Mandrich_2009_Protein.Pept.Lett_16_1189

Reference

Title : Structural and kinetic overview of the carboxylesterase EST2 from alicyclobacillus acidocaldarius: a comparison with the other members of the HSL family - Mandrich_2009_Protein.Pept.Lett_16_1189
Author(s) : Mandrich L , Merone L , Manco G
Ref : Protein Pept Lett , 16 :1189 , 2009
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.
ESTHER : Mandrich_2009_Protein.Pept.Lett_16_1189
PubMedSearch : Mandrich_2009_Protein.Pept.Lett_16_1189
PubMedID: 19508183
Gene_locus related to this paper: aliac-est2

Related information

Gene_locus related to this paper: aliac-est2

Citations formats

Mandrich L, Merone L, Manco G (2009)
Structural and kinetic overview of the carboxylesterase EST2 from alicyclobacillus acidocaldarius: a comparison with the other members of the HSL family
Protein Pept Lett 16 :1189

Mandrich L, Merone L, Manco G (2009)
Protein Pept Lett 16 :1189