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MeSH Review

Cellvibrio

 
 
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High impact information on Cellvibrio

  • The three-dimensional crystal structure of the catalytic module of a "family PL-10" polysaccharide lyase, Pel10Acm from Cellvibrio japonicus, solved at a resolution of 1.3 A, reveals a new polysaccharide lyase fold and is the first example of a polygalacturonic acid lyase that does not exhibit the "parallel beta-helix" topology [1].
  • Here we show that the X4 modules from a Cellvibrio japonicus mannanase (Man5C) and arabinofuranosidase (Abf62A) bind to polysaccharides, and thus these proteins comprise a new family of carbohydrate-binding modules (CBMs), designated CBM35 [2].
  • Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases [3].
  • The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants [4].
  • Purification and properties of Cellvibrio gilvus cellobiose phosphorylase [5].
 

Chemical compound and disease context of Cellvibrio

 

Gene context of Cellvibrio

  • In contrast, the beta-glucosidase from Cellvibrio gilvus is mesophilic (35 degrees C) and displays no such transglycosylation activity [11].
  • A gene encoding an exo-beta-glucosidase from Cellvibrio mixtus [12].
  • Possible roles for a non-modular, thermostable and proteinase-resistant cellulase from the mesophilic aerobic soil bacterium Cellvibrio mixtus [13].

References

  1. Convergent evolution sheds light on the anti-beta -elimination mechanism common to family 1 and 10 polysaccharide lyases. Charnock, S.J., Brown, I.E., Turkenburg, J.P., Black, G.W., Davies, G.J. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  2. X4 modules represent a new family of carbohydrate-binding modules that display novel properties. Bolam, D.N., Xie, H., Pell, G., Hogg, D., Galbraith, G., Henrissat, B., Gilbert, H.J. J. Biol. Chem. (2004) [Pubmed]
  3. Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases. Pell, G., Szabo, L., Charnock, S.J., Xie, H., Gloster, T.M., Davies, G.J., Gilbert, H.J. J. Biol. Chem. (2004) [Pubmed]
  4. The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants. Nagy, T., Nurizzo, D., Davies, G.J., Biely, P., Lakey, J.H., Bolam, D.N., Gilbert, H.J. J. Biol. Chem. (2003) [Pubmed]
  5. Purification and properties of Cellvibrio gilvus cellobiose phosphorylase. Sasaki, T., Tanaka, T., Nakagawa, S., Kainuma, K. Biochem. J. (1983) [Pubmed]
  6. Azospirillum irakense pectate lyase displays a toroidal fold. Novoa De Armas, H., Verboven, C., De Ranter, C., Desair, J., Vande Broek, A., Vanderleyden, J., Rabijns, A. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
  7. Cellulase induction and the use of cellulose as a preferred growth substrate by Cellvibrio gilvus. Breuil, C., Kushner, D.J. Can. J. Microbiol. (1976) [Pubmed]
  8. Optimum culture conditions for the epoxidation of cis-propenylphosphonate to fosfomycin by Cellvibrio gilvus. Aisaka, K., Ohshiro, T., Uwajima, T. Appl. Microbiol. Biotechnol. (1992) [Pubmed]
  9. A cellobiose phosphorylase from Cellvibrio gilvus recognizes only the beta-D-form of 5a-carba-glucopyranose. Kitaoka, M., Ogawa, S., Taniguchi, H. Carbohydr. Res. (1993) [Pubmed]
  10. Acceptor specificity of cellobiose phosphorylase from Cellvibrio gilvus: synthesis of three branched trisaccharides. Percy, A., Ono, H., Hayashi, K. Carbohydr. Res. (1998) [Pubmed]
  11. Enhancement of transglycosylation activity by construction of chimeras between mesophilic and thermophilic beta-glucosidase. Goyal, K., Jo Kim, B., Kim, J.D., Kim, Y.K., Kitaoka, M., Hayashi, K. Arch. Biochem. Biophys. (2002) [Pubmed]
  12. A gene encoding an exo-beta-glucosidase from Cellvibrio mixtus. Sakellaris, H., Manners, J.M., Pemberton, J.M. Curr. Microbiol. (1997) [Pubmed]
  13. Possible roles for a non-modular, thermostable and proteinase-resistant cellulase from the mesophilic aerobic soil bacterium Cellvibrio mixtus. Fontes, C.M., Clarke, J.H., Hazlewood, G.P., Fernandes, T.H., Gilbert, H.J., Ferreira, L.M. Appl. Microbiol. Biotechnol. (1997) [Pubmed]
 
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