| Type: | Family | Name: | Esterase/lipase |
| Description: | Members of this group are esterases, lipases, and (possibly) other hydrolases of the alpha/beta hydrolase fold. The Bacillus stearothermophilus(Geobacillus stearothermophilus) member, Est, has been characterised as a carboxylesterase () involved in the detoxification of xenobiotics [], and the Bacillus sp. H-257member has been characterised as monoacylglycerol lipase () [].The alpha/beta hydrolase fold is found in a wide range of enzymes with different catalytic functions []. These enzymes operate on different substrates, and may lack detectable sequence similarity. Nevertheless, they share structural similarity (an open twisted beta sheet surrounded on both sides by alpha helices) and the arrangement of three catalytic residues (the "catalytic triad"): a nucleophile (usually Ser), an acid (usually Asp), and histidine [, ]. The functional roles of the triad residues are as follows: the sidechain group at the Ser position serves as a nucleophilic centre, the His sidechain acts as a general base and is hydrogen bonded to the carboxylic group of the Asp sidechain. Together, His and Asp form a charge relay system []. | Short Name: | Esterase_lipase |
