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- W1973773455 abstract "The activity of the enzyme catalyzing the hydrolysis of IAA glucose conjugates has been studied in vegetative tissues of plants. We have demonstrated the presence of this enzyme in sprouts of oat ( Avena sativa L.), potato tubers ( Solanum tuberosum L.) and sprouts of bean ( Phaseolus vulgaris L.). 4-O and 6-O-IAA glucose esters caused the stimulation of Avena coleoptiles growth in elongation tests. This fact points to enzymatic hydrolysis of IAGlucose isomers as a process yielding free IAA and glucose. We have also found activity of two enzymes catalyzing the hydrolysis of IAA glucose esters in potato tubers. The enzyme specifically hydrolysing 6-O(4-O)-IAGlucose was partially purified using fractionation by PEG 6000, followed by ion-exchange, hydrophobic interaction and gel filtration chromatography. The enzyme has a molecular weight of 32 kDa, it shows a very similar activity over the range pH 6–9. The affinity of the enzyme for 6-O(4-O)-IAGlucose is in milimolar range, K m =10 milimolar. The presence of enzymes hydrolysing of IAA glucose conjugates in storage plant tissues may have physiological significance in regulating of free auxin level." @default.
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- W1973773455 date "1993-07-01" @default.
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- W1973773455 title "Enzymatic Hydrolysis of 4-O and 6-O-Indol-3-Ylacetyl-β-D-Glucose in Plant Tissues" @default.
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- W1973773455 doi "https://doi.org/10.1016/s0176-1617(11)80108-2" @default.
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