Characterization of a new endoglucanase from Erwinia chrysanthemi
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چکیده
منابع مشابه
Characterization of the pecT control region from Erwinia chrysanthemi 3937.
Erwinia chrysanthemi synthesizes and secretes pectate lyases that attack components of the plant cell wall and, therefore, play a major role in the pathogenesis of soft rot disease. We isolated a new mutant (designated pec-1), by Tn5 mutagenesis, that displays weak pectate lyase production and decreased motility and mucoidicity. Maceration and pathogenicity tests done on different plant organs ...
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The structure of a citrate siderophore named achromobactin isolated from the culture medium of Erwinia chrysanthemi was elucidated by spectroscopic methods and chemical degradation.
متن کاملCharacterization of the exopolygalacturonate lyase PelX of Erwinia chrysanthemi 3937.
Erwinia chrysanthemi 3937 secretes several pectinolytic enzymes, among which eight isoenzymes of pectate lyases with an endo-cleaving mode (PelA, PelB, PelC, PelD, PelE, PelI, PelL, and PelZ) have been identified. Two exo-cleaving enzymes, the exopolygalacturonate lyase, PelX, and an exo-poly-alpha-D-galacturonosidase, PehX, have been previously identified in other E. chrysanthemi strains. Usin...
متن کاملLactose metabolism in Erwinia chrysanthemi.
Wild-type strains of the phytopathogenic enterobacterium Erwinia chrysanthemi are unable to use lactose as a carbon source for growth although they possess a beta-galactosidase activity. Lactose-fermenting derivatives from some wild types, however, can be obtained spontaneously at a frequency of about 5 X 10(-7). All Lac+ derivatives isolated had acquired a constitutive lactose transport system...
متن کاملFunctional characterization of a novel xylanase from a corn strain of Erwinia chrysanthemi.
A beta-1,4-xylan hydrolase (xylanase A) produced by Erwinia chrysanthemi D1 isolated from corn was analyzed with respect to its secondary structure and enzymatic function. The pH and temperature optima for the enzyme were found to be pH 6.0 and 35 degrees C, with a secondary structure under those conditions that consists of approximately 10 to 15% alpha-helices. The enzyme was still active at t...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1987
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1987.tb10602.x