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2.3.1.98
evolution
the sequence determines SlCGT as a GDSL lipase-like protein, representing it as a member of the SGNH protein superfamily. Lipases of this family employ a catalytic triad of Ser-Asp-His with Ser as nucleophile of the GDSL motif. The catalytic triad of the GDSL lipase is not essential for SlCGT enzymatic activity. SlCGT is therefore an example of a GDSL lipase-like protein that has lost hydrolytic activity and has acquired a completely new function in plant metabolism, functioning in secondary metabolism as acyltransferase in synthesis of hydroxycinnamate esters by employing amino acid residues different from the lipase catalytic triad
719900
2.3.1.98
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the deduced SlCGT amino acid sequence matches the conservation of the serine catalytic motif GXSXXDXG within the first consensus block near the N-terminus. A serine moiety of the GDSL protein may be part of the catalytic center in SlCGT
719900
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