Metabolic Modeling Tutorial
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BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 1.2.1.3

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.2.1.3

Enzymes and Genes:
4-trimethylaminobutyraldehyde dehydrogenase Inferred from experiment : ALDH9A1 ( Homo sapiens )
fatty aldehyde dehydrogenase : ALDH3A2 ( Homo sapiens )
aldehyde dehydrogenase Inferred from experiment : ALD3 ( Saccharomyces cerevisiae )
aldehyde dehydrogenase Inferred from experiment : ALD2 ( Saccharomyces cerevisiae )
potassium-activated aldehyde dehydrogenase, mitochondrial Inferred from experiment : ALD4 ( Saccharomyces cerevisiae )
aldehyde dehydrogenase, mitochondrial Inferred from experiment : ALD5 ( Saccharomyces cerevisiae )
mitochondrial aldehyde dehydrogenase Inferred from experiment : ALDH2 ( Homo sapiens )
aldehyde dehydrogenase Inferred from experiment : alkH ( Pseudomonas oleovorans )

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

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

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

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

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

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

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

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

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

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

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

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

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

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

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

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): -2.834198 Inferred by computational analysis [Latendresse13]

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

Citations: [Racker49]

Gene-Reaction Schematic: ?

Unification Links: 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 SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC13B.