Molecular cloning of enantioselective ester hydrolase from  Bacillus pumilus  DBRL‐191 | Zendy

Rasool Shafaq | Zendy; Johri Sarojini | Zendy; RiyazulHassan Syed | Zendy; Maqbool QurratulAin | Zendy; Verma Vijeshwar | Zendy; Koul Surrinder | Zendy; Taneja Subhash C. | Zendy; Qazi Ghulam N. | Zendy

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

Author(s) -

Rasool Shafaq,

Johri Sarojini,

RiyazulHassan Syed,

Maqbool QurratulAin,

Verma Vijeshwar,

Koul Surrinder,

Taneja Subhash C.,

Qazi Ghulam N.

Publication year - 2005

Publication title -

fems microbiology letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.899

H-Index - 151

eISSN - 1574-6968

pISSN - 0378-1097

DOI - 10.1016/j.femsle.2005.06.022

Subject(s) - bacillus pumilus , enantioselective synthesis , cloning (programming) , molecular cloning , chemistry , biology , biochemistry , genetics , bacteria , gene , peptide sequence , computer science , catalysis , programming language

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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