The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity.
Identifieur interne : 000497 ( Main/Exploration ); précédent : 000496; suivant : 000498The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity.
Auteurs : Carsten Berndt [Allemagne] ; Jens-Dirk Schwenn [Allemagne] ; Christopher Horst LilligSource :
- Chemical science [ 2041-6520 ] ; 2015.
Abstract
Thiol-disulfide oxidoreductases from the thioredoxin (Trx) family of proteins have a broad range of well documented functions and possess distinct substrate specificities. The mechanisms and characteristics that control these specificities are key to the understanding of both the reduction of catalytic disulfides as well as allosteric disulfides (thiol switches). Here, we have used the catalytic disulfide of E. coli 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase (PR) that forms between the single active site thiols of two monomers during the reaction cycle as a model system to investigate the mechanisms of Trx and Grx protein specificity. Enzyme kinetics, ΔE'0 determination, and structural analysis of various Trx and Grx family members suggested that the redox potential does not determine specificity nor efficiency of the redoxins as reductant for PR. Instead, the efficiency of PR with various redoxins correlated strongly to the extent of a negative electric field of the redoxins reaching into the solvent outside the active site, and electrostatic and geometric complementary contact surfaces. These data suggest that, in contrast to common assumption, the composition of the active site motif is less important for substrate specificity than other amino acids in or even outside the immediate contact area.
DOI: 10.1039/c5sc01501d
PubMed: 29861944
PubMed Central: PMC5947528
Affiliations:
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Email: horst@lillig.de ; ; Tel: +49 3834 86 5407.</nlm:affiliation><wicri:noCountry code="subField">Germany </wicri:noCountry></affiliation></author></analytic><series><title level="j">Chemical science</title><idno type="ISSN">2041-6520</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thiol-disulfide oxidoreductases from the thioredoxin (Trx) family of proteins have a broad range of well documented functions and possess distinct substrate specificities. The mechanisms and characteristics that control these specificities are key to the understanding of both the reduction of catalytic disulfides as well as allosteric disulfides (thiol switches). Here, we have used the catalytic disulfide of <i>E. coli</i> 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase (PR) that forms between the single active site thiols of two monomers during the reaction cycle as a model system to investigate the mechanisms of Trx and Grx protein specificity. Enzyme kinetics, Δ<i>E</i>'<sub>0</sub> determination, and structural analysis of various Trx and Grx family members suggested that the redox potential does not determine specificity nor efficiency of the redoxins as reductant for PR. Instead, the efficiency of PR with various redoxins correlated strongly to the extent of a negative electric field of the redoxins reaching into the solvent outside the active site, and electrostatic and geometric complementary contact surfaces. These data suggest that, in contrast to common assumption, the composition of the active site motif is less important for substrate specificity than other amino acids in or even outside the immediate contact area.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">29861944</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">2041-6520</ISSN><JournalIssue CitedMedium="Print"><Volume>6</Volume><Issue>12</Issue><PubDate><Year>2015</Year><Month>Dec</Month><Day>01</Day></PubDate></JournalIssue><Title>Chemical science</Title><ISOAbbreviation>Chem Sci</ISOAbbreviation></Journal><ArticleTitle>The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity.</ArticleTitle><Pagination><MedlinePgn>7049-7058</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1039/c5sc01501d</ELocationID><Abstract><AbstractText>Thiol-disulfide oxidoreductases from the thioredoxin (Trx) family of proteins have a broad range of well documented functions and possess distinct substrate specificities. The mechanisms and characteristics that control these specificities are key to the understanding of both the reduction of catalytic disulfides as well as allosteric disulfides (thiol switches). Here, we have used the catalytic disulfide of <i>E. coli</i> 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase (PR) that forms between the single active site thiols of two monomers during the reaction cycle as a model system to investigate the mechanisms of Trx and Grx protein specificity. Enzyme kinetics, Δ<i>E</i>'<sub>0</sub> determination, and structural analysis of various Trx and Grx family members suggested that the redox potential does not determine specificity nor efficiency of the redoxins as reductant for PR. Instead, the efficiency of PR with various redoxins correlated strongly to the extent of a negative electric field of the redoxins reaching into the solvent outside the active site, and electrostatic and geometric complementary contact surfaces. 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