Purification and properties of indole 2,3-dioxygenase from maize leaves |
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Authors: | CS Pundir GK Garg VS Rathore |
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Institution: | 1. Departments of Biochemistry, College of Basic Sciences and Humanities, G.B. Pant University of Agriculture and Technology, Pantnagar-263145, India;2. Biological Sciencest, College of Basic Sciences and Humanities, G.B. Pant University of Agriculture and Technology, Pantnagar-263145, India |
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Abstract: | An indole 2,3-dioxygenase was purified ca 38-fold from maize leaves. The enzyme had an MW of about 98000, an optimum pH of 5.0 and the energy of activation was 9.1 kcal/mol. The Kmax for indole was 1.4 × 10?4 M. The enzyme was inhibited by diethyldithiocarbamate, salicylaldoxime and sodium dithionite. The inhibition by diethyldithiocarbamate was specifically reversed by Cu2+. The dialysed enzyme was stimulated by Cu2+. Four atoms of oxygen were utilized in the disappearance of 1 mole of indole. Inhibition of the enzyme by -SH compounds and -SH group inhibitors, and their partial removal by Cu2+ only, suggested the involvement of -SH groups in binding of Cu2+ at the catalytic site. |
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Keywords: | Gramineae maize leaf indole oxidation indole oxidase indole 2 3-dioxygenase purification -SH groups |
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