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Leucine biosynthesis in fungi: entering metabolism through the back

by Gunter B. Kohlhaw, Gunter B. Kohlhaw
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This article cites 116 articles, 72 of which can be accessed free
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The Putative Saccharomyces cerevisiae Hydrolase Ldh1p Is Localized to Lipid Droplets

by unknown authors , 2011
"... Here, we report the identification of a novel hydrolase in Saccharomyces cerevisiae. Ldh1p (systematic name, Ybr204cp) comprises the typical GXSXG-type lipase motif of members of the /-hydrolase family and shares some features with the peroxisomal lipase Lpx1p. Both proteins carry a putative peroxis ..."
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Here, we report the identification of a novel hydrolase in Saccharomyces cerevisiae. Ldh1p (systematic name, Ybr204cp) comprises the typical GXSXG-type lipase motif of members of the /-hydrolase family and shares some features with the peroxisomal lipase Lpx1p. Both proteins carry a putative peroxisomal targeting signal type1 (PTS1) and can be aligned with two regions of homology. While Lpx1p is known as a peroxisomal enzyme, subcellular localization studies revealed that Ldh1p is predominantly localized to lipid droplets, the storage compartment of nonpolar lipids. Ldh1p is not required for the function and biogenesis of peroxisomes, and targeting of Ldh1p to lipid droplets occurs independently of the PTS1 receptor Pex5p. Peroxisomes and lipid droplets (LDs) are ubiquitous eukary-otic organelles involved in lipid metabolism. LDs appear as oleosomes in plants, as adiposomes in mammals, or as lipid particles/bodies/droplets in yeasts and constitute a family of morphologically and biogenetically similar organelles (19). LDs are bound by a phospholipid monolayer and serve as the main storage sites for nonpolar lipids, mainly triacylglycerols (TAG) and cholesteryl ester (CE) (6, 7). LDs derive from the
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SEE PROFILE

by Sven Thoms, Mykhaylo Debelyy, See Profile , 2011
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All in-text references underlined in blue are linked to publications on ResearchGate, letting you access and read them immediately.
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