Evidence map›Paper›PMID 25157460›Full record

ArticleBiochemistry2014

Yeast alcohol dehydrogenase structure and catalysis.

Savarimuthu Baskar Raj, S Ramaswamy, Bryce V Plapp

Abstract read
In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

63 citing papers in PubMed, 202 citations in OpenAlex.

  1. Robots and Minimal, Physics-Informed Features: A Hybrid Framework for Enzyme Catalysis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  2. Four IgG Antibodies and Protein G Are Shapeshifters.International journal of molecular sciences · 2026
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  17. Microbes vary strategically in their metalation of mononuclear enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Savarimuthu Baskar RajDepartment of Biochemistry, The University of Iowa , Iowa City, Iowa 52242, United States.
S Ramaswamy
Bryce V Plapp
University of Iowa · US

Funding

SPECIFICITY OF ALCOHOL DEHYDROGENASESR01AA000279 · NIAAA · UNIVERSITY OF IOWA · PI PLAPP, BRYCE V · 1985 to 2004
$1.4M
Dynamic and Catalysis by Alcohol DehydrogenasesR01GM078446 · NIGMS · UNIVERSITY OF IOWA · PI PLAPP, BRYCE V · 2006 to 2009
$1.1M
NIAAA NIH HHS AA00279NIAAA NIH HHS R01 AA000279NIGMS NIH HHS R01 GM078446
6 · The paper itself

Abstract

Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during the fermentation of glucose. ADH1 is a homotetramer of subunits with 347 amino acid residues. A structure for ADH1 was determined by X-ray crystallography at 2.4 Å resolution. The asymmetric unit contains four different subunits, arranged as similar dimers named AB and CD. The unit cell contains two different tetramers made up of "back-to-back" dimers, AB:AB and CD:CD. The A and C subunits in each dimer are structurally similar, with a closed conformation, bound coenzyme, and the oxygen of 2,2,2-trifluoroethanol ligated to the catalytic zinc in the classical tetrahedral coordination with Cys-43, Cys-153, and His-66. In contrast, the B and D subunits have an open conformation with no bound coenzyme, and the catalytic zinc has an alternative, inverted coordination with Cys-43, Cys-153, His-66, and the carboxylate of Glu-67. The asymmetry in the dimeric subunits of the tetramer provides two structures that appear to be relevant for the catalytic mechanism. The alternative coordination of the zinc may represent an intermediate in the mechanism of displacement of the zinc-bound water with alcohol or aldehyde substrates. Substitution of Glu-67 with Gln-67 decreases the catalytic efficiency by 100-fold. Previous studies of structural modeling, evolutionary relationships, substrate specificity, chemical modification, and site-directed mutagenesis are interpreted more fully with the three-dimensional structure.

Indexed as

Alcohol DehydrogenaseBiocatalysisCatalytic DomainCrystallography, X-RayModels, MolecularProtein ConformationSaccharomyces cerevisiaeAlcohol Dehydrogenase

Identifiers

PMID25157460
PMCPMC4165444
OpenAlexW2053620269

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.