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Enantioselective ester hydrolase from Sphingobacterium sp. 238C5 useful for chiral resolution of β-phenylalanine and for its β-peptide synthesis
- Source :
-
Journal of Molecular Catalysis B: Enzymatic . Oct2009, Vol. 60 Issue 3/4, p138-144. 7p. - Publication Year :
- 2009
-
Abstract
- Abstract: A novel enzyme, β-phenylalanine ester hydrolase, useful for chiral resolution of β-phenylalanine and for its β-peptide synthesis was characterized. The enzyme purified from the cell free-extract of Sphingobacterium sp. 238C5 well hydrolyzed β-phenylalanine esters (S)-stereospecifically. Besides β-phenylalanine esters, the enzyme catalyzed the hydrolysis of several α-amino acid esters with l-stereospecificity, while the deduced 369 amino acid sequence of the enzyme exhibited homology to alkaline d-stereospecific peptide hydrolases from Bacillus strains. Escherichia coli transformant expressing the β-phenylalanine ester hydrolase gene exhibited an about 8-fold increase in specific (S)-β-phenylalanine ethyl ester hydrolysis as compared with that of Sphingobacterium sp. 238C5. The E. coli transformant showed (S)-enantiomer specific esterase activity in the reaction with a low concentration (30mM) of β-phenylalanine ethyl ester, while it showed both esterase and transpeptidase activity in the reaction with a high concentration (170mM) of β-phenylalanine ethyl ester and produced β-phenylalanyl-β-phenylalanine ethyl ester. This transpeptidase activity was useful for β-phenylalanine β-peptide synthesis. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 13811177
- Volume :
- 60
- Issue :
- 3/4
- Database :
- Academic Search Index
- Journal :
- Journal of Molecular Catalysis B: Enzymatic
- Publication Type :
- Academic Journal
- Accession number :
- 43619936
- Full Text :
- https://doi.org/10.1016/j.molcatb.2009.04.011