1aur
From Proteopedia
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PMSF-INHIBITED CARBOXYLESTERASE FROM PSEUDOMONAS FLUORESCENS
Overview
BACKGROUND: 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. RESULTS: In this study, the crystal structure of ... [(full description)]
About this Structure
1AUR is a [Single protein] structure of sequence from [Pseudomonas fluorescens] with PMS as [ligand]. Active as [[1]], with EC number [3.1.1.1]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity., Kim KK, Song HK, Shin DH, Hwang KY, Choe S, Yoo OJ, Suh SW, Structure. 1997 Dec 15;5(12):1571-84. PMID:9438866
Page seeded by OCA on Mon Oct 29 21:05:24 2007
