Structural and kinetic overview of the carboxylesterase EST2 from alicyclobacillus acidocaldarius: a comparison with the other members of the HSL family.
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.
Mandrich
Luigi
L
Institute of Protein Biochemistry (IBP), National Research Council (CNR), Via Pietro Castellino 111, 80131, Naples, Italy.
Merone
Luigia
L
Manco
Giuseppe
G
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
D001426:Bacterial Proteins; D043182:Carboxylesterase; D002787:Sterol Esterase