ADH7/YCR105W Summary Help

Standard Name ADH7
Systematic Name YCR105W
Feature Type ORF, Verified
Description NADPH-dependent medium chain alcohol dehydrogenase; has broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance (1 and see Summary Paragraph)
Name Description Alcohol DeHydrogenase
Chromosomal Location
ChrIII:309070 to 310155 | ORF Map | GBrowse
Gene Ontology Annotations All ADH7 GO evidence and references
  View Computational GO annotations for ADH7
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Large-scale survey
14 total interaction(s) for 14 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Affinity Capture-RNA: 2
  • Biochemical Activity: 3
  • Two-hybrid: 1

Genetic Interactions
  • Negative Genetic: 3
  • Synthetic Lethality: 1
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 361
Molecular Weight (Da) 39,348
Isoelectric Point (pI) 7.3
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIII:309070 to 310155 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1086 309070..310155 2011-02-03 1997-01-28
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 SGDIDS000000702

ADH6 and ADH7 are non-essential genes that encode the only S. cerevisiae members of the cinnamyl alcohol dehydrogase (CAD) family (2, 1). CADs are a subgroup of medium-chain zinc-containing alcohol dehydrogenases that were originally identified in plants where they are involved in the biosynthesis of lignin (3 and references therein). However, since lignin biosynthesis does not occur in yeast, in S. cerevisiae these enzymes are instead thought to participate in lignin degradation, the synthesis of fusel alcohols, and NADPH homeostasis (1).

Although their kinetic properties differ slightly, both Adh6p and Adh7p use the cofactor NADPH and have a broad substrate specificity. Adh6p and Adh7p share 64% sequence identity and each forms homodimers made up of 40 kDa subunits (2, 1).

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

Medium-chain dehydrogenase/reductases (MDRs), sometimes referred to as long-chain dehydrogenases (4), constitute an ancient and widespread enzyme superfamily with members found in Bacteria, Archaea, and Eukaryota (5, 6). 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 (5). 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 (5).

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) (5, 6). They contain 0, 1, or 2 zinc atoms (7). 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 (5, 6). 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 (5) or twenty-one (6) 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. (6) but not by Nordling et al. (5).

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 (6) or MRF; mitochondrial respiratory function (5) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (5, 6), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (6)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (6) or ACR; acyl-CoA reductase (5) family - no members in S. cerevisiae

Last updated: 2006-07-31 Contact SGD

References cited on this page View Complete Literature Guide for ADH7
1) Larroy C, et al.  (2002) Characterization of a Saccharomyces cerevisiae NADP(H)-dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family. Eur J Biochem 269(22):5738-45
2) Larroy C, et al.  (2002) Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction. Biochem J 361(Pt 1):163-72
3) Larroy C, et al.  (2003) Properties and functional significance of Saccharomyces cerevisiae ADHVI. Chem Biol Interact 143-144:229-38
4) 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
5) 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
6) Riveros-Rosas H, et al.  (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34
7) Persson B, et al.  (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463():373-7