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Erwinia chrysanthemi

Fig. 17.6. Experimental configuration for the integrated, primary purification of intracellular proteins from unclarified disruptates. Panel A configuration employed for the purification of G3PDH from baker s yeast. Elution was performed in packed bed mode under reversed flow. Panel B configuration for loading, wash and elution in fluidised bed mode (employed for the purification of L-asparaginase from Erwinia chrysanthemi). Fig. 17.6. Experimental configuration for the integrated, primary purification of intracellular proteins from unclarified disruptates. Panel A configuration employed for the purification of G3PDH from baker s yeast. Elution was performed in packed bed mode under reversed flow. Panel B configuration for loading, wash and elution in fluidised bed mode (employed for the purification of L-asparaginase from Erwinia chrysanthemi).
Nasser, W., Reverchon, S., Condemine, G. and Robert-Baudouy, J. (1994). Specific interactions of Erwinia chrysanthemi KdgR repressor with different operators of genes involved in pectinolysis. J Mol Biol 236, 427-440. [Pg.292]

Hugouvieux-Cotte-Pattat, N. and Robert-Baudouy, J. (1992). Analysis of the regulation of the pel BC genes in Erwinia chrysanthemi 3937. Mol Microbiol 6, 2363-2376. [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]

Lietzke, S.E., Yoder, M.D., Keen, N.T. and Jurnak, F. (1994) The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi. Plant Physiol Q6, 849-862. [Pg.292]

Pitkanen, K., Heikinheimo, R. and Pakkanen, R. (1992) Purification and characterization of Erwinia chrysanthemi B374 pectin methylesterase produced by Bacillus subtilis. Enzyme Microb TechnoHA, 832-836. [Pg.292]

Erwinia chrysanthemi synthesizes and secretes a large number of pectinases. The major pectinases include a pectin methylesterase PemA and five isoenzymes of endo-pectate lyases PelA, PelB, PelC, PelD and PelE. In addition, secondary pectinases were identified a pectin methylesterase PemB, two endo-pectate lyases PelL and PelZ, an exo-pectate lyase PelX and an exopolygalacturonase, PehX. The regulation of pectinase synthesis is very complex and dependent on many environmental conditions. It is induced by pectin catabolic products and affected by growth phase, catabolite repression, osmolarity, iron or oxygen starvation... [Pg.311]

Preston JF, Rice JD, Ingram LO, Keen NT (1992) Differential depolymerization mechanism of pectate lyase secreted by Erwinia chrysanthemi EC 16. J Bacteriol 174 2039-2042... [Pg.396]

Collmer A, Batemann DF (1982) Regulation of extracellular pectate lyase in Erwinia chrysanthemi. evidence that reaction products of pectate lyase and exo-poly-a-D-galacturonase mediate induction on galacturonan. Physiol Plant Pathol 21 127-139... [Pg.396]

Identification of a seventh endo-pectate lyase of the phytopathogenic bacterium Erwinia chrysanthemi... [Pg.831]

Pectin methylesterase B of Erwinia chrysanthemi, the first pectinase characterise(l as a membrane lipoprotein. [Pg.837]

Synthesis of New Methyl Esters of 3-Deoxy-D- ry /rro-2-hexulosonic acid (KDG) analogs, inducers of the Expression of Pectinase Genes in Bacteria Erwinia chrysanthemi... [Pg.845]

Fom- title compounds, 5-deoxy KDG Me estw, 5-epi KDG Me ester, 4-0-Me KDG Me ester and 4-deoxy KDG Me ester were prepared either from D-glucono-l,5-lactone or from 1,2 5,6 di-O-isopropylidene-D-mannitol. Biological tests perfcHined rat these molecules have shown that the compounds modified on the C-5 position (5-deoxy KDG Me ester and 5-epi KDG Me ester) are gratuitous inducers of the e>q>ression of pectinase genes in the phytopathogenic bacteria Erwinia Chrysanthemi when the C-4 modified molecules (4-0-Me KDG Me ester and 4-deoxy KDG Me ester) are not inducers. [Pg.845]

Differential expression of Erwinia chrysanthemi strain 3937 pectate lyases in pathogenesis of African violets importance of low iron environmental conditions... [Pg.875]

The pathogenicity of Erwinia chrysanthemi 3937 on African violets involves at least five pectate lyases (PelA to PelE), one methyl pectin esterase (Pern), encoded by pelA to pelE, pern genes and an iron assimilation system mediated by chiysobactin [1], (Fig. 1). [Pg.875]

Boccara, M., Diolez, A., Rouve, M., and Kotoujansky, A. 1988. The role of individual pectate lyases of Erwinia chrysanthemi strain 3937 in pathogenicity on saintpaulia plants. Physiol. Mol. Plant Pathol. 33 95-104... [Pg.880]

Reverchon, S., and Robert- Baudouy, J. 1987. Regulation of the expression of pectate lyase genes pelA, pelD, and pelE in Erwinia chrysanthemi. J. Bacteriol. 169 2417-2423... [Pg.880]

Sauvage, C., and Expert, D. 1994. Differential regulation by iron of Erwinia chrysanthemi pectate lyases pathogenicity of iron transport regulatory (cbr) mutants. Mol. Plant-Microbe Interact. 7 71-77... [Pg.880]

Neema, C., Laulhere, J.-P., and Expert, D. 1993. Iron deficiency induced by chiysobactin in Scdntpaulia ionantha leaves inoculated with Erwinia chrysanthemi. Plant Physiol. 102 967-973... [Pg.880]

Erwinia chrysanthemi Not characterized CbrA CbrB, CbrC CbrD Achromobactin Mahe et ah, 1995 ... [Pg.104]

The first structures of this kind were reported in 1993 pectate lyase G from Erwinia chrysanthemi (Yoder et al, 1993) and alkaline protease from Pseudomonas aeruginosa (Baumann et al, 1993). Based on consideration of these crystal structures, the term parallel //-helix was introduced for a fold containing three //-strands per coil, and parallel //-roll for a fold with two //-strands per coil (Baumann etal, 1993 Yoder andjurnak, 1995 Yoder et al., 1993). The epithet parallel was intended to emphasize the distinction between these folds and the previously observed helical structure of the antibiotic gramicidin which contains both l- and D-amino acids and... [Pg.57]

Pectin methylesterase Erwinia chrysanthemi iQJV 2.37 etal. (2001) Jenkins... [Pg.62]

Dehdashti, S.J., Doan, C. N., Chao, K. L., and Yoder, M. D. (2003). Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16. Acta Crystallogr. D Biol. Crystallogr. 59, 1339—1342. [Pg.92]

Hege, T., and Baumann, U. (2001). Protease C of Erwinia chrysanthemi The crystal structure and role of amino acids Y228 and E189./. Mol. Biol. 314, 187-193. [Pg.92]

Jenkins, J., Shevchik, V. E., Hugouvieux-Cotte-Pattat, N., and Pickersgill, R. W. (2004). The crystal structure of pectate lyase Pel9A from Erwinia chrysanthemi. J. Biol. Chem. 279, 9139-9145. [Pg.93]

Treponema pallidum Treponema denticola A Geobacter sulfurreducens Escherichia coli Salmonella typhi Yersinia enterocolitica Yersinia pestis Erwinia chrysanthemi A... [Pg.122]

See other pages where Erwinia chrysanthemi is mentioned: [Pg.409]    [Pg.410]    [Pg.410]    [Pg.285]    [Pg.295]    [Pg.295]    [Pg.311]    [Pg.312]    [Pg.313]    [Pg.314]    [Pg.837]    [Pg.837]    [Pg.842]    [Pg.880]   
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See also in sourсe #XX -- [ Pg.25 , Pg.394 ]

See also in sourсe #XX -- [ Pg.1280 ]

See also in sourсe #XX -- [ Pg.177 , Pg.188 ]



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