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MetaCyc Reaction: 1.2.1.3

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 1.2.1.3

Enzymes and Genes:

Corynebacterium glutamicum ATCC 13032: acetaldehyde dehydrogenaseInferred from experiment: ald
Homo sapiens: mitochondrial aldehyde dehydrogenaseInferred from experiment: ALDH2
4-trimethylaminobutyraldehyde dehydrogenaseInferred from experiment: ALDH9A1
fatty aldehyde dehydrogenase: ALDH3A2
Pseudomonas oleovorans: aldehyde dehydrogenaseInferred from experiment: alkH
Saccharomyces cerevisiae: aldehyde dehydrogenase, mitochondrialInferred from experiment: ALD5
potassium-activated aldehyde dehydrogenase, mitochondrialInferred from experiment: ALD4
aldehyde dehydrogenaseInferred from experiment: ALD2
aldehyde dehydrogenaseInferred from experiment: ALD3

In Pathway: NAD/NADP-NADH/NADPH mitochondrial interconversion (yeast)

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

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

fluoroacetaldehyde + NAD+ + H2O → fluoroacetate + NADH + 2 H+ (1.2.1.69)

(2E,6E)-farnesal + NAD+ + H2O → (2E,6E)-farnesoate + NADH + 2 H+ (1.2.1.94)

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

dodecanal + NAD+ + H2O = laurate + NADH + 2 H+ (1.2.1.3)

decanal + NAD+ + H2O = decanoate + NADH + 2 H+ (1.2.1.3)

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

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

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

formaldehyde + NAD+ + H2O → formate + NADH + 2 H+ (1.2.1.46)

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

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

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

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

a fatty aldehyde + NAD+ + H2O → a fatty acid + NADH + 2 H+ (1.2.1.3)

a 2-methyl branched 2,3,4-saturated fatty aldehyde + NAD+ + H2O → a 2-methyl branched 2,3,4-saturated fatty acid + NADH + 2 H+ (1.2.1.3)

a long-chain aldehyde + NAD+ + H2O = a long-chain fatty acid + NADH + 2 H+ (1.2.1.48)

an odd numbered straight chain 2,3,4-saturated fatty aldehyde + NAD+ + H2O → an odd numbered straight chain 2,3,4-saturated fatty acid + NADH + 2 H+ (1.2.1.3)

Enzyme Commission Primary Name: aldehyde dehydrogenase (NAD+)

Enzyme Commission Synonyms: CoA-independent aldehyde dehydrogenase, m-methylbenzaldehyde dehydrogenase, NAD-aldehyde dehydrogenase, NAD-dependent 4-hydroxynonenal dehydrogenase, NAD-dependent aldehyde dehydrogenase, NAD-linked aldehyde dehydrogenase, propionaldehyde dehydrogenase, aldehyde dehydrogenase (NAD)

Standard Gibbs Free Energy (ΔrG in kcal/mol): -2.834198Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.

Citations: [Racker49]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R00538, KEGG:R00632, Rhea:16185

Relationship Links: BRENDA:EC:1.2.1.3, ENZYME:EC:1.2.1.3, IUBMB-ExplorEnz:EC:1.2.1.3, UniProt:RELATED-TO:O68123, UniProt:RELATED-TO:O85973, UniProt:RELATED-TO:P00352, UniProt:RELATED-TO:P05091, UniProt:RELATED-TO:P08157, UniProt:RELATED-TO:P11884, UniProt:RELATED-TO:P12693, UniProt:RELATED-TO:P12762, UniProt:RELATED-TO:P13601, UniProt:RELATED-TO:P15437, UniProt:RELATED-TO:P20000, UniProt:RELATED-TO:P23240, UniProt:RELATED-TO:P23883, UniProt:RELATED-TO:P24549, UniProt:RELATED-TO:P27463, UniProt:RELATED-TO:P30839, UniProt:RELATED-TO:P32872, UniProt:RELATED-TO:P33008, UniProt:RELATED-TO:P33744, UniProt:RELATED-TO:P37685, UniProt:RELATED-TO:P39616, UniProt:RELATED-TO:P40047, UniProt:RELATED-TO:P40108, UniProt:RELATED-TO:P42041, UniProt:RELATED-TO:P43353, UniProt:RELATED-TO:P45959, UniProt:RELATED-TO:P46367, UniProt:RELATED-TO:P46368, UniProt:RELATED-TO:P47738, UniProt:RELATED-TO:P47895, UniProt:RELATED-TO:P49189, UniProt:RELATED-TO:P51647, UniProt:RELATED-TO:P51977, UniProt:RELATED-TO:P54114, UniProt:RELATED-TO:P54115, UniProt:RELATED-TO:P63937, UniProt:RELATED-TO:P93344, UniProt:RELATED-TO:P96824, UniProt:RELATED-TO:Q7M0F9, UniProt:RELATED-TO:Q9SU63, UniProt:RELATED-TO:Q25417, UniProt:RELATED-TO:Q27640, UniProt:RELATED-TO:Q55811, UniProt:RELATED-TO:Q62148


References

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Racker49: Racker, E. (1949). "Aldehyde dehydrogenase, a diphosphopyridine nucleotide-linked enzyme." J Biol Chem 177(2);883-92. PMID: 18110463


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 Pathway Tools version 19.5 (software by SRI International) on Fri Feb 12, 2016, biocyc13.