The reducing activity of glutaredoxin 3 toward cytoplasmic substrate proteins is restricted by methionine 43.
Identifieur interne : 000C47 ( Main/Exploration ); précédent : 000C46; suivant : 000C48The reducing activity of glutaredoxin 3 toward cytoplasmic substrate proteins is restricted by methionine 43.
Auteurs : Amir Porat [États-Unis] ; Christopher Horst Lillig ; Catrine Johansson ; Aristi Potamitou Fernandes ; Lennart Nilsson ; Arne Holmgren ; Jon BeckwithSource :
- Biochemistry [ 0006-2960 ] ; 2007.
Descripteurs français
- KwdFr :
- Cinétique (MeSH), Escherichia coli (enzymologie), Glutarédoxines (MeSH), Modèles moléculaires (MeSH), Méthionine (génétique), Méthionine (métabolisme), Oxidoreductases (antagonistes et inhibiteurs), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxydoréduction (effets des médicaments et des substances chimiques), Simulation numérique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- antagonistes et inhibiteurs : Oxidoreductases.
- effets des médicaments et des substances chimiques : Oxydoréduction.
- enzymologie : Escherichia coli.
- génétique : Méthionine, Oxidoreductases.
- métabolisme : Méthionine, Oxidoreductases.
- Cinétique, Glutarédoxines, Modèles moléculaires, Simulation numérique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Computer Simulation (MeSH), Escherichia coli (enzymology), Glutaredoxins (MeSH), Kinetics (MeSH), Methionine (genetics), Methionine (metabolism), Models, Molecular (MeSH), Oxidation-Reduction (drug effects), Oxidoreductases (antagonists & inhibitors), Oxidoreductases (genetics), Oxidoreductases (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Oxidoreductases.
- chemical , genetics : Methionine, Oxidoreductases.
- chemical , metabolism : Methionine, Oxidoreductases.
- chemical : Glutaredoxins.
- drug effects : Oxidation-Reduction.
- enzymology : Escherichia coli.
- Amino Acid Sequence, Computer Simulation, Kinetics, Models, Molecular.
Abstract
The reducing proteins glutaredoxin 3 (Grx3) and glutaredoxin 1 (Grx1) are structurally similar but exhibit different specificities toward substrates. Grx1 efficiently reduces ribonucleotide reductase and PAPS reductase, while Grx3 reduces these enzymes inefficiently or not at all. We previously described a selection for Grx3 mutants with increased activity toward substrates of Grx1 in vivo. Remarkably, we repeatedly isolated mutants with changes in only one of the amino acids of Grx3, methionine 43, converting it to either valine, leucine, or isoleucine. In this paper we present additional genetic studies and a biochemical characterization of Grx3-Met43Val, the most efficient mutant. We show that Grx3-Met43Val is able to reduce ribonucleotide reductae and PAPS reductase much more efficiently than the wild-type protein in vitro. The altered protein has an increased Vmax over that of Grx3, nearly the same Vmax as Grx1 while the Km remains high. Molecular dynamics simulations suggest that the Met43Val substitution results in changes in properties of the N-terminal cysteine of the active site leading to a considerably lower pKa. Furthermore, Grx3-Met43Val shows an 11 mV lower redox potential than the wild-type Grx3. These findings provide biochemical and structural explanations for the increased reductive efficiency of the mutant Grx3.
DOI: 10.1021/bi6024353
PubMed: 17305371
PubMed Central: PMC2518409
Affiliations:
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Massachusetts 02115</wicri:regionArea><wicri:noRegion>Massachusetts 02115</wicri:noRegion></affiliation></author><author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></author><author><name sortKey="Johansson, Catrine" sort="Johansson, Catrine" uniqKey="Johansson C" first="Catrine" last="Johansson">Catrine Johansson</name></author><author><name sortKey="Fernandes, Aristi Potamitou" sort="Fernandes, Aristi Potamitou" uniqKey="Fernandes A" first="Aristi Potamitou" last="Fernandes">Aristi Potamitou Fernandes</name></author><author><name sortKey="Nilsson, Lennart" sort="Nilsson, Lennart" uniqKey="Nilsson L" first="Lennart" last="Nilsson">Lennart Nilsson</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author><author><name sortKey="Beckwith, Jon" sort="Beckwith, Jon" uniqKey="Beckwith J" first="Jon" last="Beckwith">Jon Beckwith</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Computer Simulation (MeSH)</term><term>Escherichia coli (enzymology)</term><term>Glutaredoxins (MeSH)</term><term>Kinetics (MeSH)</term><term>Methionine (genetics)</term><term>Methionine (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Oxidation-Reduction (drug effects)</term><term>Oxidoreductases (antagonists & inhibitors)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term><term>Escherichia coli (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Méthionine (génétique)</term><term>Méthionine (métabolisme)</term><term>Oxidoreductases (antagonistes et inhibiteurs)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (effets des médicaments et des substances chimiques)</term><term>Simulation numérique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Methionine</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Methionine</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Oxydoréduction</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Méthionine</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Méthionine</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Computer Simulation</term><term>Kinetics</term><term>Models, Molecular</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Glutarédoxines</term><term>Modèles moléculaires</term><term>Simulation numérique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The reducing proteins glutaredoxin 3 (Grx3) and glutaredoxin 1 (Grx1) are structurally similar but exhibit different specificities toward substrates. Grx1 efficiently reduces ribonucleotide reductase and PAPS reductase, while Grx3 reduces these enzymes inefficiently or not at all. We previously described a selection for Grx3 mutants with increased activity toward substrates of Grx1 in vivo. Remarkably, we repeatedly isolated mutants with changes in only one of the amino acids of Grx3, methionine 43, converting it to either valine, leucine, or isoleucine. In this paper we present additional genetic studies and a biochemical characterization of Grx3-Met43Val, the most efficient mutant. We show that Grx3-Met43Val is able to reduce ribonucleotide reductae and PAPS reductase much more efficiently than the wild-type protein in vitro. The altered protein has an increased Vmax over that of Grx3, nearly the same Vmax as Grx1 while the Km remains high. Molecular dynamics simulations suggest that the Met43Val substitution results in changes in properties of the N-terminal cysteine of the active site leading to a considerably lower pKa. Furthermore, Grx3-Met43Val shows an 11 mV lower redox potential than the wild-type Grx3. These findings provide biochemical and structural explanations for the increased reductive efficiency of the mutant Grx3.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17305371</PMID><DateCompleted><Year>2007</Year><Month>05</Month><Day>16</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>46</Volume><Issue>11</Issue><PubDate><Year>2007</Year><Month>Mar</Month><Day>20</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>The reducing activity of glutaredoxin 3 toward cytoplasmic substrate proteins is restricted by methionine 43.</ArticleTitle><Pagination><MedlinePgn>3366-77</MedlinePgn></Pagination><Abstract><AbstractText>The reducing proteins glutaredoxin 3 (Grx3) and glutaredoxin 1 (Grx1) are structurally similar but exhibit different specificities toward substrates. Grx1 efficiently reduces ribonucleotide reductase and PAPS reductase, while Grx3 reduces these enzymes inefficiently or not at all. We previously described a selection for Grx3 mutants with increased activity toward substrates of Grx1 in vivo. Remarkably, we repeatedly isolated mutants with changes in only one of the amino acids of Grx3, methionine 43, converting it to either valine, leucine, or isoleucine. In this paper we present additional genetic studies and a biochemical characterization of Grx3-Met43Val, the most efficient mutant. We show that Grx3-Met43Val is able to reduce ribonucleotide reductae and PAPS reductase much more efficiently than the wild-type protein in vitro. The altered protein has an increased Vmax over that of Grx3, nearly the same Vmax as Grx1 while the Km remains high. Molecular dynamics simulations suggest that the Met43Val substitution results in changes in properties of the N-terminal cysteine of the active site leading to a considerably lower pKa. Furthermore, Grx3-Met43Val shows an 11 mV lower redox potential than the wild-type Grx3. These findings provide biochemical and structural explanations for the increased reductive efficiency of the mutant Grx3.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Porat</LastName><ForeName>Amir</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Johansson</LastName><ForeName>Catrine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Fernandes</LastName><ForeName>Aristi Potamitou</ForeName><Initials>AP</Initials></Author><Author ValidYN="Y"><LastName>Nilsson</LastName><ForeName>Lennart</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>Arne</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Beckwith</LastName><ForeName>Jon</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM041883</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM041883-17</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM-41883</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM041883-16</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM041883-15</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal 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sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><name sortKey="Johansson, Catrine" sort="Johansson, Catrine" uniqKey="Johansson C" first="Catrine" last="Johansson">Catrine Johansson</name><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name><name sortKey="Nilsson, Lennart" sort="Nilsson, Lennart" uniqKey="Nilsson L" first="Lennart" last="Nilsson">Lennart Nilsson</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Porat, Amir" sort="Porat, Amir" uniqKey="Porat A" first="Amir" last="Porat">Amir Porat</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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