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Title 

Identification, molecular cloning and expression of a new esterase from Pseudomonas sp. KCTC 10122BP with enantioselectivity towards racemic ketoprofen ethyl ester

Authors 

G J KimEun Gyo LeeB GokulM S HahmD PrernaG S ChoiY W RyuHyeon Su RoBong Hyun Chung

Publisher 

Elsevier

Issue Date 

2003

Citation 

Journal of Molecular Catalysis B:Enzymatic, vol. 22, no. 1, pp. 29-35

Keywords 

conversionenantioselectiveesteraseketoprofenpseudomonasamino acidsDNA sequencesescherichia coliestersmolecular cloning

Abstract 

A newly isolated gene from Pseudomonas sp. KCTC 10122BP, encoding an esterase with enantioselectivity towards racemic ketoprofen (rac-ketoprofen) ethyl ester, was cloned in Escherichia coli and its nucleotide sequence determined. The deduced amino acid sequence predicted an open reading frame (ORF) encoding a polypeptide of 381 amino acid residues (1143 nucleotides) with a calculated isoelectric point of pH 5.32 and molecular mass of 41,149Da. The primary structure of the enzyme exhibited a significant level of homology (>31%) with those of related enzymes from various sources and an extreme homology (>81%) with five esterases from the genus Pseudomonas. The enzyme was expressed at a high level in an active form in the soluble fraction and purified to homogeneity by a successive chromatographic procedure. The purified enzyme was determined to be a monomer, plus it exhibited a strict selectivity (>99%) and high activity (2360 units/mg-protein) towards (S)-ketoprofen ethyl ester.

ISSN 

1381-1177

Link 

http://dx.doi.org/10.1016/S1381-1177(02)00308-9

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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