Kinetic properties of phosphoglycolate phosphatase from Pisum sativum and Phaseolus vulgaris

High activities of phosphoglycolate phosphatase were observed in Pisum sativum and Phaseolus vulgaris leaves. The low values for K m phosphoglycolate and the K a values for the activation by Mg 2+ and Cl &− are consistent with the efficient hydrolysis of phosphoglycolate in these plants. This is...

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Published inPhytochemistry (Oxford) Vol. 28; no. 3; pp. 719 - 720
Main Authors Huh, David H., Kursell, Anja V., Husic, H.David
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Ltd 1989
Elsevier
Subjects
2-phosphoglycolate
Analytical, structural and metabolic biochemistry
bean
Biological and medical sciences
chemical composition
enzyme activity
enzyme inhibitors
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
leaves
Leguminosae
pea
Phaseolus vulgaris
phosphoglycolate phosphatase
phosphoric monoester hydrolases
Pisum sativum
phosphoglycolate phosphatase
2-phosphoglycolate
Leguminosae
Phaseolus vulgaris
Pisum sativum
pea
bean
Phosphoglycollate phosphatase
Vegetals
Enzyme
Dicotyledones
Angiospermae
Spermatophyta
Kinetic parameter
Catalyst activity
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Summary:High activities of phosphoglycolate phosphatase were observed in Pisum sativum and Phaseolus vulgaris leaves. The low values for K m phosphoglycolate and the K a values for the activation by Mg 2+ and Cl &− are consistent with the efficient hydrolysis of phosphoglycolate in these plants. This is confirmed by the absence of detectable phosphoglycolate in photosynthetically active leaves of Pisum sativum.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0031-9422
1873-3700
DOI:10.1016/0031-9422(89)80100-1