ALD2/YMR170C Summary Help

Standard Name ALD2
Systematic Name YMR170C
Feature Type ORF, Verified
Description Cytoplasmic aldehyde dehydrogenase; involved in ethanol oxidation and beta-alanine biosynthesis; uses NAD+ as the preferred coenzyme; expression is stress induced and glucose repressed; very similar to Ald3p (1, 2 and see Summary Paragraph)
Name Description ALdehyde Dehydrogenase
Chromosomal Location
ChrXIII:603082 to 601562 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All ALD2 GO evidence and references
  View Computational GO annotations for ALD2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 7 genes
Resources
Pathways
Classical genetics
null
Large-scale survey
null
Resources
17 total interaction(s) for 15 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 4
  • Co-purification: 1
  • Two-hybrid: 1

Genetic Interactions
  • Negative Genetic: 8
  • Phenotypic Suppression: 1
  • Positive Genetic: 1
  • Synthetic Growth Defect: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 506
Molecular Weight (Da) 55,187
Isoelectric Point (pI) 5.32
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXIII:603082 to 601562 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1521 603082..601562 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004780
SUMMARY PARAGRAPH for ALD2

Aldehyde dehydrogenases play a critical role in the conversion of acetaldehyde to acetyl-CoA during growth on non-fermentable carbon sources and in the breakdown of toxic aldehydes accumulated under stress conditions (3). Acetaldehyde arises during the metabolism of pyruvate to acetate by the cytoplasmic pyruvate dehydrogenase bypass (PDH) pathway, which involves the enzymatic activities pyruvate decarboxylase (PDC6, PDC5, PDC1), acetaldehyde dehydrogenase (ALD6), and acetyl-CoA synthetase (ACS1, ACS2) (4). In an alternate mitochondrial pyruvate dehydrogenase bypass pathway, pyruvate is first decarboxylated to acetaldehyde in the cytosol by pyruvate decarboxylase and is then converted to acetate by the mitochondrial acetaldehyde dehydrogenases (ALD4 and ALD5) (5).

In the yeast genome, there are five genes known to encode aldehyde dehydrogenases, as well as an additional gene with sequence similarity. Ald2p and Ald3p are cytosolic enzymes which use only NAD+ as cofactor. Both genes are induced in response to ethanol or stress and repressed by glucose. Ald4p and Ald5p are mitochondrial, use NAD and NADP as cofactors, and are K+ dependent. Ald4p, the major isoform, is glucose repressed and ald4 mutants do not grow on ethanol, while Ald5p, the minor isoform, is constitutively expressed (6, 7). ALD6 encodes the Mg2+ activated cytosolic enzyme, which uses NADP+ as cofactor and is constitutively expressed. HFD1 has been predicted to encode a fatty aldehyde dehydrogenase (1, 8, 5, 9).

Aldehyde dehydrogenases are conserved across many species and are key enzymes in metabolic pathways, some of which function to detoxify harmful chemical intermediates. In humans, mutations in aldehyde dehydrogenase genes (ALDH1, ALDH2, ALDH4 and ALDH10) are associated with alcoholism and carcinogenesis. In plants, these enzymes play important roles in fertility and in fruit ripening (1 and references therein).

Last updated: 2009-08-14 Contact SGD

References cited on this page View Complete Literature Guide for ALD2
1) Navarro-Avino JP, et al.  (1999) A proposal for nomenclature of aldehyde dehydrogenases in Saccharomyces cerevisiae and characterization of the stress-inducible ALD2 and ALD3 genes. Yeast 15(10A):829-42
2) White WH, et al.  (2003) Specialization of function among aldehyde dehydrogenases: the ALD2 and ALD3 genes are required for beta-alanine biosynthesis in Saccharomyces cerevisiae. Genetics 163(1):69-77
3) Aranda A and del Olmo Ml M  (2003) Response to acetaldehyde stress in the yeast Saccharomyces cerevisiae involves a strain-dependent regulation of several ALD genes and is mediated by the general stress response pathway. Yeast 20(8):747-59
4) Boubekeur S, et al.  (1999) A mitochondrial pyruvate dehydrogenase bypass in the yeast Saccharomyces cerevisiae. J Biol Chem 274(30):21044-8
5) Boubekeur S, et al.  (2001) Participation of acetaldehyde dehydrogenases in ethanol and pyruvate metabolism of the yeast Saccharomyces cerevisiae. Eur J Biochem 268(19):5057-65
6) Wang X, et al.  (1998) Molecular cloning, characterization, and potential roles of cytosolic and mitochondrial aldehyde dehydrogenases in ethanol metabolism in Saccharomyces cerevisiae. J Bacteriol 180(4):822-30
7) Tessier WD, et al.  (1998) Identification and disruption of the gene encoding the K(+)-activated acetaldehyde dehydrogenase of Saccharomyces cerevisiae. FEMS Microbiol Lett 164(1):29-34
8) Kurita O and Nishida Y  (1999) Involvement of mitochondrial aldehyde dehydrogenase ALD5 in maintenance of the mitochondrial electron transport chain in Saccharomyces cerevisiae. FEMS Microbiol Lett 181(2):281-7
9) Zahedi RP, et al.  (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50