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Identification of Enzymes Involved in Indole-3-acetic Acid Degradation by Marianne R. Olesen; Bjarne U. Jochimsen is a Agricultural and Biological Sciences article available to read on EtoBox.

What is Identification of Enzymes Involved in Indole-3-acetic Acid Degradation about?

Strains of Bradyrhizobium japonicum with the ability to catabolize indole-3-acetic acid (IAA) and strains of B. japonicum, Rhizobium loti, and Rhizobium galegae, unable to catabolize IAA, were analyzed for enzymes involved in the pathway for IAA degradation. Two enzymes having isatin as substrate were detected. An isatin amidohydrolase catalyzing the hydrolysis of isatin into isatinic acid was found in some B. japonicum strains and in two Rhizobium species, R loti and R. galegae. The enzyme was inducible (4-5-fold) by its substrate, isatin, and the partially purified enzyme from R. loti showed an apparent KM of 11 #M for isatin. A NADPH-dependent isatin reductase was measured in extracts from a strain of B. japonicum lacking the isatin amidohydrolase. The structure of the reaction product, dioxindole was verified by NMR spectroscopy. Isatin reductase activity was also detected in extracts of dry pea seeds, and present in at least two isoforms. A low Ku of 10/d,/for isatin was found with a partially purified preparation of the pea enzyme. The presence of such an enzyme activity in pea indicates dioxindole and isatin as possible intermediates in IAA degradation in pea.

Who reads Identification of Enzymes Involved in Indole-3-acetic Acid Degradation?

Author

Marianne R. Olesen; Bjarne U. Jochimsen

Publisher

Springer; Springer-Verlag; Kluwer Academic Publishers; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc. (ISSN 0032-079X)

Published

1996

Language

EN

Field

Agricultural and Biological Sciences (Life Sciences)