The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

ECs4411  -  endo-1,4-D-glucanase

Escherichia coli O157:H7 str. Sakai

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of ECs4411

  • The out genes of the enterobacterial plant pathogen Erwinia chrysanthemi are responsible for the efficient extracellular secretion of multiple plant cell wall-degrading enzymes, including four isozymes of pectate lyase, exo-poly-alpha-D-galacturonosidase, pectin methylesterase, and cellulase [1].
  • The amino acid sequences of cellulase from Bacillus subtilis (BSC) and that from an alkalophilic Bacillus sp. N-4 (NK1) show significant homology in most parts except for the C-terminal portions [2].
  • In this study, we enhanced the thermostability of endoglucanase EngB, one component of the cellulase complex (cellulosome) from Clostridium cellulovorans, by the directed evolution technique [3].
  • Conserved serine-rich sequences in xylanase and cellulase from Pseudomonas fluorescens subspecies cellulosa: internal signal sequence and unusual protein processing [4].
  • The gene encoding the cellulase (Avicelase) Cel1 from Streptomyces reticuli and analysis of protein domains [5].
 

High impact information on ECs4411

 

Chemical compound and disease context of ECs4411

 

Biological context of ECs4411

  • CenA is a bacterial cellulase (beta-1,4-glucanase) comprised of a globular catalytic domain joined to an extended cellulose-binding domain (CBD) by a short linker peptide [13].
  • A flexible linker, modeled after a secreted fungal cellulase protein, was incorporated as the interdomain linker covalently joining the two active sites [14].
  • The substrate specificity and substrate competition pattern of the purified recombinant cellulase were the same as those of the purified cellulase from Bacillus sp. D04 [7].
  • We have cloned a region involved in pectate lyase and cellulase secretion by complementation of non-secretory outJ mutants of E. chrysanthemi strain 3937 using the RP4::miniMu plasmid pULB110 [15].
  • Insertion mutagenesis of the cloned region and recombination of the corresponding mutations in the bacterial chromosome by marker exchange revealed the existence of two divergently transcribed genes, pecS and pecM, that are both involved in the pectate lyase and cellulase regulation [16].
 

Anatomical context of ECs4411

 

Associations of ECs4411 with chemical compounds

  • This gene produces a thermostable cellulase that shows both endoglucanase and exoglucanase activities on test substrates and is able to degrade crystalline cellulose to glucose [21].
  • Two of these strains were used with commercial cellulase to ferment mixed-waste office paper to ethanol [22].
  • The extracellular cellulase preparation from C. acetobutylicum BKW-1 has a specific activity towards CMC which is more than fourfold that present in C. acetobutylicum ATCC 824 [23].
  • The two 88K CMCase open reading frames had enough DNA to produce a protein of 106K, but the mobility of the enzyme in sodium dodecyl sulfate gels gave a value which was 20% lower [24].
  • In the present study, we demonstrate that a low but significant level of induction of cellulase activity occurs during growth on xylose or lichenan [25].
 

Analytical, diagnostic and therapeutic context of ECs4411

References

  1. Cloned Erwinia chrysanthemi out genes enable Escherichia coli to selectively secrete a diverse family of heterologous proteins to its milieu. He, S.Y., Lindeberg, M., Chatterjee, A.K., Collmer, A. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  2. Construction and characterization of the chimeric enzymes between the Bacillus subtilis cellulase and an alkalophilic Bacillus cellulase. Nakamura, A., Fukumori, F., Horinouchi, S., Masaki, H., Kudo, T., Uozumi, T., Horikoshi, K., Beppu, T. J. Biol. Chem. (1991) [Pubmed]
  3. Thermostabilization of cellulosomal endoglucanase EngB from Clostridium cellulovorans by in vitro DNA recombination with non-cellulosomal endoglucanase EngD. Murashima, K., Kosugi, A., Doi, R.H. Mol. Microbiol. (2002) [Pubmed]
  4. Conserved serine-rich sequences in xylanase and cellulase from Pseudomonas fluorescens subspecies cellulosa: internal signal sequence and unusual protein processing. Hall, J., Hazlewood, G.P., Huskisson, N.S., Durrant, A.J., Gilbert, H.J. Mol. Microbiol. (1989) [Pubmed]
  5. The gene encoding the cellulase (Avicelase) Cel1 from Streptomyces reticuli and analysis of protein domains. Schlochtermeier, A., Walter, S., Schröder, J., Moorman, M., Schrempf, H. Mol. Microbiol. (1992) [Pubmed]
  6. ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Trichoderma reesei. Aro, N., Saloheimo, A., Ilmén, M., Penttilä, M. J. Biol. Chem. (2001) [Pubmed]
  7. Characterization of a bifunctional cellulase and its structural gene. The cell gene of Bacillus sp. D04 has exo- and endoglucanase activity. Han, S.J., Yoo, Y.J., Kang, H.S. J. Biol. Chem. (1995) [Pubmed]
  8. Enhancement of expression and apparent secretion of Erwinia chrysanthemi endoglucanase (encoded by celZ) in Escherichia coli B. Zhou, S., Yomano, L.P., Saleh, A.Z., Davis, F.C., Aldrich, H.C., Ingram, L.O. Appl. Environ. Microbiol. (1999) [Pubmed]
  9. Overproduction from a cellulase gene with a high guanosine-plus-cytosine content in Escherichia coli. O'Neill, G.P., Kilburn, D.G., Warren, R.A., Miller, R.C. Appl. Environ. Microbiol. (1986) [Pubmed]
  10. The processive endocellulase CelF, a major component of the Clostridium cellulolyticum cellulosome: purification and characterization of the recombinant form. Reverbel-Leroy, C., Pages, S., Belaich, A., Belaich, J.P., Tardif, C. J. Bacteriol. (1997) [Pubmed]
  11. Purification and characterization of a cellulase from the ruminal fungus Orpinomyces joyonii cloned in Escherichia coli. Ye, X.Y., Ng, T.B., Cheng, K.J. Int. J. Biochem. Cell Biol. (2001) [Pubmed]
  12. Evidence for multiple carboxymethylcellulase genes in Pseudomonas fluorescens subsp. cellulosa. Gilbert, H.J., Jenkins, G., Sullivan, D.A., Hall, J. Mol. Gen. Genet. (1987) [Pubmed]
  13. The adsorption of a bacterial cellulase and its two isolated domains to crystalline cellulose. Gilkes, N.R., Jervis, E., Henrissat, B., Tekant, B., Miller, R.C., Warren, R.A., Kilburn, D.G. J. Biol. Chem. (1992) [Pubmed]
  14. Construction, expression, and activity of a bivalent bispecific single-chain antibody. Mallender, W.D., Voss, E.W. J. Biol. Chem. (1994) [Pubmed]
  15. Molecular cloning of the outJ gene involved in pectate lyase secretion by Erwinia chrysanthemi. Ji, J., Hugouvieux-Cotte-Pattat, N., Robert-Baudouy, J. Mol. Microbiol. (1989) [Pubmed]
  16. pecS: a locus controlling pectinase, cellulase and blue pigment production in Erwinia chrysanthemi. Reverchon, S., Nasser, W., Robert-Baudouy, J. Mol. Microbiol. (1994) [Pubmed]
  17. Characterization of transposon insertion out- mutants of Erwinia carotovora subsp. carotovora defective in enzyme export and of a DNA segment that complements out mutations in E. carotovora subsp. carotovora, E. carotovora subsp. atroseptica, and Erwinia chrysanthemi. Murata, H., Fons, M., Chatterjee, A., Collmer, A., Chatterjee, A.K. J. Bacteriol. (1990) [Pubmed]
  18. Cloning of the Escherichia coli endo-1,4-D-glucanase gene and identification of its product. Park, Y.W., Yun, H.D. Mol. Gen. Genet. (1999) [Pubmed]
  19. Transformation of Pythium aphanidermatum to geneticin resistance. Weiland, J.J. Curr. Genet. (2003) [Pubmed]
  20. The resistance of cellulases and xylanases to proteolytic inactivation. Fontes, C.M., Hall, J., Hirst, B.H., Hazlewood, G.P., Gilbert, H.J. Appl. Microbiol. Biotechnol. (1995) [Pubmed]
  21. celB, a gene coding for a bifunctional cellulase from the extreme thermophile "Caldocellum saccharolyticum". Saul, D.J., Williams, L.C., Grayling, R.A., Chamley, L.W., Love, D.R., Bergquist, P.L. Appl. Environ. Microbiol. (1990) [Pubmed]
  22. Isolation and molecular characterization of high-performance cellobiose-fermenting spontaneous mutants of ethanologenic Escherichia coli KO11 containing the Klebsiella oxytoca casAB operon. Moniruzzaman, M., Lai, X., York, S.W., Ingram, L.O. Appl. Environ. Microbiol. (1997) [Pubmed]
  23. Heterologous expression of endo-beta-1,4-D-glucanase from Clostridium cellulovorans in Clostridium acetobutylicum ATCC 824 following transformation of the engB gene. Kim, A.Y., Attwood, G.T., Holt, S.M., White, B.A., Blaschek, H.P. Appl. Environ. Microbiol. (1994) [Pubmed]
  24. A Bacteroides ruminicola 1,4-beta-D-endoglucanase is encoded in two reading frames. Matsushita, O., Russell, J.B., Wilson, D.B. J. Bacteriol. (1991) [Pubmed]
  25. Substrate-induced production and secretion of cellulases by Clostridium acetobutylicum. López-Contreras, A.M., Gabor, K., Martens, A.A., Renckens, B.A., Claassen, P.A., Van Der Oost, J., De Vos, W.M. Appl. Environ. Microbiol. (2004) [Pubmed]
  26. Molecular cloning and characterization of a cellulase gene from a symbiotic protist of the lower termite, Coptotermes formosanus. Inoue, T., Moriya, S., Ohkuma, M., Kudo, T. Gene (2005) [Pubmed]
  27. Bacterial cell surface display of an enzyme library for selective screening of improved cellulase variants. Kim, Y.S., Jung, H.C., Pan, J.G. Appl. Environ. Microbiol. (2000) [Pubmed]
  28. Cloning and sequencing of a Bacteroides ruminicola B(1)4 endoglucanase gene. Matsushita, O., Russell, J.B., Wilson, D.B. J. Bacteriol. (1990) [Pubmed]
  29. Cloning and sequence analysis of a new cellulase gene encoding CelK, a major cellulosome component of Clostridium thermocellum: evidence for gene duplication and recombination. Kataeva, I., Li, X.L., Chen, H., Choi, S.K., Ljungdahl, L.G. J. Bacteriol. (1999) [Pubmed]
  30. Characterization of a Neocallimastix patriciarum cellulase cDNA (celA) homologous to Trichoderma reesei cellobiohydrolase II. Denman, S., Xue, G.P., Patel, B. Appl. Environ. Microbiol. (1996) [Pubmed]
 
WikiGenes - Universities