300-Fold Increase in Production of the Zn2+-Dependent Dechlorinase TrzN in Soluble Form via Apoenzyme Stabilization
Identifieur interne : 003C75 ( Main/Curation ); précédent : 003C74; suivant : 003C76300-Fold Increase in Production of the Zn2+-Dependent Dechlorinase TrzN in Soluble Form via Apoenzyme Stabilization
Auteurs : Colin J. Jackson [Australie, France] ; Christopher W. Coppin [Australie] ; Paul D. Carr [Australie] ; Alexey Aleksandrov [France] ; Matthew Wilding [Australie] ; Elena Sugrue [Australie] ; Joanna Ubels [Australie] ; Michael Paks [Australie] ; Janet Newman [Australie] ; Thomas S. Peat [Australie] ; Robyn J. Russell [Australie] ; Martin Field [France] ; Martin Weik [France] ; John G. Oakeshott [Australie] ; Colin Scott [Australie]Source :
- Applied and Environmental Microbiology [ 0099-2240 ] ; 2014.
Descripteurs français
- KwdFr :
- Apoenzymes (), Apoenzymes (biosynthèse), Apoenzymes (génétique), Arthrobacter (enzymologie), Cinétique, Conformation des protéines, Cristallographie aux rayons X, Escherichia coli (enzymologie), Escherichia coli (métabolisme), Herbicides (métabolisme), Hydrolases (), Hydrolases (biosynthèse), Hydrolases (génétique), Hydrolyse, Modèles moléculaires, Mutation faux-sens, Protéines mutantes (), Protéines mutantes (biosynthèse), Protéines mutantes (génétique), Protéines recombinantes (), Protéines recombinantes (biosynthèse), Protéines recombinantes (génétique), Simulation numérique, Solubilité, Stabilité enzymatique, Triazines (métabolisme).
- MESH :
- biosynthèse : Apoenzymes, Hydrolases, Protéines mutantes, Protéines recombinantes.
- enzymologie : Arthrobacter, Escherichia coli.
- génétique : Apoenzymes, Hydrolases, Protéines mutantes, Protéines recombinantes.
- métabolisme : Escherichia coli, Herbicides, Triazines.
- Apoenzymes, Cinétique, Conformation des protéines, Cristallographie aux rayons X, Hydrolases, Hydrolyse, Modèles moléculaires, Mutation faux-sens, Protéines mutantes, Protéines recombinantes, Simulation numérique, Solubilité, Stabilité enzymatique.
English descriptors
- KwdEn :
- Apoenzymes (biosynthesis), Apoenzymes (chemistry), Apoenzymes (genetics), Arthrobacter (enzymology), Computer Simulation, Crystallography, X-Ray, Enzyme Stability, Escherichia coli (enzymology), Escherichia coli (metabolism), Herbicides (metabolism), Hydrolases (biosynthesis), Hydrolases (chemistry), Hydrolases (genetics), Hydrolysis, Kinetics, Models, Molecular, Mutant Proteins (biosynthesis), Mutant Proteins (chemistry), Mutant Proteins (genetics), Mutation, Missense, Protein Conformation, Recombinant Proteins (biosynthesis), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Solubility, Triazines (metabolism).
- MESH :
- chemical , biosynthesis : Apoenzymes, Hydrolases, Mutant Proteins, Recombinant Proteins.
- chemical , chemistry : Apoenzymes, Hydrolases, Mutant Proteins, Recombinant Proteins.
- chemical , genetics : Apoenzymes, Hydrolases, Mutant Proteins, Recombinant Proteins.
- enzymology : Arthrobacter, Escherichia coli.
- metabolism : Escherichia coli, Herbicides, Triazines.
- Computer Simulation, Crystallography, X-Ray, Enzyme Stability, Hydrolysis, Kinetics, Models, Molecular, Mutation, Missense, Protein Conformation, Solubility.
Abstract
Microbial metalloenzymes constitute a large library of biocatalysts, a number of which have already been shown to catalyze the breakdown of toxic chemicals or industrially relevant chemical transformations. However, while there is considerable interest in harnessing these catalysts for biotechnology, for many of the enzymes, their large-scale production in active, soluble form in recombinant systems is a significant barrier to their use. In this work, we demonstrate that as few as three mutations can result in a 300-fold increase in the expression of soluble TrzN, an enzyme from
Url:
DOI: 10.1128/AEM.00916-14
PubMed: 24771025
PubMed Central: 4054219
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PMC:4054219Le document en format XML
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-Dependent Dechlorinase TrzN in Soluble Form via Apoenzyme Stabilization</title>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">300-Fold Increase in Production of the Zn<sup>2+</sup>
-Dependent Dechlorinase TrzN in Soluble Form via Apoenzyme Stabilization</title>
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<author><name sortKey="Ubels, Joanna" sort="Ubels, Joanna" uniqKey="Ubels J" first="Joanna" last="Ubels">Joanna Ubels</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Apoenzymes (biosynthesis)</term>
<term>Apoenzymes (chemistry)</term>
<term>Apoenzymes (genetics)</term>
<term>Arthrobacter (enzymology)</term>
<term>Computer Simulation</term>
<term>Crystallography, X-Ray</term>
<term>Enzyme Stability</term>
<term>Escherichia coli (enzymology)</term>
<term>Escherichia coli (metabolism)</term>
<term>Herbicides (metabolism)</term>
<term>Hydrolases (biosynthesis)</term>
<term>Hydrolases (chemistry)</term>
<term>Hydrolases (genetics)</term>
<term>Hydrolysis</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Mutant Proteins (biosynthesis)</term>
<term>Mutant Proteins (chemistry)</term>
<term>Mutant Proteins (genetics)</term>
<term>Mutation, Missense</term>
<term>Protein Conformation</term>
<term>Recombinant Proteins (biosynthesis)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Solubility</term>
<term>Triazines (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Apoenzymes ()</term>
<term>Apoenzymes (biosynthèse)</term>
<term>Apoenzymes (génétique)</term>
<term>Arthrobacter (enzymologie)</term>
<term>Cinétique</term>
<term>Conformation des protéines</term>
<term>Cristallographie aux rayons X</term>
<term>Escherichia coli (enzymologie)</term>
<term>Escherichia coli (métabolisme)</term>
<term>Herbicides (métabolisme)</term>
<term>Hydrolases ()</term>
<term>Hydrolases (biosynthèse)</term>
<term>Hydrolases (génétique)</term>
<term>Hydrolyse</term>
<term>Modèles moléculaires</term>
<term>Mutation faux-sens</term>
<term>Protéines mutantes ()</term>
<term>Protéines mutantes (biosynthèse)</term>
<term>Protéines mutantes (génétique)</term>
<term>Protéines recombinantes ()</term>
<term>Protéines recombinantes (biosynthèse)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Simulation numérique</term>
<term>Solubilité</term>
<term>Stabilité enzymatique</term>
<term>Triazines (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Apoenzymes</term>
<term>Hydrolases</term>
<term>Mutant Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Apoenzymes</term>
<term>Hydrolases</term>
<term>Mutant Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Apoenzymes</term>
<term>Hydrolases</term>
<term>Mutant Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Apoenzymes</term>
<term>Hydrolases</term>
<term>Protéines mutantes</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arthrobacter</term>
<term>Escherichia coli</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arthrobacter</term>
<term>Escherichia coli</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Apoenzymes</term>
<term>Hydrolases</term>
<term>Protéines mutantes</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term>
<term>Herbicides</term>
<term>Triazines</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term>
<term>Herbicides</term>
<term>Triazines</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Computer Simulation</term>
<term>Crystallography, X-Ray</term>
<term>Enzyme Stability</term>
<term>Hydrolysis</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Mutation, Missense</term>
<term>Protein Conformation</term>
<term>Solubility</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Apoenzymes</term>
<term>Cinétique</term>
<term>Conformation des protéines</term>
<term>Cristallographie aux rayons X</term>
<term>Hydrolases</term>
<term>Hydrolyse</term>
<term>Modèles moléculaires</term>
<term>Mutation faux-sens</term>
<term>Protéines mutantes</term>
<term>Protéines recombinantes</term>
<term>Simulation numérique</term>
<term>Solubilité</term>
<term>Stabilité enzymatique</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>Microbial metalloenzymes constitute a large library of biocatalysts, a number of which have already been shown to catalyze the breakdown of toxic chemicals or industrially relevant chemical transformations. However, while there is considerable interest in harnessing these catalysts for biotechnology, for many of the enzymes, their large-scale production in active, soluble form in recombinant systems is a significant barrier to their use. In this work, we demonstrate that as few as three mutations can result in a 300-fold increase in the expression of soluble TrzN, an enzyme from <named-content content-type="genus-species">Arthrobacter aurescens</named-content>
with environmental applications that catalyzes the hydrolysis of triazine herbicides, in <named-content content-type="genus-species">Escherichia coli</named-content>
. Using a combination of X-ray crystallography, kinetic analysis, and computational simulation, we show that the majority of the improvement in expression is due to stabilization of the apoenzyme rather than the metal ion-bound holoenzyme. This provides a structural and mechanistic explanation for the observation that many compensatory mutations can increase levels of soluble-protein production without increasing the stability of the final, active form of the enzyme. This study provides a molecular understanding of the importance of the stability of metal ion free states to the accumulation of soluble protein and shows that differences between apoenzyme and holoenzyme structures can result in mutations affecting the stability of either state differently.</p>
</div>
</front>
</TEI>
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