ADH1/YOL086C Summary Help

Standard Name ADH1 1
Systematic Name YOL086C
Alias ADC1
Feature Type ORF, Verified
Description Alcohol dehydrogenase; fermentative isozyme active as homo- or heterotetramers; required for the reduction of acetaldehyde to ethanol, the last step in the glycolytic pathway; ADH1 has a paralog, ADH5, that arose from the whole genome duplication (2, 3, 4, 5 and see Summary Paragraph)
Name Description Alcohol DeHydrogenase
Chromosomal Location
ChrXV:160594 to 159548 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -86 cM
Gene Ontology Annotations All ADH1 GO evidence and references
  View Computational GO annotations for ADH1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 23 genes
Classical genetics
gain of function
Large-scale survey
164 total interaction(s) for 143 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 83
  • Affinity Capture-RNA: 5
  • Affinity Capture-Western: 2
  • Biochemical Activity: 1
  • Co-fractionation: 1
  • Co-localization: 2
  • Co-purification: 2
  • PCA: 2
  • Protein-RNA: 6
  • Two-hybrid: 2

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 36
  • Phenotypic Enhancement: 9
  • Phenotypic Suppression: 4
  • Positive Genetic: 4
  • Synthetic Growth Defect: 3
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 348
Molecular Weight (Da) 36,849
Isoelectric Point (pI) 6.66
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXV:160594 to 159548 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -86 cM
Last Update Coordinates: 2006-01-05 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1047 160594..159548 2006-01-05 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005446

In S. cerevisiae, there are five genes that encode alcohol dehydrogenases involved in ethanol metabolism, ADH1 to ADH5. Four of these enzymes, Adh1p, Adh3p, Adh4p, and Adh5p, reduce acetaldehyde to ethanol during glucose fermentation, while Adh2p catalyzes the reverse reaction of oxidizing ethanol to acetaldehyde (3, 6, 2, 7, 8).

The five ethanol dehydrogenases (Adh1p, Adh2p, Adh3p, Adh4p, and Adh5p) as well as the bifunctional enzyme Sfa1p are also involved in the production of fusel alcohols during fermentation (4). Fusel alcohols are end products of amino acid catabolism (of valine, leucine, isoleucine, methionine, phenylalanine, tryptophan, and tyrosine) via the Ehrlich pathway and contribute to the flavor and aroma of yeast-fermented foods and beverages (9). They may also have physiological roles. For example, exposing cells to isoamyl alcohol, derived from catabolism of leucine, stimulates filamentous growth (10, 11). Similarly, other fusel alcohols also stimulate filamentous growth in S. cerevisiae and biofilm formation in the pathogens Candida albicans and Candida dubliniensis (12, 13, reviewed in 9).

The cytosolic ADH1 gene product is the major enzyme responsible for converting acetaldehyde to ethanol (reviewed in 14). Adh1p functions as a tetramer of four identical subunits with each subunit containing two zinc ions; one zinc atom is essential for catalysis and the other is important for the structure of the protein (15, 16 and references contained therein). Although originally thought to be expressed constitutively, ADH1 transcription is repressed when cells are grown on a non-fermentable carbon source such as ethanol or glycerol (17). S. cerevisiae cells lacking Adh1p activity grow poorly on glucose under anaerobic conditions and treatment of these cells with a respiratory inhibitor blocks growth completely (18 and references contained therein). Overexpression of ADH1 is able to enhance the formaldehyde resistance of yeast cells (19).

About the medium-chain dehydrogenase/reductase (MDR) family

Medium-chain dehydrogenase/reductases (MDRs), sometimes referred to as long-chain dehydrogenases (20), constitute an ancient and widespread enzyme superfamily with members found in Bacteria, Archaea, and Eukaryota (21, 22). Many MDR members are basic metabolic enzymes acting on alcohols or aldehydes, and thus these enzymes may have roles in detoxifying alcohols and related compounds, protecting against environmental stresses such as osmotic shock, reduced or elevated temperatures, or oxidative stress (21). The family also includes the mammalian zeta-crystallin lens protein, which may protect the lens against oxidative damage and enzymes which produce lignocellulose in plants (21).

MDR enzymes typically have subunits of about 350 aa residues and are two-domain proteins, with a catalytic domain and a second domain for binding to the nicotinamide cofactor, either NAD(H) or NADP(H) (21, 22). They contain 0, 1, or 2 zinc atoms (23). When zinc is present, it is involved in catalysis at the active site.

Based on phylogenetic and sequence analysis, the members of the MDR superfamily can be further divided into more closely related subgroups (21, 22). In families which are widespread from prokaryotes to eukaryotes, some members appear conserved across all species, while others appear to be due to lineage specific duplications. Some subgroups are only found in certain taxa. S. cerevisiae contains fifteen (21) or twenty-one (22) members of the MDR superfamily, listed below. The difference in number is due to six sequences that were included as members of the quinone oxidoreductase family by Riveros-Rosas et al. (22) but not by Nordling et al. (21).

Zinc-containing enzyme groups:
- PDH; "polyol" dehydrogenase family - BDH1, BDH2, SOR1, SOR2, XYL2
- ADH; class III alcohol dehydrogenase family - SFA1
- Y-ADH; "yeast" alcohol dehydrogenase family - ADH1, ADH2, ADH3, ADH5
- CADH; cinnamyl alcohol dehydrogenase family - ADH6, ADH7

Non-zinc-containing enzyme groups:
- NRBP; nuclear receptor binding protein (22) or MRF; mitochondrial respiratory function (21) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (21, 22), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (22)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (22) or ACR; acyl-CoA reductase (21) family - no members in S. cerevisiae

Last updated: 2005-11-21 Contact SGD

References cited on this page View Complete Literature Guide for ADH1
1) Ciriacy, M.  (1985) Personal Communication, Mortimer Map Edition 9
2) Young ET and Pilgrim D  (1985) Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae. Mol Cell Biol 5(11):3024-34
3) Bennetzen JL and Hall BD  (1982) The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase. J Biol Chem 257(6):3018-25
4) Dickinson JR, et al.  (2003) The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae. J Biol Chem 278(10):8028-34
5) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
6) Russell DW, et al.  (1983) Nucleotide sequence of the yeast alcohol dehydrogenase II gene. J Biol Chem 258(4):2674-82
7) Drewke C and Ciriacy M  (1988) Overexpression, purification and properties of alcohol dehydrogenase IV from Saccharomyces cerevisiae. Biochim Biophys Acta 950(1):54-60
8) Smith MG, et al.  (2004) Microbial synergy via an ethanol-triggered pathway. Mol Cell Biol 24(9):3874-84
9) Hazelwood LA, et al.  (2008) The Ehrlich pathway for fusel alcohol production: a century of research on Saccharomyces cerevisiae metabolism. Appl Environ Microbiol 74(8):2259-66
10) Kern K, et al.  (2004) Isoamyl alcohol-induced morphological change in Saccharomyces cerevisiae involves increases in mitochondria and cell wall chitin content. FEMS Yeast Res 5(1):43-9
11) Hauser M, et al.  (2007) A transcriptome analysis of isoamyl alcohol-induced filamentation in yeast reveals a novel role for Gre2p as isovaleraldehyde reductase. FEMS Yeast Res 7(1):84-92
12) Dickinson JR  (1996) 'Fusel' alcohols induce hyphal-like extensions and pseudohyphal formation in yeasts. Microbiology 142 ( Pt 6)():1391-7
13) Lorenz MC, et al.  (2000) Characterization of alcohol-induced filamentous growth in Saccharomyces cerevisiae. Mol Biol Cell 11(1):183-99
14) Leskovac V, et al.  (2002) The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae. FEMS Yeast Res 2(4):481-94
15) Klinman JP and Welsh K  (1976) The zinc content of yeast alcohol dehydrogenase. Biochem Biophys Res Commun 70(3):878-84
16) Magonet E, et al.  (1992) Importance of the structural zinc atom for the stability of yeast alcohol dehydrogenase. Biochem J 287 ( Pt 2)():361-5
17) Denis CL, et al.  (1983) mRNA levels for the fermentative alcohol dehydrogenase of Saccharomyces cerevisiae decrease upon growth on a nonfermentable carbon source. J Biol Chem 258(2):1165-71
18) Paquin CE and Williamson VM  (1986) Ty insertions at two loci account for most of the spontaneous antimycin A resistance mutations during growth at 15 degrees C of Saccharomyces cerevisiae strains lacking ADH1. Mol Cell Biol 6(1):70-9
19) Grey M, et al.  (1996) Overexpression of ADH1 confers hyper-resistance to formaldehyde in Saccharomyces cerevisiae. Curr Genet 29(5):437-40
20) Jornvall H, et al.  (1981) Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Proc Natl Acad Sci U S A 78(7):4226-30
21) Nordling E, et al.  (2002) Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling. Eur J Biochem 269(17):4267-76
22) Riveros-Rosas H, et al.  (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34
23) Persson B, et al.  (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463():373-7