Phytochemistry p. 2423 - 2428 (1984)
Update date:2022-08-16
Topics:
Pundir, C. S.
Garg, G. K.
Rathore, V. S.
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 Km for indole was 1.4E-4 M.The enzyme was inhibited by diethyldithiocarbamate, salicylaldoxime and sodium dithionite.The inhibition by diethyldithiocarbamate was specifically reversed by Cu2+.The dialyzed 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.Key Word Index - Zea mays; Gramineae; maize leaf; indole oxidation; indole oxidase; indole 2,3-dioxygenase; purification; Cu2+; -SH groups.
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