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Peroxisomal indole-3-butyric acid (IBA) to indole-3-acetic acid (IAA) conversion enzymes are a group of plant-specific proteins that facilitate the metabolic activation of auxin (Strader & Bartel, 2011, Plant Signaling & Behavior). This pathway is essential for maintaining auxin homeostasis, as IBA serves as a stable storage form or precursor that can be converted into the potent signaling molecule IAA when needed (Zolman et al., 2008, Plant Physiology). The conversion occurs within the peroxisome through a series of reactions—including oxidation, hydration, dehydrogenation, and thiolysis—that are biochemically similar to the beta-oxidation of fatty acids (Wiszniewski et al., 2009, The Plant Cell). Key enzymes involved in this process include INDOLE-3-BUTYRIC ACID RESPONSE 1 (IBR1), IBR3, IBR10, and 3-KETOACYL-COA THIOLASE 2 (KAT2) (Strader & Bartel, 2011). While these enzymes are critical for plant developmental processes such as root branching and seedling vigor, they are not targets for human therapeutic intervention. Instead, they are of significant interest in agricultural biotechnology and herbicide development, where manipulating auxin levels can control plant growth and weed populations (Schlicht et al., 2013, Journal of Experimental Botany).
Catalyzes the conversion of the auxin precursor indole-3-butyric acid (IBA) into the active auxin indole-3-acetic acid (IAA) via a peroxisomal beta-oxidation-like cycle (Strader & Bartel, 2011).
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