Journal
PHYTOCHEMISTRY
Volume 62, Issue 3, Pages 293-300Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0031-9422(02)00563-0
Keywords
Arabidopsis thaliana; Brassicaceae; crucifers; indole-3-acetic acid; indole-3-acetamide; indole-3-acetonitrile; nitrilases; acylamide amidohydrolase; amidase
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Acylamidohydrolases from higher plants have not been characterized or cloned so far. A tAMI1 is the first member of this enzyme family from a higher plant and was identified in the genome of Arabidopsis thaliana based on sequence homology with the catalytic domain sequence of bacterial acylamidohydrolases, particularly those that exhibit indole-3-acetamide amidohydrolase activity. AtAMI1 polypeptide and mRNA are present in leaf tissues, as shown by immunoblotting and RT-PCR, respectively. AtAMI1 was expressed from its cDNA in enzymatically active form and exhibits substrate specificity for indole-3-acetamide, but also some activity against L-asparagine. The recombinant enzyme was characterized further. The results show that higher plants have acylamidohydrolases with properties similar to the enzymes of certain plant-associated bacteria such as Agrobacterium-, Pseudomonas and Rhodococcus-species, in which these enzymes serve to synthesize the plant growth hormone, indole-3-acetic acid, utilized by the bacteria to colonize their host plants. As indole-3-acetamide is a native metabolite in Arabidopsis thaliana, it can no longer be ruled out that one pathway for the biosynthesis of indole-3-acetic acid involves indole-3-acetamide-hydrolysis by AtAMI1 (C) 2003 Elsevier Science Ltd. All rights reserved.
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