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Yeast Alcohol Dehydrogenase Structure and Catalysis

103/103 checkable references clean · checked 2026-07-22

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

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The 103 checked references that resolve

resolves10.1016/j.cbi.2012.11.008

Origin and evolution of medium chain alcohol dehydrogenases

resolves10.1016/0022-2836(76)90072-3

Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution

resolves10.1016/0022-2836(81)90047-4

Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution

resolves10.1007/s00018-008-8589-x

Medium- and short-chain dehydrogenase/reductase gene and protein families

resolves10.1016/S0021-9258(18)61419-X

Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

resolves10.1111/j.1432-1033.1977.tb11267.x

The Primary Structure of Yeast Alcohol Dehydrogenase

resolves10.1016/S0021-9258(19)81067-0

The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase.

resolves10.1016/S0021-9258(17)34307-7

Subunit conformation of yeast alcohol dehydrogenase.

resolves10.1006/jmbi.1994.1031

Crystallization and Preliminary Crystallographic Studies of Saccharomyces cerevisiae Alcohol Dehydrogenase I

resolves10.1110/ps.03531404

The ternary complex of Pseudomonas aeruginosa alcohol dehydrogenase with NADH and ethylene glycol

resolves10.1038/283214a0

Isolation of the structural gene for alcohol dehydrogenase by genetic complementation in yeast

resolves10.1021/bi00475a009

Substitution of arginine for histidine-47 in the coenzyme binding site of yeast alcohol dehydrogenase I

resolves10.1107/S0108767393007597

AMoRe: an automated package for molecular replacement

resolves10.1107/S0108767390010224

Improved methods for building protein models in electron density maps and the location of errors in these models

resolves10.1016/S0076-6879(97)76068-3

[22] Detecting and overcoming crystal twinning

resolves10.1002/(SICI)1097-0134(19980201)30:2<144::AID-PROT4>3.0.CO;2-N

Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme

resolves10.1002/pro.5560050410

Crystal structure of cod liver class I alcohol dehydrogenase: Substrate pocket and structurally variable segments

resolves10.1016/S0009-2797(02)00222-3

Tetrameric NAD-dependent alcohol dehydrogenase

resolves10.1021/bi049736p

Crystal Structure and Amide H/D Exchange of Binary Complexes of Alcohol Dehydrogenase from Bacillus stearothermophilus: Insight into Thermostability and Cofactor Binding,

resolves10.1016/j.abb.2009.07.001

Conformational changes and catalysis by alcohol dehydrogenase

resolves10.1111/j.1432-1033.1995.tb20689.x

Identification of Residues Potentially Involved in the Interactions Between Subunits in Yeast Alcohol Dehydrogenases

resolves10.1110/ps.0222102

Structural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridging

resolves10.1007/BF00160465

Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family

resolves10.1111/j.1432-1033.1977.tb11268.x

Differences between Alcohol Dehydeogenases

resolves10.1007/s00018-002-8487-6

Differential multiplicity of MDR alcohol dehydrogenases: enzyme genes in the human genome versus those in organisms initially studied

resolves10.1110/ps.035428.108

The Medium‐Chain Dehydrogenase/Reductase Engineering Database: A systematic analysis of a diverse protein family to understand sequence–structure–function relationship

resolves10.1016/j.jmb.2004.06.037

Apo and Holo Structures of an NADP(H)-dependent Cinnamyl Alcohol Dehydrogenase from Saccharomyces cerevisiae

resolves10.1021/bi052554q

Structure−Function Relationships in Human Glutathione-Dependent Formaldehyde Dehydrogenase. Role of Glu-67 and Arg-368 in the Catalytic Mechanism,

resolves10.1006/jmbi.1996.0731

Structure of human χχ alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase

resolves10.1021/bi026705q

Human Glutathione-Dependent Formaldehyde Dehydrogenase. Structural Changes Associated with Ternary Complex Formation

resolves10.1021/bi0257639

Human Glutathione-Dependent Formaldehyde Dehydrogenase. Structures of Apo, Binary, and Inhibitory Ternary Complexes

resolves10.1021/bi00739a013

Active-site sulfhydryl groups of yeast alcohol dehydrogenase

resolves10.1111/j.1432-1033.1976.tb10517.x

Spectroscopic Investigation of Binary and Ternary Coenzyme Complexes of Yeast Alcohol Dehydrogenase

resolves10.1021/bi0272656

Amino Acid Residues in the Nicotinamide Binding Site Contribute to Catalysis by Horse Liver Alcohol Dehydrogenase,

resolves10.1021/bi00386a014

Yeast and horse liver alcohol dehydrogenases: potential problems in target size analysis and evidence for a monomer active unit

resolves10.1021/bi991731i

Substitutions in a Flexible Loop of Horse Liver Alcohol Dehydrogenase Hinder the Conformational Change and Unmask Hydrogen Transfer,

resolves10.1042/bj1470303

A study of the pH- and temperature-dependence of the reactions of yeast alcohol dehydrogenase with ethanol, acetaldehyde and butyraldehyde as substrates

resolves10.1042/bj1470541

A study of the oxidation of butan-1-ol and propan-2-ol by nicotinamide-adenine dinucleotide catalysed by yeast alcohol dehydrogenase.

resolves10.1021/bi00905a007

Product Inhibition Studies on Yeast and Liver Alcohol Dehydrogenases*

resolves10.1016/S0021-9258(19)41638-4

Acid-base catalysis in the yeast alcohol dehydrogenase reaction.

resolves10.1016/S0021-9258(18)66863-2

Interdomain motion in liver alcohol dehydrogenase. Structural and energetic analysis of the hinge bending mode.

resolves10.1021/bi300378n

Atomic-Resolution Structures of Horse Liver Alcohol Dehydrogenase with NAD+ and Fluoroalcohols Define Strained Michaelis Complexes

resolves10.1016/S0021-9258(18)66181-2

THE ENZYMATIC TRANSFER OF HYDROGEN

resolves10.1021/bi401583f

Effects of Cavities at the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase on Structure, Dynamics and Catalysis

resolves10.1016/S0021-9258(19)45387-8

Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase.

resolves10.1042/bj1450581

Evidence for a histidine and a cysteine residue in the substrate-binding site of yeast alcohol dehydrogenase

resolves10.1111/j.1432-1033.1975.tb04031.x

The Role of an Essential Histidine Residue of Yeast Alcohol Dehydrogenase

resolves10.1042/bj1610073

A study of the ionic properties of the essential histidine residue of yeast alcohol dehydrogenase in complexes of the enzyme with its coenzymes and substrates

resolves10.1007/978-1-4684-5901-2_26

Catalysis by Yeast Alcohol Dehydrogenase

resolves10.1021/bi991306p

Control of Coenzyme Binding to Horse Liver Alcohol Dehydrogenase

resolves10.1021/bi036103m

Participation of Histidine-51 in Catalysis by Horse Liver Alcohol Dehydrogenase,

resolves10.1021/bi00644a020

Epoxide inhibition of alcohol dehydrogenases. Identification of modified cysteines in yeast alcohol dehydrogenase and demonstration of reversible and irreversible inhibition of liver alcohol dehydrogenase by styrene oxide

resolves10.1021/bi00183a028

Structures of Horse Liver Alcohol Dehydrogenase Complexed with NAD+ and Substituted Benzyl Alcohols

resolves10.1110/ps.0213502

A structurally conserved water molecule in Rossmann dinucleotide‐binding domains

resolves10.1016/j.cbi.2012.11.010

Bradykinetic alcohol dehydrogenases make yeast fitter for growth in the presence of allyl alcohol

resolves10.1021/bi00327a012

Interaction of pyrophosphate moieties with .alpha.-helixes in dinucleotide-binding proteins

resolves10.1016/0022-2836(86)90409-2

Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint

resolves10.1006/abbi.1999.1242

Probing the Affinity and Specificity of Yeast Alcohol Dehydrogenase I for Coenzymes

resolves10.1021/bi00240a008

An aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme

resolves10.1021/bi00014a027

Substitutions of isoleucine residues at the adenine binding site activate horse liver alcohol dehydrogenase

resolves10.1016/S0021-9258(18)53028-3

Inversion of the substrate specificity of yeast alcohol dehydrogenase.

resolves10.1016/j.cbi.2008.10.037

Activity of yeast alcohol dehydrogenases on benzyl alcohols and benzaldehydes

resolves10.1093/protein/3.6.523

Protein engineering of alcohol dehydrogenases; effects of amino acid changes at positions 93 and 48 of yeast ADH1

resolves10.1016/S0021-9258(18)60436-3

Stereospecific Oxidation of Secondary Alcohols by Human Alcohol Dehydrogenases

resolves10.1093/protein/8.5.457

Engineering yeast alcohol dehydrogenase. Replacing Trp54 by Leu broadens substrate specificity

resolves10.1073/pnas.88.19.8420

Structural determinants of stereospecificity in yeast alcohol dehydrogenase.

resolves10.1021/ja00344a037

Equilibration of 1-octanol with alcohol dehydrogenase. Evidence for horse liver alcohol dehydrogenase responsibility for exchange of the 1-pro-S hydrogen atom

resolves10.1038/214031a0

Substrate Specificity and Stereospecificity of Alcohol Dehydrogenases

resolves10.1042/bj1040165

The specificities and configurations of ternary complexes of yeast and liver alcohol dehydrogenases

resolves10.1042/bj1710629

Estimation of rate dissociation constants involving ternary complexes in reactions catalysed by yeast alcohol dehydrogenase

resolves10.1021/bi00470a005

Rate constants for a mechanism including intermediates in the interconversion of ternary complexes by horse liver alcohol dehydrogenase

resolves10.1021/bi050865v

Deprotonation of the Horse Liver Alcohol Dehydrogenase−NAD+ Complex Controls Formation of the Ternary Complexes

resolves10.1021/bi990625d

Effects of Pressure on the Kinetics of Capture by Yeast Alcohol Dehydrogenase

resolves10.1021/bi00389a026

Interdependence of coenzyme-induced conformational work and binding potential in yeast alcohol and porcine heart lactate dehydrogenases: a hydrogen-deuterium exchange study

resolves10.1002/pro.5560040611

On the role of Glu‐68 in alcohol dehydrogenase

resolves10.1016/S0021-9258(18)60737-9

Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenase.

resolves10.1021/bi00631a020

pH, isotope, and substituent effects on the interconversion of aromatic substrates catalyzed by hydroxybutyrimidylated liver alcohol dehydrogenase

resolves10.1111/j.1432-1033.1977.tb11655.x

X‐Ray Investigation of the Binding of 1,10‐Phenanthroline and Imidazole to Horse‐Liver Alcohol Dehydrogenase

resolves10.1016/S0969-2126(03)00167-9

X-Ray Crystallographic and Kinetic Studies of Human Sorbitol Dehydrogenase

resolves10.1074/jbc.M010870200

On the Enzymatic Activation of NADH

resolves10.1021/bi6023594

Structural Evidence for a Ligand Coordination Switch in Liver Alcohol Dehydrogenase

resolves10.1038/nsb889

Active site electronic structure and dynamics during metalloenzyme catalysis

resolves10.1110/ps.0221603

The conserved Glu‐60 residue in Thermoanaerobacter brockii alcohol dehydrogenase is not essential for catalysis

resolves10.1016/S0021-9258(20)81798-0

The Mechanism of Enzyme-catalyzed Reduced Nicotinamide Adenine Dinucleotide-dependent Reductions

resolves10.1021/bi00654a032

Isotope effects and structure-reactivity correlations in the yeast alcohol dehydrogenase reaction. A study of the enzyme-catalyzed oxidation of aromatic alcohols

resolves10.1021/bi00551a001

Transition-state structure in the yeast alcohol dehydrogenase reaction: the magnitude of solvent and .alpha.-secondary hydrogen isotope effects

resolves10.3109/10409238109114635

Probes of Mechanism and Transition-State Structure in the Alcohol Dehydrogenase Reactio

resolves10.1021/bi00510a013

Mechanistic deductions from isotope effects in multireactant enzyme mechanisms

resolves10.1021/bi00510a014

pH Variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same

resolves10.1021/bi00510a015

pH Variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent. Kinetic mechanism of alcohol dehydrogenase

resolves10.1021/bi00318a015

Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 1. Liver alcohol dehydrogenase with benzyl alcohol and yeast aldehyde dehydrogenase with benzaldehyde

resolves10.1126/science.2646716

Hydrogen Tunneling in Enzyme Reactions

resolves10.1021/bi00072a003

Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis

resolves10.1038/20981

Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase

resolves10.1021/bi3001352

Active Site Hydrophobic Residues Impact Hydrogen Tunneling Differently in a Thermophilic Alcohol Dehydrogenase at Optimal versus Nonoptimal Temperatures

resolves10.1021/cr1001035

Update 1 of: Tunneling and Dynamics in Enzymatic Hydride Transfer

resolves10.1146/annurev-biochem-051710-133623

Hydrogen Tunneling Links Protein Dynamics to Enzyme Catalysis

resolves10.1021/bi992537z

Effect of Pressure on Deuterium Isotope Effects of Yeast Alcohol Dehydrogenase: Evidence for Mechanical Models of Catalysis

resolves10.1016/S0006-3495(00)76412-5

Effects of High Pressure on Solvent Isotope Effects of Yeast Alcohol Dehydrogenase

resolves10.2174/0929866043406157

Pressure Stability of Proteins at their Isoelectric Points

resolves10.1021/ja056525e

Effect of Pressure on a Heavy-Atom Isotope Effect of Yeast Alcohol Dehydrogenase

resolves10.1073/pnas.1000931107

Elusive transition state of alcohol dehydrogenase unveiled

resolves10.1038/355472a0

Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

The 14 references without a DOI — listed, not checked

no DOI — not checkedref5/cit5

no DOI — not checkedThe Enzymes

no DOI — not checkedref12/cit12

no DOI — not checkedref13/cit13

no DOI — not checkedref15/cit15

no DOI — not checkedref21/cit21

no DOI — not checkedThe Enzymes

no DOI — not checkedPerspectives in Evolution

no DOI — not checkedref41/cit41

no DOI — not checkedGould, R. M. (1988) Histidines in the Mechanism of Yeast Alcohol Dehydrogenase. Ph.D. Thesis,The University of Iowa,Iowa City, IA.

no DOI — not checkedThe Enzymes

no DOI — not checkedref115/cit115

no DOI — not checkedref117/cit117

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