Kinetic and structural evidence of the alkenal/one reductase specificity of human ζ-crystallin

Sergio Porté, Agrin Moeini, Irene Reche, Naeem Shafqat, Udo Oppermann, Jaume Farrés, Xavier Parés

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15 Citations (Scopus)


Human ζ-crystallin is a Zn2+-lacking medium-chain dehydrogenase/reductase (MDR) included in the quinone oxidoreductase (QOR) family because of its activity with quinones. In the present work a novel enzymatic activity was characterized: the double bond α,β- hydrogenation of medium-chain 2-alkenals and 3-alkenones. The enzyme is especially active with lipid peroxidation products such as 4-hydroxyhexenal, and a role in their detoxification is discussed. This specificity is novel in the QOR family, and it is similar to that described in the distantly related alkenal/one reductase family. Moreover, we report the X-ray structure of ζ-crystallin, which represents the first structure solved for a tetrameric Zn2+-lacking MDR, and which allowed the identification of the active-site lining residues. Docking simulations suggest a role for Tyr53 and Tyr59 in catalysis. The kinetics of Tyr53Phe and Tyr59Phe mutants support the implication of Tyr53 in binding/catalysis of alkenal/one substrates, while Tyr59 is involved in the recognition of 4-OH-alkenals. © 2010 Springer Basel AG.
Original languageEnglish
Pages (from-to)1065-1077
JournalCellular and Molecular Life Sciences
Publication statusPublished - 1 Mar 2011


  • Alkenal/one reductase
  • Double-bond α,β-hydrogenation
  • Lipid peroxidation products
  • Medium-chain dehydrogenases/reductases
  • Quinone oxidoreductase


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