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- W2018347941 abstract "Chloroplasts of Dunaliella salina contain a lipid acyl hydrolase having very different properties from the acyl hydrolase present in D. salina microsomes. Chloroplast fragments hydrolyzed endogenous and exogenous lipids with a marked preference for removing fatty acids bound at the sn-1 position of monogalactosyldia-cylglycerol (MGDG) molecular species typical of this alga. Pisum sativum MGDG molecular species were hydrolyzed less effectively, and catalytically hydrogenated MGDG was completely resistant. Digalactosyl-diacylglycerol and phospholipids were deacylated to a much smaller extent. The enzyme required 10 mM Ca2+ for full activity but, unlike the phosphatidylglycerol acyl hydrolase of microsomes, was not affected by calmodulin or calmodulin antagonists. Its activity also differed from that of the microsomal enzyme by not increasing in cells stressed by low temperature. While no evidence for MGDG hydrolysis was detected in vivo under normal growing conditions, indications of acyl hydrolase activity appeared when cells were grown in nutrient-deficient medium." @default.
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- W2018347941 title "Properties of a fatty acyl hydrolase preferentially attacking monogalactosyldiacylglycerols in Dunaliella salina chloroplasts" @default.
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- W2018347941 doi "https://doi.org/10.1016/0005-2760(86)90243-2" @default.
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