A Short C-Terminal Region of Alpha-Synuclein Protects a (R/S)-Nonspecific Esterase from Archaeglobus fulgidus

Abstract

We show that alpha-synuclein could assist the molecular activity of a ketoprofen-(R/S) nonspecific esterase from Archaeglobus Fulgidus. Specifically, several synthetic peptides from alpha-synuclein, each having random coil conformation in far-UV spectra, could protect the enzyme activity against stress conditions such as heat and organic solvents.

Purification, crystallization and preliminary crystallographic analysis of Est-Y29: a novel oligomeric β-lactamase

“…In a previous report, we identified a novel oligomeric class C -lactamase, Est-Y29, from a metagenomic library (Yoon et al, 2007). Interestingly, Est-Y29 can catalyze the kinetic resolution of ketoprofen ethyl ester used in the production of the anti-inflammatory drug (S)-ketoprofen (Yoon et al, 2007;Kim et al, 2007). Est-Y29 possesses the Ser-X-X-Lys motif which is highly conserved among -lactamases and site-directed mutagenesis of Ser to Ala resulted in complete loss of activity (unpublished results).…”

Characterization of a new thermophilic and acid tolerant esterase from Thermotoga maritima capable of hydrolytic resolution of racemic ketoprofen ethyl ester

“…6B and C. About 41.1% conversion of (S)-ketoprofen was obtained after a reaction time of 23 h and c increased very little (c was 45.2% for 60 h) after 23 h. The highest E value of (S)-ketoprofen was 91.4 and the ee p was 95.7% after 23 h. Keroprofen [(R,S)-2-(3-benzoyl-phenyl) propionic acid] is one of the most prevalent anti-inflammatory drugs (NSAIDs) and only (S)-ketoprofen is pharmacologically active to act to reduce inflammation and alleviate pain [41]. Esterases from the mesophilic organisms are known to have a high specificity for the hydrolysis of racemic ketoprofen ester [42][43][44]. However, so far only one thermophilic esterase Est3 from S. solfataricus with a strict stereoselectivity toward (S)-ketoprofen was identified and characterized [5].…”