ArticleBiochemistry2017
Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 58 citations in OpenAlex.
- Redox-dependent binding and conformational equilibria govern the fluorescence decay of NAD(P)H in living cells.FEBS letters · 2025Article
- A Tight-Knit Family: The Medium-Chain Dehydrogenase/Reductases of Monoterpene Indole Alkaloid Biosynthesis.Biochemistry · 2025Review
- Engineering of Transmembrane Alkane Monooxygenases to Improve a Key Reaction Step in the Synthesis of Polymer Precursor Tulipalin A.Angewandte Chemie (International ed. in English) · 2025Article
- In silico evaluation of N-aryl-1,10-phenanthroline-2-amines as potential inhibitors of T. cruzi GP63 zinc-metalloprotease by docking and molecular dynamics simulations.Scientific reports · 2025Article
- A pH-dependent shift of redox cofactor specificity in a benzyl alcohol dehydrogenase of aromatoleum aromaticum EbN1.Applied microbiology and biotechnology · 2024Article
- The metal cofactor: stationary or mobile?Applied microbiology and biotechnology · 2024Review
- Substitution of both histidines in the active site of yeast alcohol dehydrogenase 1 exposes underlying pH dependencies.Chemico-biological interactions · 2024Article
- Enhanced active-site electric field accelerates enzyme catalysis.Nature chemistry · 2023Article
- Specific base catalysis by yeast alcohol dehydrogenase I with substitutions of histidine-48 by glutamate or serine residues in the proton relay system.Chemico-biological interactions · 2023Article
- Supersulfide catalysis for nitric oxide and aldehyde metabolism.Science advances · 2023Article
- NAD(P)H binding configurations revealed by time-resolved fluorescence and two-photon absorption.Biophysical journal · 2023Article
- Structural and Biochemical Analyses of the Butanol Dehydrogenase fromInternational journal of molecular sciences · 2023Article
- Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.Angewandte Chemie (International ed. in English) · 2022Article
- Dependence of crystallographic atomic displacement parameters on temperature (25-150 K) for complexes of horse liver alcohol dehydrogenase.Acta crystallographica. Section D, Structural biology · 2022Article
- Hydride Transfer Mechanism of Enzymatic Sugar Nucleotide C2 Epimerization Probed with a Loose-Fit CDP-Glucose Substrate.ACS catalysis · 2022Article
- The Thr45Gly substitution in yeast alcohol dehydrogenase substantially decreases catalysis, alters pH dependencies, and disrupts the proton relay system.Chemico-biological interactions · 2021Article
- Alternative binding modes in abortive NADH-alcohol complexes of horse liver alcohol dehydrogenase.Archives of biochemistry and biophysics · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
During catalysis by liver alcohol dehydrogenase (ADH), a water bound to the catalytic zinc is replaced by the oxygen of the substrates. The mechanism might involve a pentacoordinated zinc or a double-displacement reaction with participation by a nearby glutamate residue, as suggested by studies of human ADH3, yeast ADH1, and some other tetrameric ADHs. Zinc coordination and participation of water in the enzyme mechanism were investigated by X-ray crystallography. The apoenzyme and its complex with adenosine 5'-diphosphoribose have an open protein conformation with the catalytic zinc in one position, tetracoordinated by Cys-46, His-67, Cys-174, and a water molecule. The bidentate chelators 2,2'-bipyridine and 1,10-phenanthroline displace the water and form a pentacoordinated zinc. The enzyme-NADH complex has a closed conformation similar to that of ternary complexes with coenzyme and substrate analogues; the coordination of the catalytic zinc is similar to that found in the apoenzyme, except that a minor, alternative position for the catalytic zinc is ∼1.3 Å from the major position and closer to Glu-68, which could form the alternative coordination to the catalytic zinc. Complexes with NADH and N-1-methylhexylformamide or N-benzylformamide (or with NAD
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