Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots
Abstract: The main form of pectate hydrolases in the cell wall of parsley roots showed a unique substrate preference of a plant exopolygalacturonase because it clearly preferred the substrates with degree of polymerization about 10. This form was separated from the others, purified and characterized. Enzyme exhibited sharp pH optimum corresponding to pH 4.7, molecular mass 53.5 kDa, and isoelectric point 5.3. It was stable at 50°C in 2-h assay and had optimum of temperature at 60°C (activation energy being 37.0 kJ/mol). The interaction with concanavalin A indicated the glycosylation of enzyme. Substrates were cleaved from the non-reducing end.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots ; volume:64 ; number:2 ; year:2009 ; pages:228-234 ; extent:7
Biologia ; 64, Heft 2 (2009), 228-234 (gesamt 7)
- Creator
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Flodrová, Dana
Garajová, Soňa
Malovíková, Anna
Mislovičová, Danica
Omelková, Jiřina
Stratilová, Eva
- DOI
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10.2478/s11756-009-0038-2
- URN
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urn:nbn:de:101:1-2409221621406.604898374803
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:30 AM CEST
Data provider
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Flodrová, Dana
- Garajová, Soňa
- Malovíková, Anna
- Mislovičová, Danica
- Omelková, Jiřina
- Stratilová, Eva
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The neural substrate of spectral preference in Drosophila
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Inhibition of soluble epoxide hydrolase enhances the dentin-pulp complex regeneration mediated by crosstalk between vascular endothelial cells and dental pulp stem cells
Clostridioides difficile bile salt hydrolase activity has substrate specificity and affects biofilm formation
Reduced sphingolipid hydrolase activities, substrate accumulation and ganglioside decline in Parkinson’s disease
Phylogenetic analyses suggest multiple changes of substrate specificity within the Glycosyl hydrolase 20 family
SPOP point mutations regulate substrate preference and affect its function
Unique steel belt press technology for high strength papers from high yield pulp
Tunnel engineering for modulating the substrate preference in cytochrome P450BsβHI
A new buckwheat dihydroflavonol 4-reductase (DFR), with a unique substrate binding structure, has altered substrate specificity
A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement
Mechanism-based traps enable protease and hydrolase substrate discovery
The neural substrate of spectral preference in Drosophila
Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)
Inhibition of soluble epoxide hydrolase enhances the dentin-pulp complex regeneration mediated by crosstalk between vascular endothelial cells and dental pulp stem cells
Clostridioides difficile bile salt hydrolase activity has substrate specificity and affects biofilm formation
Reduced sphingolipid hydrolase activities, substrate accumulation and ganglioside decline in Parkinson’s disease
Phylogenetic analyses suggest multiple changes of substrate specificity within the Glycosyl hydrolase 20 family
SPOP point mutations regulate substrate preference and affect its function
Unique steel belt press technology for high strength papers from high yield pulp
Tunnel engineering for modulating the substrate preference in cytochrome P450BsβHI