메뉴 건너뛰기




Volumn 4, Issue 6, 2000, Pages 377-383

Highly alkaline pectate lyase Pel-4A from alkaliphilic Bacillus sp. strain P-4-N: Its catalytic properties and deduced amino acid sequence

Author keywords

Alkaliphile; Bacillus; Cloning; Pectate lyase; Salt dependency

Indexed keywords

DNA; PECTATE LYASE; POLYSACCHARIDE LYASE; RECOMBINANT PROTEIN;

EID: 0034571727     PISSN: 14310651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007920070008     Document Type: Article
Times cited : (17)

References (27)
  • 2
    • 0034008851 scopus 로고    scopus 로고
    • Deduced amino-acid sequence and possible catalytic residues of a novel pectate lyase from an alkaliphilic strain of Bacillus
    • Hatada Y, Saito K, Koike K, Yoshimatsu T, Ozawa T, Kobayashi T, Ito S (2000) Deduced amino-acid sequence and possible catalytic residues of a novel pectate lyase from an alkaliphilic strain of Bacillus. Eur J Biochem 267:2268-2275
    • (2000) Eur J Biochem , vol.267 , pp. 2268-2275
    • Hatada, Y.1    Saito, K.2    Koike, K.3    Yoshimatsu, T.4    Ozawa, T.5    Kobayashi, T.6    Ito, S.7
  • 5
    • 0032995005 scopus 로고    scopus 로고
    • Production of highly efficient enzymes for flax retting by Rhizomucor pusillus
    • Henriksson G, Akin DE, Slomczynski D, Eriksson K-EL (1999) Production of highly efficient enzymes for flax retting by Rhizomucor pusillus. J Biotechnol 68:115-123
    • (1999) J Biotechnol , vol.68 , pp. 115-123
    • Henriksson, G.1    Akin, D.E.2    Slomczynski, D.3    Eriksson, K.-E.L.4
  • 6
    • 0029257437 scopus 로고
    • Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfiamily
    • Henrissat B, Heffron SE, Yoder MD, Lietzke SE, Jurnak F (1995) Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfiamily. Plant Physiol 107:963-976
    • (1995) Plant Physiol , vol.107 , pp. 963-976
    • Henrissat, B.1    Heffron, S.E.2    Yoder, M.D.3    Lietzke, S.E.4    Jurnak, F.5
  • 7
    • 0000156727 scopus 로고
    • Production of alkaline enzymes by alkalophilic microorganisms. Part III. Alkaline pectinase of Bacillus no. P-4-N
    • Horikoshi K (1972) Production of alkaline enzymes by alkalophilic microorganisms. Part III. Alkaline pectinase of Bacillus no. P-4-N. Agric Biol Chem 36:285-293
    • (1972) Agric Biol Chem , vol.36 , pp. 285-293
    • Horikoshi, K.1
  • 8
    • 0032712358 scopus 로고    scopus 로고
    • Alkaliphiles; some applications of their products for biotechnology
    • Horikoshi K (1999) Alkaliphiles; some applications of their products for biotechnology. Microbiol Mol Biol Rev 63:735-750
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 735-750
    • Horikoshi, K.1
  • 9
    • 84996335527 scopus 로고
    • New shuttle vectors for Escherichia coli and Bacillus subtilis. IV. The nucleotide sequence of pHY300PLK and some properties in relation to transformation
    • Ishiwa H, Shibahara-Sone H (1986) New shuttle vectors for Escherichia coli and Bacillus subtilis. IV. The nucleotide sequence of pHY300PLK and some properties in relation to transformation. Jpn J Genet 61:515-528
    • (1986) Jpn J Genet , vol.61 , pp. 515-528
    • Ishiwa, H.1    Shibahara-Sone, H.2
  • 10
    • 0023036933 scopus 로고
    • Structure of two pectate lyase genes from Envinia chrysanthemi EC16 and their high-level expression in Escherichia coli
    • Keen NT, Tamaki S (1986) Structure of two pectate lyase genes from Envinia chrysanthemi EC16 and their high-level expression in Escherichia coli. J Bacteriol 168:595-606
    • (1986) J Bacteriol , vol.168 , pp. 595-606
    • Keen, N.T.1    Tamaki, S.2
  • 11
    • 0029861087 scopus 로고    scopus 로고
    • Differential effect of site-directed mutations in pelC on pectate lyase activity, plant tissue maceration, and elicitor activity
    • Kita N, Boyd CM, Garrett MR, Jurnak F, Keen NT (1996) Differential effect of site-directed mutations in pelC on pectate lyase activity, plant tissue maceration, and elicitor activity. J Biol Chem 271:26529-26535
    • (1996) J Biol Chem , vol.271 , pp. 26529-26535
    • Kita, N.1    Boyd, C.M.2    Garrett, M.R.3    Jurnak, F.4    Keen, N.T.5
  • 12
    • 0032908426 scopus 로고    scopus 로고
    • Enzymatic properties and deduced amino acid sequence of a high-alkaline pectate lyase from an alkaliphilic Bacillus isolate
    • Kobayashi T, Hatada Y, Higaki N, Lusterio DD, Ozawa T, Koike K, Kawai S, Ito S (1999) Enzymatic properties and deduced amino acid sequence of a high-alkaline pectate lyase from an alkaliphilic Bacillus isolate. Biochim Biophys Acta 1427:145-154
    • (1999) Biochim Biophys Acta , vol.1427 , pp. 145-154
    • Kobayashi, T.1    Hatada, Y.2    Higaki, N.3    Lusterio, D.D.4    Ozawa, T.5    Koike, K.6    Kawai, S.7    Ito, S.8
  • 13
    • 0026887880 scopus 로고
    • Cloning and characterization of a pectate lyase gene from the soft-rotting bacterium Pseudomonas viridiflava
    • Liao C-H, Sasaki K, Nagahashi G, Hicks KB (1992) Cloning and characterization of a pectate lyase gene from the soft-rotting bacterium Pseudomonas viridiflava. Mol Plant-Microbe Interact 5:301-308
    • (1992) Mol Plant-Microbe Interact , vol.5 , pp. 301-308
    • Liao, C.-H.1    Sasaki, K.2    Nagahashi, G.3    Hicks, K.B.4
  • 14
    • 0028191528 scopus 로고
    • The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi
    • Lietzke SE, Yoder MD, Keen NT, Jurnak F (1994) The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi. Plant Physiol 106:849-862
    • (1994) Plant Physiol , vol.106 , pp. 849-862
    • Lietzke, S.E.1    Yoder, M.D.2    Keen, N.T.3    Jurnak, F.4
  • 15
    • 0041894256 scopus 로고    scopus 로고
    • Characterization of a fungal amylase from Mucor sp. associated with the marine sponge Spirastrella sp
    • Mohapatra BR, Banerjee UC, Bapuji M (1998) Characterization of a fungal amylase from Mucor sp. associated with the marine sponge Spirastrella sp. J Biotechnol 60:113-117
    • (1998) J Biotechnol , vol.60 , pp. 113-117
    • Mohapatra, B.R.1    Banerjee, U.C.2    Bapuji, M.3
  • 17
    • 0027360579 scopus 로고
    • Pectate lyase from Bacillus subtilis: Molecular characterization of the gene, and properties of the cloned enzyme
    • Nasser W, Awadé AC, Reverchon S, Robert-Baudouy J (1993) Pectate lyase from Bacillus subtilis: molecular characterization of the gene, and properties of the cloned enzyme. FEBS Lett 335:319-326
    • (1993) FEBS Lett , vol.335 , pp. 319-326
    • Nasser, W.1    Awadé, A.C.2    Reverchon, S.3    Robert-Baudouy, J.4
  • 18
    • 0034200611 scopus 로고    scopus 로고
    • A new high-alkaline and high-molecular-weight pectate lyase from a Bacillus isolate: Enzymatic properties and cloning of the gene for the enzyme
    • Ogawa A, Sawada K, Saito K, Hakamada Y, Sumitomo N, Hatada Y, Kobayashi T, Ito S (2000) A new high-alkaline and high-molecular-weight pectate lyase from a Bacillus isolate: enzymatic properties and cloning of the gene for the enzyme. Biosci Biotechnol Biochem 64:1133-1141
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1133-1141
    • Ogawa, A.1    Sawada, K.2    Saito, K.3    Hakamada, Y.4    Sumitomo, N.5    Hatada, Y.6    Kobayashi, T.7    Ito, S.8
  • 20
    • 0024790115 scopus 로고
    • Nucleotide sequences of the Erwinia chrysanthemi ogl and pelE genes negatively regulated by the kdgR gene product
    • Amst
    • Reverchon S, Huang Y, Bourson C, Robert-Baudouy J (1989) Nucleotide sequences of the Erwinia chrysanthemi ogl and pelE genes negatively regulated by the kdgR gene product. Gene (Amst) 85:125-134
    • (1989) Gene , vol.85 , pp. 125-134
    • Reverchon, S.1    Huang, Y.2    Bourson, C.3    Robert-Baudouy, J.4
  • 21
    • 0001333801 scopus 로고
    • Pectic enzymes
    • Rose AH (ed) Academic Press, London
    • Rombouts FM, Pilnik W (1980) Pectic enzymes. In: Rose AH (ed) Economic microbiology, vol 5. Academic Press, London, pp 227-282
    • (1980) Economic Microbiology , vol.5 , pp. 227-282
    • Rombouts, F.M.1    Pilnik, W.2
  • 22
    • 0034097684 scopus 로고    scopus 로고
    • Nucleotide and amino-acid sequences of a new-type pectate lyase from an alkaliphilic strain of Bacillus
    • Sawada K, Ogawa A, Ozawa T, Sumitomo N, Hatada Y, Kobayashi T, Ito S (2000) Nucleotide and amino-acid sequences of a new-type pectate lyase from an alkaliphilic strain of Bacillus. Eur J Biochem 267:1510-1515
    • (2000) Eur J Biochem , vol.267 , pp. 1510-1515
    • Sawada, K.1    Ogawa, A.2    Ozawa, T.3    Sumitomo, N.4    Hatada, Y.5    Kobayashi, T.6    Ito, S.7
  • 24
    • 0027401020 scopus 로고
    • Protein secretion in Bacillus species
    • Simonen M, Palva I (1993) Protein secretion in Bacillus species. Microbiol Rev 57:109-137
    • (1993) Microbiol Rev , vol.57 , pp. 109-137
    • Simonen, M.1    Palva, I.2
  • 25
    • 0024060080 scopus 로고
    • Structure and organization of the pel genes from Erwinia chrysanthemi EC16
    • Tamaki SJ, Gold S, Robeson M, Manulis S, Keen NT (1988) Structure and organization of the pel genes from Erwinia chrysanthemi EC16. J Bacteriol 170:3468-3478
    • (1988) J Bacteriol , vol.170 , pp. 3468-3478
    • Tamaki, S.J.1    Gold, S.2    Robeson, M.3    Manulis, S.4    Keen, N.T.5
  • 26
    • 0030944441 scopus 로고    scopus 로고
    • Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: Enzyme characteristics and potential inhibitors
    • Tardy F, Nasser W, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N (1997) Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: enzyme characteristics and potential inhibitors. J Bacteriol 179:2503-2511
    • (1997) J Bacteriol , vol.179 , pp. 2503-2511
    • Tardy, F.1    Nasser, W.2    Robert-Baudouy, J.3    Hugouvieux-Cotte-Pattat, N.4
  • 27
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder MD, Keen NT, Jurnak F (1993) New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science 260:1503-1507
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.