A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a lipase‐like fold

A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a... AbbreviationsBCEBacillus coagulans carboxylesterase 1CDcircular dichroismEtOAcethyl acetatehMGLhuman monoacylglycerol lipaseIPG1,2‐O‐isopropylideneglycerolpNPAp‐nitrophenyl acetateIntroductionCarboxylester hydrolases (EC 3.1.1.1) are enzymes that catalyze the cleavage or formation of carboxyl ester bonds, being often classified as esterases and lipases, based on experimental data and theoretical hypotheses. Recently, it has been suggested to simply organize carboxylester hydrolases into lipolytic esterases (proposed EC: L3.1.1.1) and nonlipolytic esterases (NLEst, proposed EC: NL3.1.1.1) ; however, they have also been classified, based on their sequence similarity and secondary structure conservation, taking advantage of databases, such as the Lipase Engineering Database (LED), the α/β‐hydrolase Fold Enzyme Family 3DM or ESTHER . Lipolytic esterases and nonlipolytic esterases are useful biocatalysts, especially for the (stereo)selective hydrolysis or synthesis of esters, for the preparation of chiral drugs and their intermediates .Bacteria belonging to the genus Bacillus are known producers of stereoselective carboxylesterases . Lipolytic and nonlipolytic esterases from Bacillus subtilis , Bacillus coagulans , Bacillus amyloliquefaciens , Bacillus stearothermophilus , and generic Bacillus sp. have been identified as excellent biocatalysts for the stereoselective hydrolysis of chiral and prochiral esters. This feature allows for the preparation of structurally different alcohols and carboxylic acids as single enantiomers.Significant attention has been dedicated to the enantioselective hydrolysis of racemic esters of 1,2‐O‐isopropylideneglycerol (IPG or http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Febs Journal Wiley

A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a lipase‐like fold

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Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
Copyright © 2018 Federation of European Biochemical Societies
ISSN
1742-464X
eISSN
1742-4658
D.O.I.
10.1111/febs.14368
Publisher site
See Article on Publisher Site

Abstract

AbbreviationsBCEBacillus coagulans carboxylesterase 1CDcircular dichroismEtOAcethyl acetatehMGLhuman monoacylglycerol lipaseIPG1,2‐O‐isopropylideneglycerolpNPAp‐nitrophenyl acetateIntroductionCarboxylester hydrolases (EC 3.1.1.1) are enzymes that catalyze the cleavage or formation of carboxyl ester bonds, being often classified as esterases and lipases, based on experimental data and theoretical hypotheses. Recently, it has been suggested to simply organize carboxylester hydrolases into lipolytic esterases (proposed EC: L3.1.1.1) and nonlipolytic esterases (NLEst, proposed EC: NL3.1.1.1) ; however, they have also been classified, based on their sequence similarity and secondary structure conservation, taking advantage of databases, such as the Lipase Engineering Database (LED), the α/β‐hydrolase Fold Enzyme Family 3DM or ESTHER . Lipolytic esterases and nonlipolytic esterases are useful biocatalysts, especially for the (stereo)selective hydrolysis or synthesis of esters, for the preparation of chiral drugs and their intermediates .Bacteria belonging to the genus Bacillus are known producers of stereoselective carboxylesterases . Lipolytic and nonlipolytic esterases from Bacillus subtilis , Bacillus coagulans , Bacillus amyloliquefaciens , Bacillus stearothermophilus , and generic Bacillus sp. have been identified as excellent biocatalysts for the stereoselective hydrolysis of chiral and prochiral esters. This feature allows for the preparation of structurally different alcohols and carboxylic acids as single enantiomers.Significant attention has been dedicated to the enantioselective hydrolysis of racemic esters of 1,2‐O‐isopropylideneglycerol (IPG or

Journal

Febs JournalWiley

Published: Jan 1, 2018

Keywords: ; ; ; ; ;

References

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