Nadp+-Dependent Dehydrogenase Activity Of Carbonyl Reductase On Glutathionyl-Hydroxynonanal As A New Pathway For Hydroxynonenal Detoxification. (Articolo in rivista)

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  • Nadp+-Dependent Dehydrogenase Activity Of Carbonyl Reductase On Glutathionyl-Hydroxynonanal As A New Pathway For Hydroxynonenal Detoxification. (Articolo in rivista) (literal)
Anno
  • 2015-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.freeradbiomed.2015.02.001 (literal)
Alternative label
  • Moschini R, Peroni E, Rotondo R, Renzone G, Melck D, Cappiello M, Srebot M, Napolitano E, Motta A, Scaloni A, Mura U, Del-Corso A. (2015)
    Nadp+-Dependent Dehydrogenase Activity Of Carbonyl Reductase On Glutathionyl-Hydroxynonanal As A New Pathway For Hydroxynonenal Detoxification.
    in Free radical biology & medicine
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Moschini R, Peroni E, Rotondo R, Renzone G, Melck D, Cappiello M, Srebot M, Napolitano E, Motta A, Scaloni A, Mura U, Del-Corso A. (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.sciencedirect.com/science/article/pii/S0891584915000416 (literal)
Rivista
Note
  • PubMe (literal)
  • cience direct - Elsevier (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • University of Pisa, Department of Biology, Biochemistry Unit, via S. Zeno, 51, 56123, Pisa, Italy. Proteomics & Mass Spectrometry Laboratory, ISPAAM-CNR, via Argine 1085, I-80147, Napoli, Italy. Institute of Biomolecular Chemistry, ICB-CNR, Comprensorio Olivetti, Edificio A, Via Campi Flegrei 34, I-80078 Pozzuoli (Naples), Italy. Health Unit 5 Pisa, Pontedera Hospital, Ginecology and Obstetric Unit, Via Roma 180, 56025 Pontedera, Italy. Scuola Normale Superiore, Piazza dei Cavalieri, Pisa, Italy. University of Pisa, Department of Biology, Biochemistry Unit, via S. Zeno, 51, 56123, Pisa, Italy. Electronic address: antonella.delcorso@unipi.it. (literal)
Titolo
  • Nadp+-Dependent Dehydrogenase Activity Of Carbonyl Reductase On Glutathionyl-Hydroxynonanal As A New Pathway For Hydroxynonenal Detoxification. (literal)
Abstract
  • A NADP+ dependent dehydrogenase activity on 3-glutathionyl-4-hydroxynonanal (GSHNE) was purified to electrophoretic homogeneity from a line of human astrocytoma cells (ADF). Proteomic analysis identified this enzymatic activity as associated with carbonyl reductase 1 (E.C. 1.1.1.184). The enzyme is highly efficient at catalyzing the oxidation of GSHNE (KM33µM,kcat.405min-1), as it is practically inactive towards trans-4-hydroxy-2-nonenal (HNE) and other HNE-addicted thiol-containing amino acid derivatives. Combined mass spectrometry and nuclear magnetic resonance spectroscopy analysis of the reaction products revealed that carbonyl reductase oxidizes the hydroxyl group of GSHNE in its hemiacetal form, with the formation of the corresponding 3-glutathionyl-nonanoic-?-lactone. The relevance of this new reaction catalyzed by carbonyl reductase 1 is discussed in terms of HNE detoxification and the recovery of reducing power. (literal)
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