Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9121539 | FEMS Microbiology Letters | 2005 | 8 Pages |
Abstract
A gene from Bacillus pumilus expressed under its native promoter was cloned in Escherichia coli. Recombinant B. pumilus esterase (BPE) affects the kinetic resolution of racemic mixtures such as unsubstituted and substituted 1-(phenyl)ethanols (E â¼Â 33-103), ethyl 3-hydroxy-3-phenylpropanoate (E â¼Â 45-71), trans-4-fluorophenyl-3-hydroxymethyl-N-methylpiperidine (E â¼Â 10-13) and ethyl 2-hydroxy-4-phenylbutyrate (E â¼Â 7). The enzyme is composed of a 34-amino acid signal peptide and a 181-amino acid mature protein corresponding to a molecular weight of â¼19.2 kD and pI â¼Â 9.4. 3-D the structural model of the enzyme built by homology modelling using the atomic coordinates from the crystal structure of B. subtilis lipase (LipA) showed a compact minimal α/β hydrolase fold.
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Authors
Shafaq Rasool, Sarojini Johri, Syed Riyaz-ul-Hassan, Qurrat-ul-Ain Maqbool, Vijeshwar Verma, Surrinder Koul, Subhash C. Taneja, Ghulam N. Qazi,