ArticleCellular and molecular life sciences : CMLS2011
Kinetic and structural evidence of the alkenal/one reductase specificity of human ζ-crystallin.
Article in Cellular and molecular life sciences : CMLS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Transcriptomic and proteomic retinal pigment epithelium signatures of age-related macular degeneration.Nature communications · 2022Article
- Structural Insights into the NAD(P)H:Quinone Oxidoreductase fromACS omega · 2022Article
- Activation of farnesoid X receptor (FXR) induces crystallin zeta expression in mouse medullary collecting duct cells.Pflugers Archiv : European journal of physiology · 2020Article
- Zeta-crystallin: a moonlighting player in cancer.Cellular and molecular life sciences : CMLS · 2020Review
- Crystal Structure of the Chloroplastic Oxoene Reductase ceQORH fromFrontiers in plant science · 2017Article
- Direct evidence for a covalent ene adduct intermediate in NAD(P)H-dependent enzymes.Nature chemical biology · 2014Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Human ζ-crystallin is a Zn(2+)-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 Zn(2+)-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.
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Registered trials
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