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Molecular cloning of enantioselective ester hydrolase from Bacillus pumilus DBRL-191

  1. Shafaq Rasool,
  2. Sarojini Johri,
  3. Syed Riyaz-ul-Hassan,
  4. Qurrat-ul-Ain Maqbool,
  5. Vijeshwar Verma*,
  6. Surrinder Koul,
  7. Subhash C. Taneja,
  8. Ghulam N. Qazi

Article first published online: 9 JAN 2006

DOI: 10.1016/j.femsle.2005.06.022

Issue

FEMS Microbiology Letters

FEMS Microbiology Letters

Volume 249, Issue 1, pages 113–120, August 2005

Additional Information

How to Cite

Rasool, S., Johri, S., Riyaz-ul-Hassan, S., Maqbool, Q.-u.-A., Verma, V., Koul, S., Taneja, S. C. and Qazi, G. N. (2005), Molecular cloning of enantioselective ester hydrolase from Bacillus pumilus DBRL-191. FEMS Microbiology Letters, 249: 113–120. doi: 10.1016/j.femsle.2005.06.022

Author Information

  1. Biotechnology Division, Regional Research Laboratory, Canal Road, Jammu Tawi 180001, India

* *Corresponding author. Tel.: +91 191 2571163; fax: +91 191 2543829., E-mail address: v_verma2k@rediffmail.com

Publication History

  1. Issue published online: 9 JAN 2006
  2. Article first published online: 9 JAN 2006
  3. Received 21 May 2005, Accepted 3 June 2005

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Keywords:

  • Phenyl–Sepharose;
  • Drug intermediates;
  • Kinetic resolution;
  • Enantioselective hydrolysis

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? 33–103), ethyl 3-hydroxy-3-phenylpropanoate (E? 45–71), trans-4-fluorophenyl-3-hydroxymethyl-N-methylpiperidine (E? 10–13) and ethyl 2-hydroxy-4-phenylbutyrate (E? 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 ?19.2 kD and pI ? 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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