Linoleic acid A9 hydratase

Substrate specificity of hydration reaction catalyzed by linoleic acid A9 hydratase. 

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Linoleic acid A9 hydratase, which is involved in the linoleic acid saturation metabolism of Lactobacillus plantarum AKU 1009a, was cloned as his-tagged recombinant enz une, purified with affinity column, and characterized [30]. The enzyme required FAD as a cofactor for its activity, and the activity was enhanced by NADH. The maximum activities for hydration of linoleic acid and for dehydration of lO-hydroxy-czs-12-octadecenoic acid (HYA) were observed at 37°C, pH5.5, with 0.5M NaCl. C16 and CIS free fatty acids with cis-9 double bond served as substrates for hydration with CIO regiospecificity and (S) stereospecificity (Figure 22.9). 10-Hydroxy fatty acids served as substrates for dehydration reactions. The apparent value for linoleic acid was estimated to be 92 irM with its values at 2.6 x 10 s and Hill factor was 3.3. The apparent K value for HYA was estimated to be 98 iM with its values at 1.2 x 10 s ... 

Efficient Enzymatic Production of Hydroxy Fatty Acids by Linoleic Acid A9 Hydratase... 

Takeuchi, M., Kishino, S., Hirata, A., Park, S. B., Kitamura, N., Ogawa, J. (2015). Characterization of the linoleic acid A9 hydratase catalyzing the first step of polyunsaturated fatty acid saturation metabolism in Lactobacillus plantarum AKU 1009a. /. Biosci. Bioeng., 119,636-641. 

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