title: Structural and kinetic overview of the carboxylesterase EST2 from alicyclobacillus acidocaldarius: a comparison with the other members of the HSL family.
abstract: Thermophilic and hyperthermophilic carboxylesterases (EC 3.1.1.1) are excellent model systems for studying structure function relationships as well as in vitro and in vivo evolution and possible biotechnological applications. In this paper we review the main aspect of one of most studied microbial representative of the hormone sensitive lipase family (HSL), namely carboxylesterase 2 (EST2) from Alicyclobacillus acidocaldarius.
authors.affiliation: Institute of Protein Biochemistry (IBP), National Research Council (CNR), Via Pietro Castellino 111, 80131, Naples, Italy.
authors.forename: Luigi
authors.initials: L
authors.lastname: Mandrich
authors.forename: Luigia
authors.initials: L
authors.lastname: Merone
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Manco
mesh_terms: D056450:Alicyclobacillus / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D043182:Carboxylesterase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D007700:Kinetics; D009154:Mutation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D002787:Sterol Esterase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D043182:Carboxylesterase; D002787:Sterol Esterase