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Volumn 1804, Issue 9, 2010, Pages 1925-1936

Molecular identification of unsaturated uronate reductase prerequisite for alginate metabolism in Sphingomonas sp. A1

Author keywords

2 Keto 3 deoxy d gluconic acid; Alginate; Crystal structure; Short chain dehydrogenase reductase; Sphingomonas

Indexed keywords

4 DEOXY LEVO ERYTHRO 5 HEXOSEULOSE URONIC ACID; ALGINIC ACID; ARGININE; GLYCINE; HYALURONIC ACID DERIVATIVE; LYSINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SERINE; TYROSINE; UNCLASSIFIED DRUG; ALDEHYDE DEHYDROGENASE; GLUCONIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; POLY(BETA-D-MANNURONATE) LYASE; POLYSACCHARIDE LYASE; RECOMBINANT PROTEIN; URONATE DEHYDROGENASE;

EID: 77955093827     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.05.010     Document Type: Article
Times cited : (66)

References (35)
  • 2
    • 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., Murata K. Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases. Protein Expr. Purif. 2000, 19:84-90.
    • (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
  • 3
    • 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., 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. 2000, 182:4572-4577.
    • (2000) J. Bacteriol. , vol.182 , pp. 4572-4577
    • Hashimoto, W.1    Miyake, O.2    Momma, K.3    Kawai, S.4    Murata, K.5
  • 4
    • 73849154299 scopus 로고
    • Alginic acid metabolism in bacteria: I. Enzymatic formation of unsaturated oligosaccharides and 4-deoxy-L-erythro-5-hexoseulose uronic acid
    • Preiss J., Ashwell G. Alginic acid metabolism in bacteria: I. Enzymatic formation of unsaturated oligosaccharides and 4-deoxy-L-erythro-5-hexoseulose uronic acid. J. Biol. Chem. 1962, 237:317-321.
    • (1962) J. Biol. Chem. , vol.237 , pp. 317-321
    • Preiss, J.1    Ashwell, G.2
  • 5
    • 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., 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. 2003, 29:33-41.
    • (2003) Protein Expr. Purif. , vol.29 , pp. 33-41
    • Miyake, O.1    Hashimoto, W.2    Murata, K.3
  • 6
    • 33747181070 scopus 로고    scopus 로고
    • A biosystem for alginate metabolism in Agrobacterium tumefaciens strain C58: molecular identification of Atu3025 as an exotype family PL-15 alginate lyase
    • Ochiai A., Hashimoto W., Murata K. A biosystem for alginate metabolism in Agrobacterium tumefaciens strain C58: molecular identification of Atu3025 as an exotype family PL-15 alginate lyase. Res. Microbiol. 2006, 157:642-649.
    • (2006) Res. Microbiol. , vol.157 , pp. 642-649
    • Ochiai, A.1    Hashimoto, W.2    Murata, K.3
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 20444407677 scopus 로고    scopus 로고
    • Structure and function of bacterial super-biosystem responsible for import and depolymerization of macromolecules
    • Hashimoto W., Momma K., Maruyama Y., Yamasaki M., Mikami B., Murata K. Structure and function of bacterial super-biosystem responsible for import and depolymerization of macromolecules. Biosci. Biotechnol. Biochem. 2005, 69:673-692.
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 673-692
    • Hashimoto, W.1    Momma, K.2    Maruyama, Y.3    Yamasaki, M.4    Mikami, B.5    Murata, K.6
  • 11
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 14
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Meth. Enzymol. 1997, 276:307-326.
    • (1997) Meth. Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D. Biol. Crystallogr. 1994, 50:760-763.
    • (1994) Acta Crystallogr. Sect. D. Biol. Crystallogr. , vol.50 , pp. 760-763
  • 20
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. Sect. A 1976, 32:922-923.
    • (1976) Acta Crystallogr. Sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 23
    • 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 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 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., Hisano T., Momma K., Murata K. Sphingomonas sp. A1 lyase active on both poly-βbet-D-mannuronate and heteropolymeric regions in alginate. J. Ferment. Bioeng. 1998, 86:236-238.
    • (1998) J. Ferment. Bioeng. , vol.86 , pp. 236-238
    • Hashimoto, W.1    Okamoto, M.2    Hisano, T.3    Momma, K.4    Murata, K.5
  • 26
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallogr. 1952, 5:802-810.
    • (1952) Acta Crystallogr. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 29
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann M.G., Moras D., Olsen K.W. Chemical and biological evolution of nucleotide-binding protein. Nature 1974, 250:194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 31
    • 0000070863 scopus 로고
    • Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type
    • Jornvall H., Persson M., Jeffery J. Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Proc. Natl. Acad. Sci. U. S. A. 1981, 78:4226-4230.
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 4226-4230
    • Jornvall, H.1    Persson, M.2    Jeffery, J.3
  • 33
    • 0037324955 scopus 로고    scopus 로고
    • Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs)
    • Persson B., Kallberg Y., Oppermann U., Jörnvall H. Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem. Biol. Interact. 2003, 143-144:271-278.
    • (2003) Chem. Biol. Interact. , pp. 271-278
    • Persson, B.1    Kallberg, Y.2    Oppermann, U.3    Jörnvall, H.4
  • 34
    • 0029683826 scopus 로고    scopus 로고
    • Involvement of two basic residues (Lys-17 and Arg-39) of mouse lung carbonyl reductase in NADP(H)-binding and fatty acid activation: site-directed mutagenesis and kinetic analyses
    • Nakanishi M., Kakumoto M., Matsuura K., Deyashiki Y., Tanaka N., Nonaka T., Mitsui Y., Hara A. Involvement of two basic residues (Lys-17 and Arg-39) of mouse lung carbonyl reductase in NADP(H)-binding and fatty acid activation: site-directed mutagenesis and kinetic analyses. J. Biochem. (Tokyo) 1996, 120:257-263.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 257-263
    • Nakanishi, M.1    Kakumoto, M.2    Matsuura, K.3    Deyashiki, Y.4    Tanaka, N.5    Nonaka, T.6    Mitsui, Y.7    Hara, A.8
  • 35
    • 0029643855 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8Å resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family
    • Tanaka N., Nonaka T., Nakanishi M., Deyashiki Y., Hara A., Mitsui Y. Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8Å resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family. Structure 1996, 4:33-45.
    • (1996) Structure , vol.4 , pp. 33-45
    • Tanaka, N.1    Nonaka, T.2    Nakanishi, M.3    Deyashiki, Y.4    Hara, A.5    Mitsui, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.