A cofactor requirement for polygalacturonase from Cuscuta campestris

The occurrence of a polygalacturonase in tissue of Cuscuta is reported. The enzyme activity requires the presence of a cofactor, which can be removed by dialysis. The cofactor is heat stable and extractable in 80% methanol or in petroleum ether. It appears to be a low molecular weight peptide, since...

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Bibliographic Details
Published inPhytochemistry (Oxford) Vol. 52; no. 7; pp. 1217 - 1221
Main Authors Bar Nun, Nurit, Mor, Amram, Mayer, Alfred M.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Ltd 01.12.1999
Elsevier
Subjects
Biological and medical sciences
Characterisation
Cofactor for activity
Convolvulaceae
Cuscuta campestris
Fundamental and applied biological sciences. Psychology
Parasitic plants
Parasitic plants. Weeds
Parasitism
Parasitism and symbiosis
Peptide
Phytopathology. Animal pests. Plant and forest protection
Plant physiology and development
Polygalacturonase
Cuscuta campestris
Polygalacturonase
Characterisation
Cofactor for activity
Convolvulaceae
Peptide
Peptides
Enzyme
Cofactor
Thermal stability
Characterization
Enzymatic activity
Dicotyledones
Glycosidases
Angiospermae
Hydrolases
Spermatophyta
O-Glycosidases
Parasitic plant
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Summary:The occurrence of a polygalacturonase in tissue of Cuscuta is reported. The enzyme activity requires the presence of a cofactor, which can be removed by dialysis. The cofactor is heat stable and extractable in 80% methanol or in petroleum ether. It appears to be a low molecular weight peptide, since its activity is lost on incubation with proteinase K or papain. The exact nature and the possible function of this co-factor in the breakdown of pectins by Cuscuta are under investigation.
ISSN:0031-9422
1873-3700
DOI:10.1016/S0031-9422(99)00418-5