Erwinia chrysanthemi

Shikimate kinase was chosen as a convenient representative example of the subclass of a/b proteins with which to examine the mechanism of protein folding. In this paper we report on the refolding of the enzyme after denaturation in urea. As shown by the changes in secondary and tertiary structure monitored by far UV circular dichroism (CD) and fluorescence, respectively, the enzyme was fully unfolded in 4 M urea. From an analysis of the unfolding curve in terms of the two-state model, the stability of the folded state could be estimated as 17 kJÆmol)1.

9p system191 01-06-2013 46 5   Download

The mode of action of xylanase A from a phytopathogenic bacterium, Erwinia chrysanthemi, classified in glycoside hydrolase family 5, was investi-gated on xylooligosaccharides and polysaccharides using TLC, MALDI-TOF MS and enzyme treatment with exoglycosidases.

12p galaxyss3 21-03-2013 46 2   Download

Xylanase A from the phytopathogenic bacteriumErwinia chrysanthemiis classified as a glycoside hydrolase family 30 enzyme (previously in family 5) and is specialized for degradation of glucuronoxylan. The recombinant enzyme was crystallized with the aldotetraouronic acidb-D-xylopyranosyl-(1fi4)-[4-O-methyl-a-D-glucuronosyl-(1 fi2)]-b-D-xylopyranosyl-(1 fi4)-D-xylose as a ligand.

12p cosis54 05-01-2013 53 4   Download

Bệnh thối mềm gây ra do vi khuẩn Erwinia carotovora pv. carotovora và Erwinia chrysanthemi trên lan Phalaenopsis.

4p nhungmon 19-03-2009 247 89   Download