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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 (1, 6). The crystal structure of Adh6p shows that its two subunits are structurally dissimilar with one subunit in the apo (inactive) and the other in the holo (active) conformation. Additonally, two zinc atoms are found per Adh6p subunit and only one cofactor molecule binds per dimer (9).

ADH6 is induced when galactose is the sole source of carbon in the media (2). Yeast strains overexpressing ADH6 are able to grow under toxic concentrations of veratraldehyde, and cell lysates from overexpressing strains are able to support the use of both NADPH and NADH as co-factors during the conversion of 5-hydroxymethyl furfural to 5-hydroxymethylfurfuryl alcohol (1, 10).

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, 7). 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, 7). They contain 0, 1, or 2 zinc atoms (8). 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, 7). 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 (7) 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. (7) 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 (
7) or MRF; mitochondrial respiratory function (5) family - ETR1
- QOR; quinone oxidoreductase family -
ZTA1 (5, 7), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (7)
- LTD; leukotriene B4 dehydrogenases -
YML131W
- ER; enoyl reductases (
7) or ACR; acyl-CoA reductase (5) family - no members in S. cerevisiae
", "date_edited": "2008-08-19"}, "literature_overview": {"primary_count": 24, "additional_count": 76, "review_count": 35, "go_count": 3, "phenotype_count": 4, "disease_count": 0, "interaction_count": 37, "regulation_count": 2, "ptm_count": 9, "funComplement_count": 0, "htp_count": 7, "total_count": 185}, "disease_overview": {"manual_disease_terms": [], "htp_disease_terms": [], "computational_annotation_count": 0, "date_last_reviewed": null}, "ecnumbers": [{"display_name": "1.1.1.2", "link": "/ecnumber/EC:1.1.1.2"}], "URS_ID": null, "main_strain": "S288C", "regulation_overview": {"regulator_count": 9, "target_count": 0}, "reference_mapping": {"564742": 1, "553701": 2, "398398": 3, "485127": 4, "506873": 5, "556264": 6, "506897": 7, "485140": 8, "516421": 9, "521655": 10}, "history": [{"category": "Name", "history_type": "LSP", "note": "Name: ADH6", "date_created": "2000-05-19", "references": [{"id": 564742, "display_name": "Larroy C, et al. (2002)", "citation": "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", "pubmed_id": 11742541, "link": "/reference/S000068777", "year": 2002, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1042/0264-6021:3610163"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222291/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/11742541"}]}]}, {"category": "Name", "history_type": "LSP", "note": "Name: ADHVI", "date_created": "2010-02-16", "references": [{"id": 564742, "display_name": "Larroy C, et al. (2002)", "citation": "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", "pubmed_id": 11742541, "link": "/reference/S000068777", "year": 2002, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1042/0264-6021:3610163"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222291/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/11742541"}]}]}], "complexes": []}, tabs: {"id": 1284692, "protein_tab": true, "interaction_tab": true, "summary_tab": true, "go_tab": true, "sequence_section": true, "expression_tab": true, "phenotype_tab": true, "literature_tab": true, "wiki_tab": false, "regulation_tab": true, "sequence_tab": true, "history_tab": true, "homology_tab": true, "disease_tab": false} }; ADH6 | SGD

ADH6 / YMR318C Overview


Standard Name
ADH6 1
Systematic Name
YMR318C
SGD ID
SGD:S000004937
Aliases
ADHVI
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; protein abundance increases in response to DNA replication stress 1 2 3
Name Description
Alcohol DeHydrogenase 1
Comparative Info
Sequence Details

Sequence

The S. cerevisiae Reference Genome sequence is derived from laboratory strain S288C. Download DNA or protein sequence, view genomic context and coordinates. Click "Sequence Details" to view all sequence information for this locus, including that for other strains.


Protein Details

Protein

Basic sequence-derived (length, molecular weight, isoelectric point) and experimentally-determined (median abundance, median absolute deviation) protein information. Click "Protein Details" for further information about the protein such as half-life, abundance, domains, domains shared with other proteins, protein sequence retrieval for various strains, physico-chemical properties, protein modification sites, and external identifiers for the protein.


Summary
Protein abundance increases in response to DNA replication stress
Length (a.a.)
360
Mol. Weight (Da)
39613.9
Isoelectric Point
6.73
Median Abundance (molecules/cell)
14717 +/- 6098
Half-life (hr)
7.1

Alleles

Curated mutant alleles for the specified gene, listed alphabetically. Click on the allele name to open the allele page. Click "SGD search" to view all alleles in search results.


View all ADH6 alleles in SGD search

Gene Ontology Details

Gene Ontology

GO Annotations consist of four mandatory components: a gene product, a term from one of the three Gene Ontology (GO) controlled vocabularies (Molecular Function, Biological Process, and Cellular Component), a reference, and an evidence code. SGD has manually curated and high-throughput GO Annotations, both derived from the literature, as well as computational, or predicted, annotations. Click "Gene Ontology Details" to view all GO information and evidence for this locus as well as biological processes it shares with other genes.


Summary
Alcohol dehydrogenase involved in alcohol, aldehyde, and furaldehyde metabolism

View computational annotations

Biological Process

Manually Curated

Cellular Component

Manually Curated
Phenotype Details

Phenotype

Phenotype annotations for a gene are curated single mutant phenotypes that require an observable (e.g., "cell shape"), a qualifier (e.g., "abnormal"), a mutant type (e.g., null), strain background, and a reference. In addition, annotations are classified as classical genetics or high-throughput (e.g., large scale survey, systematic mutation set). Whenever possible, allele information and additional details are provided. Click "Phenotype Details" to view all phenotype annotations and evidence for this locus as well as phenotypes it shares with other genes.


Summary
Non-essential gene in reference strain S288C; null mutant is sensitive to veratraldehyde, amitrole, cycloheximide and streptomycin
Interaction Details

Interaction

Interaction annotations are curated by BioGRID and include physical or genetic interactions observed between at least two genes. An interaction annotation is composed of the interaction type, name of the interactor, assay type (e.g., Two-Hybrid), annotation type (e.g., manual or high-throughput), and a reference, as well as other experimental details. Click "Interaction Details" to view all interaction annotations and evidence for this locus, including an interaction visualization.


114 total interactions for 96 unique genes

Physical Interactions

  • Affinity Capture-MS: 17
  • Affinity Capture-RNA: 9
  • Co-crystal Structure: 1
  • Co-localization: 1
  • Co-purification: 1
  • PCA: 3
  • Proximity Label-MS: 1

Genetic Interactions

  • Negative Genetic: 63
  • Positive Genetic: 13
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 2
  • Synthetic Rescue: 2
Regulation Details

Regulation

The number of putative Regulators (genes that regulate it) and Targets (genes it regulates) for the given locus, based on experimental evidence. This evidence includes data generated through high-throughput techniques. Click "Regulation Details" to view all regulation annotations, shared GO enrichment among regulation Targets, and a regulator/target diagram for the locus.


Regulators
9
Targets
0
Expression Details

Expression

Expression data are derived from records contained in the Gene Expression Omnibus (GEO), and are first log2 transformed and normalized. Referenced datasets may contain one or more condition(s), and as a result there may be a greater number of conditions than datasets represented in a single clickable histogram bar. The histogram division at 0.0 separates the down-regulated (green) conditions and datasets from those that are up-regulated (red). Click "Expression Details" to view all expression annotations and details for this locus, including a visualization of genes that share a similar expression pattern.


Summary Paragraph

A summary of the locus, written by SGD Biocurators following a thorough review of the literature. Links to gene names and curated GO terms are included within the Summary Paragraphs.


Last Updated: 2008-08-19

Literature Details

Literature

All manually curated literature for the specified gene, organized into topics according to their relevance to the gene (Primary Literature, Additional Literature, or Review). Click "Literature Details" to view all literature information for this locus, including shared literature between genes.


Primary
24
Additional
76
Reviews
35

Resources


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