Rodanaza i transferaza siarkowa 3-merkaptopirogronianu - enzymy pokrewne ewolucyjnie

• Authors: Maria Wróbel , Halina Jurkowska , Marta Kaczor , Tomasz Uchacz

Title variants

EN

Rhodanese and 3-mercaptopyruvate sulfurtransferase - evolutionary related enzymes

• Languages of publication: PL EN

Abstracts

PL

Endogenne związki siarki odgrywają ważną rolę w przebiegu wielu fizjologicznych procesów w organizmie, takich jak: stabilizacja struktury białek, regulacja aktywności enzymów oraz udział w procesach utleniania i redukcji (glutation, tioredoksyna). Transferazy siarkowe: rodanaza (transferaza siarkowa tiosiarczanu, EC 2.8.1.1) i transferaza siarkowa 3-merkaptopirogronianu (MPST, EC 2.8.1.2) są szeroko rozpowszechnionymi enzymami w świecie organizmów prokariotycznych i eukariotycznych. W komórkach ssaków MPST występuje w cytoplazmie i mitochondriach, zaś rodanaza głównie w mitochondriach. W przypadku niższych kręgowców takich jak: płazy, gady i ryby jej aktywność stwierdzono również w cytozolu. Rodanaza przenosi atomy siarki z anionowych donorów (związki zawierające siarkę sulfanową) na różne nukleofilowe akceptory. MPST katalizuje przeniesienie atomu siarki z 3-merkaptopirogronianu na nukleofilowe akceptory wytwarzając związki zawierające atomy siarki sulfanowej (jak np.: tiosiarczan) lub uwalnia ją w postaci siarkowodoru. Rodanaza i MPST są enzymami pokrewnymi ewolucyjnie. Świadczą o tym podobieństwa w strukturze genów, struktura trzeciorzędowej obydwu białek oraz strukturze miejsca aktywnego. Masy cząsteczkowe obydwu enzymów są podobne - około 33 kDa. Ponadto, enzymy te mają podobne właściwości fizykochemiczne i katalityczne. Aktywność katalityczna obydwu zaangażowanych w przemiany L-cysteiny enzymów zależna jest od reszty cysteinowej centrum aktywnego. Podczas katalizy enzymy te oscylują pomiędzy dwoma stabilnymi stanami: niezwiązanym z atomem siarki i związanym z dwuwartościowym atomem siarki z utworzeniem nadsiarczku z grupą tiolową miejsca aktywnego. Związki chemiczne zanieczyszczające środowisko i ksenobiotyki mogą łączyć się z grupami -SH tych enzymów obniżając ich aktywność i zmieniając poziom siarki sulfanowej - produktu desulfuracji L-cysteiny. Cysteina miejsca aktywnego enzymów tiolowych może uczestniczyć w procesach utlenienia i redukcji; MPST i rodanaza mogą funkcjonować jako miejscowe białkowe przeciwutleniacze. Reaktywne formy tlenu modyfikujące białka sygnałowe i/lub czynniki transkrypcyjne mogą wpływać na ekspresję genów, w tym również genu dla rodanazy, co ze względu na potencjalne terapeutyczne efekty może być interesujące z punktu widzenia medycyny molekularnej.

EN

Endogenous sulfur-containing compounds play an important role in numerous physiological processes in organisms, such as stabilization of protein structure, regulation of enzymatic activity, and they are engaged in redox reactions (glutathione, thioredoxine). Sulfurtransferases are enzymes widespread in nature. Rhodanese (thiosulfate sulfurtransferase, EC 2.8.1.1) and 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2) have been found in the majority of living organism. In animal cells, MPST is located in cytosol and mitochondria, while rhodanese distribution is restricted to mitochondria. In lower vertebrates, such as amphibians, reptiles and fish, it has been also detected in cytosol. Rhodanese transfers sulfur atoms from various donors (sulfane sulfur-containing compounds) to various acceptors. MPST catalyses the transfer of the sulfur atom from 3-mercaptopyruvate to various acceptors, producing sulfane sulfur containing compounds (e.g. thiosulfate), or releases it as hydrogen sulfide. Rhodanese and MPST are evolutionary related enzymes. Both of them have similar structure of gene, protein tertiary structure and the structure of active site. Molecular weight is also comparable - about 33 kDa. Moreover, they have similar physicochemical and catalytic properties. The catalytic activity of these two enzymes participating in L-cysteine metabolism depends on cysteine residues in their active sites. During catalysis, enzymes cycle between two stable intermediates: a sulfur-free form and a sulfur-substituted enzyme containing a divalent sulfur atom bound by persulfide linkage to the sulfhydryl group of the active site. Pollutants and xenobiotics can bind to -SH groups and, therefore, lower the activity of enzymes and change the level of sulfane sulfur, a product of L-cysteine desulfuration. The catalytic site cysteine of a thiol enzyme is redox active; MPST and rhodanese could locally serve as antioxidant proteins. Reactive oxygen species modify signal proteins and/or transcription factors and have an impact on rhodanese gene expression. It is interesting from the point of view of molecular medicine because of potential therapeutic effects.

• Journal: Kosmos
• Year: 2012
• Volume: 61
• Issue: 2
• Pages: 233-244

Dates

published

2012

Contributors

author

Maria Wróbel

• Katedra Biochemii Lekarskiej UJ CM, Kopernika 7, 31-034 Kraków, Polska

author

Halina Jurkowska

• Katedra Biochemii Lekarskiej UJ CM, Kopernika 7, 31-034 Kraków, Polska

author

Marta Kaczor

• Katedra Biochemii Lekarskiej UJ CM, Kopernika 7, 31-034 Kraków, Polska

author

Tomasz Uchacz

• Katedra Biochemii Lekarskiej UJ CM, Kopernika 7, 31-034 Kraków, Polska

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