.