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. 2010 Sep 29;285(49):38374–38381. doi: 10.1074/jbc.M110.171637

FIGURE 2.

FIGURE 2.

Alignment of the deduced amino acid sequence of SlCGT with characterized related GDSL lipase-like proteins. SlCGT amino acid sequences were deduced from cDNA and aligned with a carboxylic ester hydrolase (A. thaliana; U38916) (33), sinapine esterase (B. napus; AAX59709) (17), lanatoside 15′-O-acetylesterase-like enzyme (Oryza sativa; AP002866) (60), and acetylajmalan acetylesterase (R. serpentina; AY762990) (36). The predicted N-terminal leader sequences of all enzymes are shown in italics. Highly conserved residues are shaded in blue. Asterisks, peptides identified by sequencing and used to identify SlCGT; blue box, amino acid motif used to deduce degenerated primers for PCR, red box, GDSL motif; red triangles, catalytic triad (Ser27, Asp328, His331); black box, conserved blocks in the SGNH hydrolase family (I, II, III, V) (35, 42).