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Structure of hydrophobic core in plant carboxylesterase

Banach M., Konieczny L., Wiśniowski Z., Roterman I.

Bio-Algorithms and Med-Systems

2017

Vol. 13, no. 1

13--16

The fuzzy oil drop model was applied to characterize the hydrophobic core structure in plant carboxylesterase. The characteristics revealed the status of β-sheets in the central part of the molecule as discordant as opposed to the expected hydrophobicity distribution. Particularly, the β-strands and helices in close proximity to the enzymatic residues recognized as discordant with respect to the ideal hydrophobicity distribution of hydrophobic core are of high importance. It is assumed that this local irregularity is the form of coding the specificity of enzymes. The protein under consideration appears to be the next example proving this assumption.

The activity of selected hydrolases in excretionsecretion products and exctracts from larvae and mature specimens of Cystidicola farionis

Dziekońska-Rynko J., Rokicki J., Jabłonowski Z.

Oceanological and Hydrobiological Studies

2003

Vol. 32, No. 4

117-129

The results of the study indicated that there are differences in the activity of hydrolases depending on the development stage of the parasite and the season of the year. Twelve hydrolases were confirmed to be active in excretion-secretion (ES) products of larvae collected in fall, while nine were active in spring. The activity of hydrolase from the extracts of fall samples was most often higher than in spring. Eight active hydrolases were confirmed in mature specimens both in spring and fall, and they exhibited a lower activity level than the ES products of larvae. However, the activity of enzymes was higher in mature specimens than in larvae in the extracts from both spring and fall samples.