Publication detail
Comparison of pectate hydrolases from parsley root cells
OMELKOVÁ, J.
Original Title
Comparison of pectate hydrolases from parsley root cells
Type
journal article - other
Language
English
Original Abstract
Pectate hydrolases of plants are generally supposed to be bound on primary cell wall where the catalysis of homogalacturonan as a side chain of pectin structure occures. These enzymes with terminal action pattern (exopolygalacturonases, EC 3.2.1.67) can be found in each plant species while the production of those with random action pattern (polygalacturonases, EC 3.2.1.15) indicates the requirement of plant tissue softening. Interestingly, while the function, structure and importance of plant polygalacturonases is widely known, the reseach of exopolygalacturonases is still on its beginning. References about the strict preference for polymeric substrates of these enzymes can be found unlike exopolygalacturonases produced by microorganisms which can prefer substrates with lower degree of polymerization, too. Five forms of pectate hydrolases purified from parsley roots cells are described in this work. Only one of them was strictly bound on the cell wall, enzyme with preference for decamer as the substrate. Other three forms, surprisingly with the preference for hexagalacturonate, were found in other cell structures. Only one typical form of exopolygalacturonase with preference for polymeric substrate was identified, partially bound on the cell wall and partially free in cytosole. The action pattern of individual forms for oligogalacturonides was evaluated using HPLC.
Keywords
pectate hydrolases, exopolygalacturonase
Authors
OMELKOVÁ, J.
RIV year
2008
Released
9. 12. 2008
ISBN
1213-7103
Periodical
Chemické listy
Year of study
102
Number
15
State
Czech Republic
Pages from
630
Pages to
632
Pages count
3
BibTex
@article{BUT47271,
author="Jiřina {Omelková} and Dana {Flodrová}",
title="Comparison of pectate hydrolases from parsley root cells",
journal="Chemické listy",
year="2008",
volume="102",
number="15",
pages="630--632",
issn="1213-7103"
}