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ALD4  -  aldehyde dehydrogenase (NADP(+)) ALD4

Saccharomyces cerevisiae S288c

Synonyms: ALD7, ALDH2, K(+)-ACDH, K(+)-activated acetaldehyde dehydrogenase, O6730, ...
 
 
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Disease relevance of ALD4

  • We report a method to assess ALDH2 activity in intact hepatoma cells that does not require mitochondrial isolation [1].
 

High impact information on ALD4

  • However, the codisruption of PDA1 and ALD7 genes prevented the growth on lactate, indicating that each of these pathways contributes to the oxidative metabolism of pyruvate [2].
  • Mutants disrupted for the mitochondrial acetaldehyde dehydrogenase gene (ALD7) did not oxidize pyruvate unless malate was added [2].
  • Preferential ionization was tested on a yeast aldehyde dehydrogenase (ALD7), and it was shown that the ionization of some peptides was clearly suppressed by the presence of others [3].
  • The exchange of the N-terminal 21 residues from the mature portion altered import, folding, and assembly of precursor ALDH1 and precursor ALDH2 [4].
  • The ALDH5 gene was located on chromosome V. The commercial ALDH (designated ALDH2) was partially sequenced and appears to be a mitochondrial enzyme encoded by a gene located on chromosome XV [5].
 

Biological context of ALD4

 

Anatomical context of ALD4

 

Associations of ALD4 with chemical compounds

  • Engineering of the pyruvate dehydrogenase bypass in Saccharomyces cerevisiae: role of the cytosolic Mg(2+) and mitochondrial K(+) acetaldehyde dehydrogenases Ald6p and Ald4p in acetate formation during alcoholic fermentation [8].
  • Growth on glucose was not affected in the mutants lacking ALD7 (in contrast to the behaviour of ald6 mutants), whereas growth on ethanol was severely impaired [6].
  • The co-disruption of ALD4 and PDA1 (encoding subunit E1alpha of pyruvate dehydrogenase) prevented the growth on pyruvate for both strains but prevented growth on lactate only in the double mutant derived from the YPH499 strain, indicating that the mutation effects are strain-dependent [9].
  • Mature ALDH1 proved to be more stable against urea denaturation than ALDH2 [4].
 

Analytical, diagnostic and therapeutic context of ALD4

  • Activity staining of isoelectric focusing gels showed that cytosolic ALDH1 contributed 30 to 70% of the overall activity, depending on the cofactor used, while mitochondrial ALDH2 contributed the rest [5].

References

  1. Use of an "acetaldehyde clamp" in the determination of low-KM aldehyde dehydrogenase activity in H4-II-E-C3 rat hepatoma cells. Moncada, C., Fuentes, N., Lladser, A., Encina, G., Sapag, A., Karahanian, E., Israel, Y. Alcohol (2003) [Pubmed]
  2. A mitochondrial pyruvate dehydrogenase bypass in the yeast Saccharomyces cerevisiae. Boubekeur, S., Bunoust, O., Camougrand, N., Castroviejo, M., Rigoulet, M., Guérin, B. J. Biol. Chem. (1999) [Pubmed]
  3. Identification of two-dimensional gel electrophoresis resolved yeast proteins by matrix-assisted laser desorption ionization mass spectrometry. Larsson, T., Norbeck, J., Karlsson, H., Karlsson, K.A., Blomberg, A. Electrophoresis (1997) [Pubmed]
  4. The N-terminal portion of mature aldehyde dehydrogenase affects protein folding and assembly. Zhou, J., Weiner, H. Protein Sci. (2001) [Pubmed]
  5. Molecular cloning, characterization, and potential roles of cytosolic and mitochondrial aldehyde dehydrogenases in ethanol metabolism in Saccharomyces cerevisiae. Wang, X., Mann, C.J., Bai, Y., Ni, L., Weiner, H. J. Bacteriol. (1998) [Pubmed]
  6. Identification and disruption of the gene encoding the K(+)-activated acetaldehyde dehydrogenase of Saccharomyces cerevisiae. Tessier, W.D., Meaden, P.G., Dickinson, F.M., Midgley, M. FEMS Microbiol. Lett. (1998) [Pubmed]
  7. Functional analysis of the ALD gene family of Saccharomyces cerevisiae during anaerobic growth on glucose: the NADP+-dependent Ald6p and Ald5p isoforms play a major role in acetate formation. Saint-Prix, F., Bönquist, L., Dequin, S. Microbiology (Reading, Engl.) (2004) [Pubmed]
  8. Engineering of the pyruvate dehydrogenase bypass in Saccharomyces cerevisiae: role of the cytosolic Mg(2+) and mitochondrial K(+) acetaldehyde dehydrogenases Ald6p and Ald4p in acetate formation during alcoholic fermentation. Remize, F., Andrieu, E., Dequin, S. Appl. Environ. Microbiol. (2000) [Pubmed]
  9. Participation of acetaldehyde dehydrogenases in ethanol and pyruvate metabolism of the yeast Saccharomyces cerevisiae. Boubekeur, S., Camougrand, N., Bunoust, O., Rigoulet, M., Guérin, B. Eur. J. Biochem. (2001) [Pubmed]
 
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