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MetaCyc Enzyme: potassium-activated aldehyde dehydrogenase, mitochondrial

Gene: ALD4 Accession Number: G-10422 (MetaCyc)

Synonyms: ALD7, YOR374W

Species: Saccharomyces cerevisiae

Summary:
Two types of aldehyde dehydrogenase activities have been described biochemically in Saccharomyces cerevisiae: the mitochondrial type, which uses both NAD+ and NADP+ as coenzymes, is activated by K+ and repressed during growth and glucose, and the cytosolic type, which is specific for NADP+, is activated by Mg2+, and is not repressed by glucose.

Following the sequencing of the genome, these two types were mapped to five different genes - three that encode cytosolic forms, and two that encode mytochondrial forms [NavarroAvino99].

ALD4 encodes the main mytochondrial form of the enzyme. It is activated by K+, and uses both NAD and NADP. This enzyme is necessary for growth on ethanol [Tessier98].

Locations: mitochondrial lumen

Molecular Weight of Polypeptide: 56.724 kD (from nucleotide sequence)

Unification Links: Entrez-gene:854556

Relationship Links: Entrez-Nucleotide:PART-OF:Z75282

Gene-Reaction Schematic: ?

Instance reactions of [an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+] (1.2.1.4):
i1: benzaldehyde + NADP+ + H2O → benzoate + NADPH + 2 H+ (1.2.1.7)

i2: acetaldehyde + NADP+ + H2O → acetate + NADPH + 2 H+ (1.2.1.4)

i3: D-glyceraldehyde + NADP+ + H2O = D-glycerate + NADPH + 2 H+ (1.2.1.89)

i4: (S)-lactaldehyde + NADP+ + H2O → (S)-lactate + NADPH + 2 H+ (1.2.1.-)

i5: methylglyoxal + NADP+ + H2O → pyruvate + NADPH + 2 H+ (1.2.1.49)

Instance reactions of [an aldehyde + NAD+ + H2O → a carboxylate + NADH + 2 H+] (1.2.1.3):
i6: fluoroacetaldehyde + NAD+ + H2O → fluoroacetate + NADH + 2 H+ (1.2.1.69)

i7: benzaldehyde + NAD+ + H2O ↔ benzoate + NADH + 2 H+ (1.2.1.28)

i8: 4-methylbenzaldehyde + NAD+ + H2O → 4-toluenecarboxylate + NADH + 2 H+ (no EC#)

i9: all-trans-retinal + NAD+ + H2O = all-trans-retinoate + NADH + 2 H+ (1.2.1.36)

i10: acetaldehyde + NAD+ + H2O → acetate + NADH + 2 H+ (1.2.1.3)

i11: octanal + NAD+ + H2O → octanoate + NADH + 2 H+ (1.2.1.3)

i12: phytenal + NAD+ + H2O → phytenate + NADH + 2 H+ (1.2.1.3)

i13: (2E,6E)-farnesal + NAD+ + H2O → (2-trans-6-trans)-farnesoate + NADH + 2 H+ (1.2.1.3)

i14: salicylaldehyde + NAD+ + H2O → salicylate + NADH + 2 H+ (1.2.1.65)

i15: (R)-lactaldehyde + NAD+ + H2O → (R)-lactate + NADH + 2 H+ (no EC#)

i16: (S)-lactaldehyde + NAD+ + H2O → (S)-lactate + NADH + 2 H+ (1.2.1.22)

i17: methylglyoxal + NAD+ + H2O → pyruvate + NADH + 2 H+ (1.2.1.23)

GO Terms:

Cellular Component: GO:0005759 - mitochondrial matrix [Tessier98]

Credits:
Created 08-Jan-2008 by Caspi R , SRI International


Enzymatic reaction of: aldehyde dehydrogenase

EC Number: 1.2.1.4

an aldehyde + NADP+ + H2O <=> a carboxylate + NADPH + 2 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: pyruvate fermentation to acetate VIII , superpathway NAD/NADP - NADH/NADPH interconversion (yeast) , NAD/NADP-NADH/NADPH mitochondrial interconversion (yeast)


Enzymatic reaction of: aldehyde dehydrogenase

EC Number: 1.2.1.3

an aldehyde + NAD+ + H2O <=> a carboxylate + NADH + 2 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: methylglyoxal degradation V , superpathway NAD/NADP - NADH/NADPH interconversion (yeast) , NAD/NADP-NADH/NADPH mitochondrial interconversion (yeast)

Activators (Allosteric): K+


References

NavarroAvino99: Navarro-Avino JP, Prasad R, Miralles VJ, Benito RM, Serrano R (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. PMID: 10407263

Tessier98: Tessier WD, Meaden PG, Dickinson FM, Midgley M (1998). "Identification and disruption of the gene encoding the K(+)-activated acetaldehyde dehydrogenase of Saccharomyces cerevisiae." FEMS Microbiol Lett 164(1);29-34. PMID: 9675847


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, biocyc14.