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Its physiological function is not known. Displays neither proteolytic activity using casein as substrate, nor peptidase activity when assayed with L-leucine p-nitroanilide and L-proline p-nitroanilide"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a carboxylic ester + H2O = an alcohol + a carboxylate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21164"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29067"},{"database":"ChEBI","id":"CHEBI:30879"},{"database":"ChEBI","id":"CHEBI:33308"}],"ecNumber":"3.1.1.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17466017"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17466017"}],"value":"Is strongly inhibited by phenylmethylsulfonyl fluoride, a serine protease inhibitor, and by mercury chloride. 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Shows >70% of its maximal activity in the pH range of 5-9. Displays a relatively high thermostability with a half-life of 1 hour at 100 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17466017"}],"value":"Exists mainly as a monomer and, to some extent as a dimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17466017"}],"value":"The high thermal stability and activity in the presence of organic solvents makes EstD an attractive catalyst for future applications in industry"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17466017"}],"value":"Belongs to the AB hydrolase superfamily. 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