The level of ABA in plants is controlled not only by its synthesis, but also through its catabolism (Fig. 12). There are two major pathways for ABA inactivation. One of the primary catabolites of ABA is phaseic acid (PA), which is biologically inactive. The conversion of ABA to PA begins with the hydroxylation of the 8' position by ABA 8'-hydroxylase. The 8' hydroxyl appears to be an unstable intermediate that spontaneously rearranges to form PA. Phaseic acid is further converted to dihydrophaseic acid (DPA), which can be conjugated to glucose at the 4'position. The 8'-hydroxylase activity has been characterized in a microsomal fraction from maize suspension cultures (20). The requirements for this activity
and the sensitivity of the enzyme to inhibition by carbon monoxide and tetcyclacis indicate that the ABA 8'-hydroxylase is a cytochrome P450.In suspension cultures pretreated with ABA, the rate of conversion of ABA to PA is increased significantly, indicating that the 8'-hydroxylase is itself induced by ABA. This negative feedback regulation is consistent with time course measurements of ABA and PA accumulation in stressed plants. It has also been observed that several ABA-insensitive mutants contain elevated levels of ABA. Once the gene encoding the 8'-hydroxylase has been identified,
its manipulation may offer another approach for modifying ABA levels in transgenic plants. Recently, a new catabolite of ABA has been identified. This