uniconazole-p and uniconazole

uniconazole-p has been researched along with uniconazole* in 2 studies

Other Studies

2 other study(ies) available for uniconazole-p and uniconazole

Article	Year
Structure-activity relationship of uniconazole, a potent inhibitor of ABA 8'-hydroxylase, with a focus on hydrophilic functional groups and conformation. Bioorganic & medicinal chemistry, 2008, Mar-15, Volume: 16, Issue:6 The plant growth retardant S-(+)-uniconazole (UNI-OH) is a strong inhibitor of abscisic acid (ABA) 8'-hydroxylase, a key enzyme in the catabolism of ABA, a plant hormone involved in stress tolerance, stomatal closure, flowering, seed dormancy, and other physiological events. In the present study, we focused on the two polar sites of UNI-OH and synthesized 3- and 2''-modified analogs. Conformational analysis and an in vitro enzyme inhibition assay yielded new findings on the structure-activity relationship of UNI-OH: (1) by substituting imidazole for triazole, which increases affinity to heme iron, we identified a more potent compound, IMI-OH; (2) the polar group at the 3-position increases affinity for the active site by electrostatic or hydrogen-bonding interactions; (3) the conformer preference for a polar environment partially contributes to affinity for the active site. These findings should be useful for designing potent azole-containing specific inhibitors of ABA 8'-hydroxylase. Topics: Binding Sites; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Mixed Function Oxygenases; Molecular Conformation; Plant Proteins; Static Electricity; Structure-Activity Relationship; Triazoles	2008
Metabolism of uniconazole-P in water-sediment systems under illumination. Environmental toxicology and chemistry, 2006, Volume: 25, Issue:2 Aerobic soil metabolism of uniconazole-P ([S]-E-1-[4-chlorophenyl]-4,4-dimethyl-2-[1,2,4-triazole-1-yl]-penten-3-ol) and the effect of illumination on metabolic profiles were studied in the water-sediment system when spiked to water. Uniconazole-P was gradually partitioned to the sediment with an aquatic half-life of 6.9 d in darkness with formation of bound residues. Illumination of the system from a xenon lamp (>290 nm) greatly accelerated the degradation of uniconazole-P via photoinduced isomerization between E- and Z-isomers with a subsequent intramolecular cyclization, and its aquatic half-life was greatly reduced to 0.6 d. Kinetic analysis based on compartment models suggested the possible contribution of photodegradation at the water-sediment interface, leading to more formation of the cyclized derivative in the sediment. Topics: Geologic Sediments; Half-Life; Kinetics; Light; Photochemistry; Soil Microbiology; Soil Pollutants; Triazoles; Water	2006

Article

Year

Structure-activity relationship of uniconazole, a potent inhibitor of ABA 8'-hydroxylase, with a focus on hydrophilic functional groups and conformation.

Bioorganic & medicinal chemistry, 2008, Mar-15, Volume: 16, Issue:6

The plant growth retardant S-(+)-uniconazole (UNI-OH) is a strong inhibitor of abscisic acid (ABA) 8'-hydroxylase, a key enzyme in the catabolism of ABA, a plant hormone involved in stress tolerance, stomatal closure, flowering, seed dormancy, and other physiological events. In the present study, we focused on the two polar sites of UNI-OH and synthesized 3- and 2''-modified analogs. Conformational analysis and an in vitro enzyme inhibition assay yielded new findings on the structure-activity relationship of UNI-OH: (1) by substituting imidazole for triazole, which increases affinity to heme iron, we identified a more potent compound, IMI-OH; (2) the polar group at the 3-position increases affinity for the active site by electrostatic or hydrogen-bonding interactions; (3) the conformer preference for a polar environment partially contributes to affinity for the active site. These findings should be useful for designing potent azole-containing specific inhibitors of ABA 8'-hydroxylase.

Topics: Binding Sites; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System; Mixed Function Oxygenases; Molecular Conformation; Plant Proteins; Static Electricity; Structure-Activity Relationship; Triazoles

2008

Metabolism of uniconazole-P in water-sediment systems under illumination.

Environmental toxicology and chemistry, 2006, Volume: 25, Issue:2

Aerobic soil metabolism of uniconazole-P ([S]-E-1-[4-chlorophenyl]-4,4-dimethyl-2-[1,2,4-triazole-1-yl]-penten-3-ol) and the effect of illumination on metabolic profiles were studied in the water-sediment system when spiked to water. Uniconazole-P was gradually partitioned to the sediment with an aquatic half-life of 6.9 d in darkness with formation of bound residues. Illumination of the system from a xenon lamp (>290 nm) greatly accelerated the degradation of uniconazole-P via photoinduced isomerization between E- and Z-isomers with a subsequent intramolecular cyclization, and its aquatic half-life was greatly reduced to 0.6 d. Kinetic analysis based on compartment models suggested the possible contribution of photodegradation at the water-sediment interface, leading to more formation of the cyclized derivative in the sediment.

Topics: Geologic Sediments; Half-Life; Kinetics; Light; Photochemistry; Soil Microbiology; Soil Pollutants; Triazoles; Water

2006