@article{ ref52,
  author = {Toppo, S. and Flohe, L. and Ursini, F. and Vanin, S. and Maiorino, M.},
  title = {Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme},
  journal = {Biochimica Et Biophysica Acta-General Subjects},
  volume = {1790},
  number = {11},
  pages = {1486-1500},
  abstract = {Kinetics and molecular mechanisms of GPx-type enzymes are reviewed with emphasis on structural features relevant to efficiency and specificity. In Sec-GPxs the reaction takes place at a single redox centre with selenocysteine as redox-active residue (peroxidatic Sec, Up). In contrast, most of the non-vertebrate GPx have the Up replaced by a cysteine (peroxidatic Cys, C(P)) and work with a second redox centre that contains a resolving cysteine (C(R)). While the former type of enzymes is more or less specific for GSH, the latter are reduced by "redoxins". The common denominator of the GPx family is the first redox centre comprising the (seleno)cysteine, tryptophan, asparagine and glutamine. In this architectural context the rate of hydroperoxide reduction by Up or C(P), respectively, is enhanced by several orders of magnitude compared to that of free selenolate or thiolate. Mammalian GPx-1 dominates H(2)O(2) metabolism, whereas the domain of GPx-4 is the reduction of lipid hydroperoxides with important consequences such as counteracting 12/15-lipoxygenase-induced apoptosis and regulation of inflammatory responses. Beyond, the degenerate GSH specificity of GPx-4 allows selenylation and oxidation to disuffides of protein thiols. Heterodimer formation of yeast GPx with a transcription factor is discussed as paradigm of a redox sensing that might also be valid in vertebrates. (C) 2009 Elsevier B.V. All rights reserved.},
  keywords = {enzyme kinetics
glutathione peroxidases
hydroperoxide
molecular phylogenesis
redox signaling
selenium
tryparedoxin peroxidase
rat-liver
thioredoxin peroxidase
crithidia-fasciculata
trypanosoma-brucei
thiol peroxidase
oxidative stress
sperm maturation
structural basis
selenoprotein-p},
  year = {2009},
  doi = {DOI:10.1016/j.bbagen.2009.04.007},
  url = {<Go to ISI>://000271454600013}
}

{"_id":"uejYAnAwTXyqTbhyo","bibbaseid":"toppo-flohe-ursini-vanin-maiorino-catalyticmechanismsandspecificitiesofglutathioneperoxidasesvariationsofabasicscheme-2009","downloads":0,"creationDate":"2015-05-14T13:09:08.887Z","title":"Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme","author_short":["Toppo, S.","Flohe, L.","Ursini, F.","Vanin, S.","Maiorino, M."],"year":2009,"bibtype":"article","biburl":"http://www.medcomp.medicina.unipd.it/stefano/scopusDef.bib","bibdata":{"abstract":"Kinetics and molecular mechanisms of GPx-type enzymes are reviewed with emphasis on structural features relevant to efficiency and specificity. In Sec-GPxs the reaction takes place at a single redox centre with selenocysteine as redox-active residue (peroxidatic Sec, Up). In contrast, most of the non-vertebrate GPx have the Up replaced by a cysteine (peroxidatic Cys, C(P)) and work with a second redox centre that contains a resolving cysteine (C(R)). While the former type of enzymes is more or less specific for GSH, the latter are reduced by \"redoxins\". The common denominator of the GPx family is the first redox centre comprising the (seleno)cysteine, tryptophan, asparagine and glutamine. In this architectural context the rate of hydroperoxide reduction by Up or C(P), respectively, is enhanced by several orders of magnitude compared to that of free selenolate or thiolate. Mammalian GPx-1 dominates H(2)O(2) metabolism, whereas the domain of GPx-4 is the reduction of lipid hydroperoxides with important consequences such as counteracting 12/15-lipoxygenase-induced apoptosis and regulation of inflammatory responses. Beyond, the degenerate GSH specificity of GPx-4 allows selenylation and oxidation to disuffides of protein thiols. Heterodimer formation of yeast GPx with a transcription factor is discussed as paradigm of a redox sensing that might also be valid in vertebrates. (C) 2009 Elsevier B.V. All rights reserved.","author":["Toppo, S.","Flohe, L.","Ursini, F.","Vanin, S.","Maiorino, M."],"author_short":["Toppo, S.","Flohe, L.","Ursini, F.","Vanin, S.","Maiorino, M."],"bibtex":"@article{ ref52,\n author = {Toppo, S. and Flohe, L. and Ursini, F. and Vanin, S. and Maiorino, M.},\n title = {Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme},\n journal = {Biochimica Et Biophysica Acta-General Subjects},\n volume = {1790},\n number = {11},\n pages = {1486-1500},\n abstract = {Kinetics and molecular mechanisms of GPx-type enzymes are reviewed with emphasis on structural features relevant to efficiency and specificity. In Sec-GPxs the reaction takes place at a single redox centre with selenocysteine as redox-active residue (peroxidatic Sec, Up). In contrast, most of the non-vertebrate GPx have the Up replaced by a cysteine (peroxidatic Cys, C(P)) and work with a second redox centre that contains a resolving cysteine (C(R)). While the former type of enzymes is more or less specific for GSH, the latter are reduced by \"redoxins\". The common denominator of the GPx family is the first redox centre comprising the (seleno)cysteine, tryptophan, asparagine and glutamine. In this architectural context the rate of hydroperoxide reduction by Up or C(P), respectively, is enhanced by several orders of magnitude compared to that of free selenolate or thiolate. Mammalian GPx-1 dominates H(2)O(2) metabolism, whereas the domain of GPx-4 is the reduction of lipid hydroperoxides with important consequences such as counteracting 12/15-lipoxygenase-induced apoptosis and regulation of inflammatory responses. Beyond, the degenerate GSH specificity of GPx-4 allows selenylation and oxidation to disuffides of protein thiols. Heterodimer formation of yeast GPx with a transcription factor is discussed as paradigm of a redox sensing that might also be valid in vertebrates. (C) 2009 Elsevier B.V. All rights reserved.},\n keywords = {enzyme kinetics\nglutathione peroxidases\nhydroperoxide\nmolecular phylogenesis\nredox signaling\nselenium\ntryparedoxin peroxidase\nrat-liver\nthioredoxin peroxidase\ncrithidia-fasciculata\ntrypanosoma-brucei\nthiol peroxidase\noxidative stress\nsperm maturation\nstructural basis\nselenoprotein-p},\n year = {2009},\n doi = {DOI:10.1016/j.bbagen.2009.04.007},\n url = {<Go to ISI>://000271454600013}\n}","bibtype":"article","doi":"DOI:10.1016/j.bbagen.2009.04.007","id":"ref52","journal":"Biochimica Et Biophysica Acta-General Subjects","key":"ref52","keywords":"enzyme kinetics glutathione peroxidases hydroperoxide molecular phylogenesis redox signaling selenium tryparedoxin peroxidase rat-liver thioredoxin peroxidase crithidia-fasciculata trypanosoma-brucei thiol peroxidase oxidative stress sperm maturation structural basis selenoprotein-p","number":"11","pages":"1486-1500","title":"Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme","type":"article","url":"<Go to ISI>://000271454600013","volume":"1790","year":"2009","bibbaseid":"toppo-flohe-ursini-vanin-maiorino-catalyticmechanismsandspecificitiesofglutathioneperoxidasesvariationsofabasicscheme-2009","role":"author","urls":{"Paper":"http://www.medcomp.medicina.unipd.it/stefano/%3CGo%20to%20ISI%3E://000271454600013"},"keyword":["enzyme kinetics glutathione peroxidases hydroperoxide molecular phylogenesis redox signaling selenium tryparedoxin peroxidase rat-liver thioredoxin peroxidase crithidia-fasciculata trypanosoma-brucei thiol peroxidase oxidative stress sperm maturation structural basis selenoprotein-p"],"downloads":0,"html":""},"search_terms":["catalytic","mechanisms","specificities","glutathione","peroxidases","variations","basic","scheme","toppo","flohe","ursini","vanin","maiorino"],"keywords":["enzyme kinetics glutathione peroxidases hydroperoxide molecular phylogenesis redox signaling selenium tryparedoxin peroxidase rat-liver thioredoxin peroxidase crithidia-fasciculata trypanosoma-brucei thiol peroxidase oxidative stress sperm maturation structural basis selenoprotein-p"],"authorIDs":["55549696fe38bf120a0006ed"],"dataSources":["fhoWjCRp5bAHzjBdW"]}