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Discovery and characterization of a second extremely thermostable (+)-γ-lactamase from Sulfolobus solfataricus P2

Paper ID Volume ID Publish Year Pages File Format Full-Text
20106 43158 2016 7 PDF Available
Title
Discovery and characterization of a second extremely thermostable (+)-γ-lactamase from Sulfolobus solfataricus P2
Abstract

A thermostable formamidase from the hyperthermophilic archaeon Sulfolobus solfataricus P2 was revealed to be a novel, thermostable (+)-γ-lactamase. This (+)-γ-lactamase (Sso2810) is composed of only 318 amino acid residues, in contrast to a previously reported (+)-γ-lactamase (Sso2122) with 504 amino acid residues from the same strain. Herein, we demonstrate that a single strain may contain diverse (+)-γ-lactamases. The gene of this thermostable (+)-γ-lactamase was cloned, functionally expressed in Escherichia coli BL21 and purified by a simple yet effective heat treatment method. Sso2810 was biochemically characterized and compared to Sso2122, with phylogenetic analysis indicating different evolutionary histories for the two encoding genes. This newly found thermostable enzyme shows promising properties for industrial applications; specifically, it could be used for the production of chirally pure (−)-γ-lactam for the synthesis of well-known carbocyclic nucleoside antiretroviral agents like Abacavir and Peramivir. The chiral product of the enzyme was purified to >99% enantiomeric excess.

Keywords
Sulfolobus solfataricus; (+)-γ-Lactamase; Stereoselective hydrolysis; Enzyme promiscuity; Nucleotide analogues
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Discovery and characterization of a second extremely thermostable (+)-γ-lactamase from Sulfolobus solfataricus P2
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 121, Issue 5, May 2016, Pages 484–490
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
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