| http://purl.uniprot.org/citations/24611845 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24611845 | http://www.w3.org/2000/01/rdf-schema#comment | "Glutaredoxins (Grxs) are wide-spread oxidoreductases that are found in all kingdoms of life. The yeast Saccharomyces cerevisiae encodes eight Grxs, among which, Grx8 shares a sequence identity of 30 and 23% with typical dithiol Grx1 and Grx2, respectively, but it exhibits a much lower GSH-dependent oxidoreductase activity. To elucidate its catalytic mechanism, we solved the solution structure of Grx8, which displays a typical Grx fold. Structural analysis indicated that Grx8 possesses a negatively charged CXXC motif (Cys(33)-Pro(34)-Asp(35)-Cys(36)) and a GSH-recognition site, which are distinct from Grx1 and Grx2. Subsequent structure-guided site mutations revealed that the D35Y single mutant and N80T/L81V double mutant possess increased activity of 10- and 11-fold, respectively; moreover, the D35Y/N80T/L81V triple mutant has increased activity of up to 44-fold, which is comparable to that of canonical Grx. Biochemical analyses suggested that the increase in catalytic efficiency resulted from a decreased pKa value of catalytic cysteine Cys33 and/or enhancement of the putative GSH-recognition site. Moreover, NMR chemical shift perturbation analyses combined with GSH analogue inhibition assays enabled us to elucidate that wild-type Grx8 and all mutants adopt a ping-pong mechanism of catalysis. All together, these findings provide structural insights into the catalytic mechanism of dithiol Grxs."xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi401293s"xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/author | "Shi Y."xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/author | "Tang Y."xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/author | "Wu J."xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/author | "Xu L."xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/author | "Zhang J."xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/author | "Yu J."xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/author | "Zhou C.Z."xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/pages | "2185-2196"xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/title | "Structure-guided activity enhancement and catalytic mechanism of yeast grx8."xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://purl.uniprot.org/core/volume | "53"xsd:string |
| http://purl.uniprot.org/citations/24611845 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24611845 |
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