GlutaredoxinV1, Main, Exploration, bibRecord, 000362

Glutaredoxin catalysis requires two distinct glutathione interaction sites.

Identifieur interne : 000362 ( Main/Exploration ); précédent : 000361; suivant : 000363

Glutaredoxin catalysis requires two distinct glutathione interaction sites.

Auteurs : Patricia Begas [Allemagne] ; Linda Liedgens [Allemagne] ; Anna Moseler [Allemagne] ; Andreas J. Meyer [Allemagne] ; Marcel Deponte [Allemagne]

Source :

Nature communications [ 2041-1723 ] ; 2017.

RBID : pubmed:28374771

Descripteurs français

KwdFr :
- Acide glutamique (métabolisme), Catalyse (MeSH), Cinétique (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (métabolisme), Lysine (métabolisme), Mutation (MeSH), Oxydoréduction (MeSH), Relation structure-activité (MeSH), Sites de fixation (MeSH).
MESH :
- composition chimique : Glutarédoxines.
- génétique : Glutarédoxines.
- métabolisme : Acide glutamique, Glutarédoxines, Glutathion, Lysine.
- Catalyse, Cinétique, Mutation, Oxydoréduction, Relation structure-activité, Sites de fixation.

English descriptors

KwdEn :
- Binding Sites (MeSH), Catalysis (MeSH), Glutamic Acid (metabolism), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (metabolism), Kinetics (MeSH), Lysine (metabolism), Mutation (MeSH), Oxidation-Reduction (MeSH), Structure-Activity Relationship (MeSH).
MESH :
- chemical , chemistry : Glutaredoxins.
- chemical , genetics : Glutaredoxins.
- chemical , metabolism : Glutamic Acid, Glutaredoxins, Glutathione, Lysine.
- Binding Sites, Catalysis, Kinetics, Mutation, Oxidation-Reduction, Structure-Activity Relationship.

Abstract

Glutaredoxins are key players in cellular redox homoeostasis and exert a variety of essential functions ranging from glutathione-dependent catalysis to iron metabolism. The exact structure-function relationships and mechanistic differences among glutaredoxins that are active or inactive in standard enzyme assays have so far remained elusive despite numerous kinetic and structural studies. Here, we elucidate the enzymatic mechanism showing that glutaredoxins require two distinct glutathione interaction sites for efficient redox catalysis. The first site interacts with the glutathione moiety of glutathionylated disulfide substrates. The second site activates glutathione as the reducing agent. We propose that the requirement of two distinct glutathione interaction sites for the efficient reduction of glutathionylated disulfide substrates explains the deviating structure-function relationships, activities and substrate preferences of different glutaredoxin subfamilies as well as thioredoxins. Our model also provides crucial insights for the design or optimization of artificial glutaredoxins, transition-state inhibitors and glutaredoxin-coupled redox sensors.

DOI: 10.1038/ncomms14835
PubMed: 28374771
PubMed Central: PMC5382279

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000354
to stream Main, to step Curation: 000354

Le document en format XML

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<term>Catalysis (MeSH)</term>
<term>Glutamic Acid (metabolism)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Lysine (metabolism)</term>
<term>Mutation (MeSH)</term>
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<term>Structure-Activity Relationship (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Acide glutamique (métabolisme)</term>
<term>Catalyse (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Lysine (métabolisme)</term>
<term>Mutation (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Relation structure-activité (MeSH)</term>
<term>Sites de fixation (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutamic Acid</term>
<term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Lysine</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term>
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<term>Glutarédoxines</term>
<term>Glutathion</term>
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<term>Catalysis</term>
<term>Kinetics</term>
<term>Mutation</term>
<term>Oxidation-Reduction</term>
<term>Structure-Activity Relationship</term>
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<term>Cinétique</term>
<term>Mutation</term>
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<term>Relation structure-activité</term>
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<front><div type="abstract" xml:lang="en">Glutaredoxins are key players in cellular redox homoeostasis and exert a variety of essential functions ranging from glutathione-dependent catalysis to iron metabolism. The exact structure-function relationships and mechanistic differences among glutaredoxins that are active or inactive in standard enzyme assays have so far remained elusive despite numerous kinetic and structural studies. Here, we elucidate the enzymatic mechanism showing that glutaredoxins require two distinct glutathione interaction sites for efficient redox catalysis. The first site interacts with the glutathione moiety of glutathionylated disulfide substrates. The second site activates glutathione as the reducing agent. We propose that the requirement of two distinct glutathione interaction sites for the efficient reduction of glutathionylated disulfide substrates explains the deviating structure-function relationships, activities and substrate preferences of different glutaredoxin subfamilies as well as thioredoxins. Our model also provides crucial insights for the design or optimization of artificial glutaredoxins, transition-state inhibitors and glutaredoxin-coupled redox sensors.</div>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Begas</LastName>
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<ReferenceList><Reference><Citation>FEBS Lett. 2002 Jan 30;511(1-3):145-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11821065</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2003 Jul 11;278(28):25745-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12730244</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1992 Sep 29;31(38):9288-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1390715</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2005 Jul 1;280(26):24544-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15833738</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biol Chem. 2005 Jan;386(1):33-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15843145</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2005 Oct 28;353(3):629-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16181638</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2006 Apr 18;45(15):4785-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16605247</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2006 Nov 3;281(44):33107-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16956877</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):288-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17327665</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Mol Life Sci. 2007 Jun;64(12):1518-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17415523</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant J. 2007 Dec;52(5):973-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17892447</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biol Chem. 2008 Jan;389(1):21-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18095866</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2008 Feb 5;47(5):1452-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18171082</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2008 Apr 4;283(14):8868-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18216016</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Biol Cell. 2008 Jun;19(6):2673-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18400945</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proteins. 2008 Aug 15;72(3):1077-83</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18473363</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eukaryot Cell. 2008 Aug;7(8):1415-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18503006</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2008 Nov;1780(11):1304-17</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18621099</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2008 Nov 21;283(47):32839-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18757366</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2008 Oct 21;47(42):11144-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18816065</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1991 Sep 10;30(36):8883-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1888746</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2009 Jan 23;385(3):889-901</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18992757</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2009 May;11(5):1059-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19119916</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2009 Feb 17;48(6):1410-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19166312</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2009 Nov;1790(11):1486-500</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19376195</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Biosyst. 2010 Jan;6(1):241-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20024086</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2010 May 14;398(4):614-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20347849</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1991 Jul 5;266(19):12759-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2061338</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2012 Jan 1;16(1):17-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21707412</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS J. 2012 Jul;279(14):2568-78</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22607473</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2013 Sep 1;19(7):708-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22978520</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2013 May;1830(5):3217-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23036594</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2013 Aug;1830(8):4073-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23624334</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Microbiol. 2013 Dec;16(6):662-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23962819</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Protein Sci. 2014 Feb;23(2):238-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24243781</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Front Plant Sci. 2013 Dec 16;4:506</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24379821</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2014 Apr 8;53(13):2185-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24611845</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2015 Jun;1853(6):1513-27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25264274</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biol Chem. 2015 May;396(5):401-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25581754</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biol Chem. 2015 May;396(5):495-509</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25781542</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2016 May 1;24(13):680-712</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25867539</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2015 Nov 3;112(44):13735-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26483494</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Chem Sci. 2015 Jul 1;6(7):3788-3796</Citation>
<ArticleIdList><ArticleId IdType="pubmed">29218148</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1968 Apr 25;243(8):1942-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">5646485</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1995;252:283-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7476363</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 1995 May 18;1249(1):29-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7766681</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1976 Jul;73(7):2275-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7783</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1994 Feb 4;235(5):1585-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8107093</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1993 Apr 6;32(13):3368-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8461300</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1997 Mar 18;36(11):3199-206</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9115997</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Electrophoresis. 1997 Dec;18(15):2714-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9504803</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1998 Dec 8;37(49):17145-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9860827</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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Glutaredoxin catalysis requires two distinct glutathione interaction sites.

Glutaredoxin catalysis requires two distinct glutathione interaction sites.

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