Studium mutací karbonylreduktasy 1 a 3 s důrazem na S-nitrosoglutathion jako substrát a inaktivátor
Charles University in Prague Faculty of Pharmacy in Hradec Králové Department of Biochemical Sciences Candidate: Tereza Hartmanová Supervisor: Dr. Claudia Staab, Dr. Hans-Jörg Martin, Prof. Ing. Vladimír Wsól, Ph.D. Title of the diploma thesis: Studies on carbonyl reductases 1 and 3 variants with em...
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2010
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ndltd-nusl.cz-oai-invenio.nusl.cz-2790602017-06-27T04:40:30Z Studium mutací karbonylreduktasy 1 a 3 s důrazem na S-nitrosoglutathion jako substrát a inaktivátor Studies on carbonyl reductases 1 and 3 variants with emphasis on S-nitrosoglutathione as substrate and inactivator Hartmanová, Tereza Wsól, Vladimír Kvasničková, Eva Charles University in Prague Faculty of Pharmacy in Hradec Králové Department of Biochemical Sciences Candidate: Tereza Hartmanová Supervisor: Dr. Claudia Staab, Dr. Hans-Jörg Martin, Prof. Ing. Vladimír Wsól, Ph.D. Title of the diploma thesis: Studies on carbonyl reductases 1 and 3 variants with emphasis on S-nitrosoglutathione as substrate and inactivator Human CBR1 and CBR3 (carbonyl reductases 1 and 3) are monomeric, NADPH-dependent enzymes belonging to the short chain dehydrogenase/reductase superfamily. Although they are highly similar at the amino acid level (72 % identity) the enzymes exhibit considerable differences in substrate specificity. The CBR1 substrate spectrum is well described, including a variety of compounds e.g. the endogenous indol isatin, S-nitrosoglutathione (GSNO), prostaglandins, quinones, and many carbonyl group bearing xenobiotics. In contrast, CBR3 shows a distinct and much narrower range of substrates and its role is still not fully clarified. Nevertheless, the dissimilar substrate spectra strongly indicate that CBR1 and CBR3 play different metabolic roles. In the present study, the catalytic properties of CBR1 towards the latest CBR1 substrate described, GSNO, were investigated. CBR3 was assessed for potential GSNO-reducing activity, but no in vitro activity was... 2010 info:eu-repo/semantics/masterThesis http://www.nusl.cz/ntk/nusl-279060 eng info:eu-repo/semantics/restrictedAccess |
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English |
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Dissertation |
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Charles University in Prague Faculty of Pharmacy in Hradec Králové Department of Biochemical Sciences Candidate: Tereza Hartmanová Supervisor: Dr. Claudia Staab, Dr. Hans-Jörg Martin, Prof. Ing. Vladimír Wsól, Ph.D. Title of the diploma thesis: Studies on carbonyl reductases 1 and 3 variants with emphasis on S-nitrosoglutathione as substrate and inactivator Human CBR1 and CBR3 (carbonyl reductases 1 and 3) are monomeric, NADPH-dependent enzymes belonging to the short chain dehydrogenase/reductase superfamily. Although they are highly similar at the amino acid level (72 % identity) the enzymes exhibit considerable differences in substrate specificity. The CBR1 substrate spectrum is well described, including a variety of compounds e.g. the endogenous indol isatin, S-nitrosoglutathione (GSNO), prostaglandins, quinones, and many carbonyl group bearing xenobiotics. In contrast, CBR3 shows a distinct and much narrower range of substrates and its role is still not fully clarified. Nevertheless, the dissimilar substrate spectra strongly indicate that CBR1 and CBR3 play different metabolic roles. In the present study, the catalytic properties of CBR1 towards the latest CBR1 substrate described, GSNO, were investigated. CBR3 was assessed for potential GSNO-reducing activity, but no in vitro activity was... |
author2 |
Wsól, Vladimír |
author_facet |
Wsól, Vladimír Hartmanová, Tereza |
author |
Hartmanová, Tereza |
spellingShingle |
Hartmanová, Tereza Studium mutací karbonylreduktasy 1 a 3 s důrazem na S-nitrosoglutathion jako substrát a inaktivátor |
author_sort |
Hartmanová, Tereza |
title |
Studium mutací karbonylreduktasy 1 a 3 s důrazem na S-nitrosoglutathion jako substrát a inaktivátor |
title_short |
Studium mutací karbonylreduktasy 1 a 3 s důrazem na S-nitrosoglutathion jako substrát a inaktivátor |
title_full |
Studium mutací karbonylreduktasy 1 a 3 s důrazem na S-nitrosoglutathion jako substrát a inaktivátor |
title_fullStr |
Studium mutací karbonylreduktasy 1 a 3 s důrazem na S-nitrosoglutathion jako substrát a inaktivátor |
title_full_unstemmed |
Studium mutací karbonylreduktasy 1 a 3 s důrazem na S-nitrosoglutathion jako substrát a inaktivátor |
title_sort |
studium mutací karbonylreduktasy 1 a 3 s důrazem na s-nitrosoglutathion jako substrát a inaktivátor |
publishDate |
2010 |
url |
http://www.nusl.cz/ntk/nusl-279060 |
work_keys_str_mv |
AT hartmanovatereza studiummutacikarbonylreduktasy1a3sdurazemnasnitrosoglutathionjakosubstratainaktivator AT hartmanovatereza studiesoncarbonylreductases1and3variantswithemphasisonsnitrosoglutathioneassubstrateandinactivator |
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1718468623171846144 |