Kinetic Comparison of Cytokinin Nucleosidase Activity Isolated from Normally Ripening and Mutant Tomato Varieties

Kinetic parameters for cytokinin nucleosidase activity which catalyzes the deribosylation of N6(Δ 2-isopentenyl)adenosine ($\text{I}^{6}$Ado) to produce the more "active" free base $N^{5}$(Δ 2-isopenetyl)adenine ($\text{I}^{6}$Ade) were compared for a normally ripening tomato (Lycopersicon...

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Published inPlant physiology (Bethesda) Vol. 91; no. 1; pp. 148 - 150
Main Authors ROLLE, R. S, CHISM, G. W. III
Format Journal Article
LanguageEnglish
Published Rockville, MD American Society of Plant Physiologists 01.09.1989
Subjects
Biological and medical sciences
Cytokinins
Enzyme substrates
Enzymes
Experimentation
Food science
Fruits
Fundamental and applied biological sciences. Psychology
Kinetics
Metabolism
Plant physiology and development
Plants
Ripening
Enzyme
Cytochemistry
Enzymatic activity
Michaelis constant
Dicotyledones
Nucleosidase
Angiospermae
Lycopersicon esculentum
Spermatophyta
Solanaceae
Kinetics
Intraspecific comparison
Mutation
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Summary:Kinetic parameters for cytokinin nucleosidase activity which catalyzes the deribosylation of N6(Δ 2-isopentenyl)adenosine ($\text{I}^{6}$Ado) to produce the more "active" free base $N^{5}$(Δ 2-isopenetyl)adenine ($\text{I}^{6}$Ade) were compared for a normally ripening tomato (Lycopersicon esculentum L.) cultivar Rutgers, and two mutant tomato varieties (Nor and Rin). Km for nucleosidase activity in Rutgers was lower (Km = 0.1 millimolar) than that in either Nor (Km = 0.14 millimolar) or Rin (Km = 0.13 millimolar).
Bibliography:ObjectType-Article-1
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ISSN:0032-0889
1532-2548
DOI:10.1104/pp.91.1.148