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Erwinia carotovora

By separation Irom bacterial culture such as Escherichia coli, Serratia marcescens, Erwinia aroideae, Erwinia atroseptica, Erwinia carotovora. [Pg.139]

L-Asparaginase, an enzyme derived from E. coli or Erwinia carotovora, has been employed in cancer chemotherapy where its selectivity depends upon the essential requirement of some tumours for the amino acid L-asparagine. Normal tissues do not require this amino acid and thus the enzyme is administered with the intention of depleting tumour cells of asparagine by converting it to aspartic acid and ammonia. Whilst L-asparaginase showed promise in a variety of experimentally induced tumours, it is only useful in humans for the treatment of acute lymphoblastic leukaemia, although it is sometimes used for myeloid leukaemia. [Pg.476]

Wegener, C., Bartling, S., Olsen, O., Thomsen, K.K., Bahlow, R. and von Wettstein, D. Differences in cell wall degradation patterns by Erwinia carotovora pectate lyase isoenzymes. Submitted to Protoplasma. [Pg.292]

Ried, J. L. and Collmer, A. (1986). Comparison of pectic enzymes produced by Erwinia chrysanthemi, Erwinia carotovora subsp. carotovora, and Erwinia carotovora subsp. atroseptica. AppI Environ Microbiol 52, 305-310. [Pg.292]

Recently, a new pectate lyase gene pelZ, was identified at the vicinity of the pelB-pelC cluster (Pissavin et al, submitted). ApelZ homologue was also foimd in Erwinia carotovora. PelZ defines a new family of endo-pectate lyase since its amino acid sequence displays only very low homology with that of other pectinases. [Pg.316]

Wegener C, Battling S, Olsen O, Thomsen KK, Bahlow R, von Wettstein D (1995) Differences in cell wall degradation by Erwinia carotovora pectate lyase isoenzymes. Prep, for publication. [Pg.396]

Heikinheimo R, Flego D, Pirhonen M, Karlsson M-B, Eriksson A, Mae A, Koiv V, Palva ET (1995) Characterization of a novel pectate lyase from Erwinia carotovora subsp, carotovora. Mol Plant Mlcrob Interact 8 207-217... [Pg.396]

Weber J, Wegener C (1986) Virulence and enzyme production of Erwinia carotovora ssp. atroseptica on potato tuber tissue. J Phytopathol 117 97-106... [Pg.397]

Yang Z, Cramer CL, Lacy GH (1992) Erwinia carotovora subsp. carotovora pectic enzymes In planta gene activation and roles in soft rot pathogenesis. Mol Plant-Microbe Interact 5 104-112... [Pg.397]

A. Chatterjee, Y. Cui, Y. Liu, C. K. Dumenyo, A. K. Chatterjee, Inactivation of rsmA leads to overproduction of extracellular pectinases, cellula.ses, and proteases in Erwinia carotovora subsp. carotovora in the absence of the starvation/cell densitysensing signal, N-(3-oxohexanoyl)-L-homoserine lactone. AppL Environ. Microbiol. 6/ 1959 (1995). [Pg.16]

H. Murata, J. L. McEvoy, A. Chatterjee, A. Collmer, A. K. Chatterjee. Molecular cloning of an aepA gene that activates production of extracellular pectolytic, cellulolytic, and proteolytic enzymes in Erwinia carotovora subsp. carotovora. Mol. Plant Micr. Interact. 4 239 (1991). [Pg.16]

Cladera-Olivera F, Caron GR, Motta AS, Souto AA and Brandelli A. 2006. Bacteriocin-like substance inhibits potato soft rot caused by Erwinia carotovora. Can J Microbiol 52(6) 533-539. [Pg.352]

Quevillon-Cheruel S, Leulliot N, Acosta Muniz C, Vincent M, Gallay J, Argentini M, Cornu D, Boccard F, Lemaitre B and van Tilbeurgh H. 2009. EVF, a virulence factor produced by the Drosophila pathogen Erwinia carotovora is a S-palmitoylated protein with a new fold that binds to lipid vesicles. J Biol Chem. 284(6) 3552-3562. [Pg.354]

Action pattern A was observed with extracellular, endopectate lyase of Bacillus polymyxa,4,240 with extra- and intra-cellular lyase of Erwinia carotovora,241 with extracellular enzyme of Xanthomonas campestris,23S and with lyase produced by Bacteroides ruminicola242 isolated from the rumen fluid of sheep.243... [Pg.373]

The signal molecule, 30,C6-HSL and number of its analogues, with variations in the acyl chain and the hetero-ring, have been prepared [15,56,57] to investigate the mechanism of induction of carbapenem and luminescence in Erwinia carotovora and V.fischeri respectively. Essentially, the acylation of l-HSL with 3-oxoalkanoic acid by the same method as outlined for the preparation of AT-acyl-L-HSL delivers the desired derivatives. However, as the p-keto acids are thermally labile, these were prepared from the corresponding p-keto ester after the initial protection of the p-keto function as ethylene glycol ketal (route a, Scheme 6). [Pg.305]

Ishimaru CA, Loper JE (1992) High-Affinity Iron Uptake Systems Present in Erwinia carotovora subsp. carotovora Include the Hydroxamate Siderophore Aerobactin. J Bacteriol 174 2993... [Pg.62]

MeGuire, R. G., Kelman, A. (1986). Calcium in potato tuber cell walls in relation to tissue maceration by Erwinia carotovora pv. atroseptica. Phytopathol., 76,401 06. [Pg.122]

Asparaginases with antilymphoma activity have also been found in extracts of Serratia marcescens (35-37), Erwinia carotovora (38), and Proteus vulgaris (36). Escherichia coli extracts contain a second asparaginase that is devoid of antilymphoma activity (39), and a similarly inactive enzyme has been found in a fungus, Fusarium tricinctum (40). An enzyme from Streptomyces griseus has L-asparaginase activity when assayed in tris-Cl (pH 8.6) but little or no activity in sodium borate (pH... [Pg.104]


See other pages where Erwinia carotovora is mentioned: [Pg.283]    [Pg.283]    [Pg.292]    [Pg.344]    [Pg.385]    [Pg.385]    [Pg.661]    [Pg.842]    [Pg.11]    [Pg.347]    [Pg.375]    [Pg.378]    [Pg.62]    [Pg.218]    [Pg.228]    [Pg.260]    [Pg.296]    [Pg.31]    [Pg.649]    [Pg.106]    [Pg.152]    [Pg.350]    [Pg.363]    [Pg.1555]    [Pg.394]    [Pg.420]    [Pg.426]   
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