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YSIRK-targeted triacylglycerol lipase
Members of this staphylococcal lipase family have an N-terminal YSIRK-type signal peptide that is known for targeting sortase-dependent (LPXTG motif-containing) cell wall proteins to the cross-wall of growing and dividing cells. However, YSIRK also occurs on proteins that associate with the cell surface through other means. The YSIRK region is followed by a long, variable length low-complexity region rich in Ser, Thr, Asn, Asp, Glu, and Gln, followed by the lipase domain. Genes for member of this family in Staphylococcus aureus may be given as lip1 (e.g. YP_501455.1) and lip2 (YP_498890.1), or gehA and gehB. Members of this family in Staphylococcus aureus are considered virulence factors.
triacylglycerol lipase
triacylglycerol lipase is an alpha/beta hydrolase that catalyzes the hydrolysis of a triacylglycerol to form the corresponding diacylglycerol and a carboxylate
PGAP1-like protein
The sequences found in this family are similar to PGAP1 (Swiss:Q765A7). This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body [1]. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts [2]. [1]. 14734546. Inositol deacylation of glycosylphosphatidylinositol-anchored. proteins is mediated by mammalian PGAP1 and yeast Bst1p.. Tanaka S, Maeda Y, Tashima Y, Kinoshita T;. J Biol Chem. 2004;279:14256-14263.. [2]. 19959834. The TGL2 gene of Saccharomyces cerevisiae encodes an active. acylglycerol lipase located in the mitochondria.. Ham HJ, Rho HJ, Shin SK, Yoon HJ;. J Biol Chem. 2010;285:3005-3013. (from Pfam)
Lipase (class 2)
This family consists of hypothetical C. elegans proteins and lipases. Lipases or triacylglycerol acylhydrolases hydrolyse ester bonds in triacylglycerol giving diacylglycerol, monoacylglycerol, glycerol and free fatty acids [1]. Swiss:P37957 is a extracellular lipase from B. subtilis 168 [1]. [1]. 1320940. Cloning, nucleotide sequence and expression in Escherichia coli. of a lipase gene from Bacillus subtilis 168.. Dartois V, Baulard A, Schanck K, Colson C;. Biochim Biophys Acta 1992;1131:253-260. (from Pfam)
lipase family protein
lipase family protein such as triacylglycerol lipase, which is an alpha/beta hydrolase that catalyzes the hydrolysis of a triacylglycerol to form the corresponding diacylglycerol and a carboxylate
SGNH family lipase
alpha/beta hydrolase; lipase family alpha/beta hydrolase
uncharacterized alpha/beta hydrolase; may catalyze the cleavage and formation of ester bonds; lipase family alpha/beta hydrolase similar to triacylglycerol lipase that catalyzes the hydrolysis of triacylglycerol
alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad; lipase family alpha/beta hydrolase similar to triacylglycerol lipase that catalyzes the hydrolysis of triacylglycerol
lipid droplet-associated hydrolase family protein
lipid droplet-associated hydrolase (LDAH) family protein is a lipid hydrolase associated with lipid droplets; similar to Saccharomyces cerevisiae lipid droplet-associated triacylglycerol lipase that shows both triacylglycerol (TAG) lipase and ester hydrolase activities
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