Plant Physiol. Drug Metab Dispos
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Plant Physiology 84:972-974 (1987)
© 1987 American Society of Plant Biologists

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Metabolism and Enzymology

Evidence for Transglutaminase Activity in Plant Tissue

Isaac Icekson and Akiva Apelbaum

Department of Fruit and Vegetable Storage, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel

An extract prepared from the apical meristematic region of etiolated pea seedlings was able to catalyze the incorporation of putrescine into trichloroacetic acid precipitable material. The enzyme was found to be soluble and followed a typical Michaelis-Menten kinetics when N-N-dimethyl casein was used as a substrate. Its activity was promoted by Ca2+ and inhibited by Cu2+ and DL-dithiothreitol. Other polyamines competed with putrescine as substrates and cadaverine was the most potent inhibitor of putrescine incorporation. Plant transglutaminase is capable of recognizing specific sites in substrates described for animal transglutaminase, like insulin, fibrinogen, pepsin, and thrombin. However, it can also use as substrates cellulase and creatine kinase which have not been described for transglutaminase from other sources.




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D. Serafini-Fracassini and S. Del Duca
Transglutaminases: Widespread Cross-linking Enzymes in Plants
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[Abstract] [Full Text] [PDF]

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G. R. Lilley, J. Skill, M. Griffin, and P. L.R. Bonner
Detection of Ca2+-Dependent Transglutaminase Activity in Root and Leaf Tissue of Monocotyledonous and Dicotyledonous Plants
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Copyright © 1987 by the American Society of Plant Biologists