Crystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity.
Kim, K.K., Song, H.K., Shin, D.H., Hwang, K.Y., Choe, S., Yoo, O.J., Suh, S.W.(1997) Structure 5: 1571-1584
- PubMed: 9438866 
- DOI: https://doi.org/10.1016/s0969-2126(97)00306-7
- Primary Citation of Related Structures:  
1AUO, 1AUR - PubMed Abstract: 
A group of esterases, classified as carboxylesterases, hydrolyze carboxylic ester bonds with relatively broad substrate specificity and are useful for stereospecific synthesis and hydrolysis of esters. One such carboxylesterase from Pseudomonas fluorescens is a homodimeric enzyme, consisting of 218-residue subunits. It shows a limited sequence similarity to some members of the alpha/beta hydrolase superfamily. Although crystal structures of a number of serine esterases and lipases have been reported, structural information on carboxylesterases is very limited. This study was undertaken in order to provide such information and to understand a structural basis for the substrate specificity of this carboxylesterase.
Organizational Affiliation: 
Department of Chemistry, College of Natural Sciences, Seoul National University, Korea.