MetaCyc Compound: indole

Superclasses: an aromatic compoundan indole

Chemical Formula: C8H7N

Molecular Weight: 117.15 Daltons

Monoisotopic Molecular Weight: 117.0578492299 Daltons

indole compound structure

SMILES: C2(C=CC1(=C(C=CN1)C=2))

InChI: InChI=1S/C8H7N/c1-2-4-8-7(3-1)5-6-9-8/h1-6,9H


Unification Links: CAS:120-72-9, ChEBI:16881, ChemSpider:776, DrugBank:DB04532, HMDB:HMDB00738, IAF1260:35045, KEGG:C00463, PubChem:798

Standard Gibbs Free Energy of Formation (ΔfG in kcal/mol): 125.38785Inferred by computational analysis [Latendresse13]

Reactions known to consume the compound:

DIBOA-glucoside biosynthesis :
indole + NAD(P)H + oxygen + H+ → indolin-2-one + NAD(P)+ + H2O

indican biosynthesis , indigo biosynthesis :
indole + NADH + oxygen + H+cis-indole-2,3-dihydrodiol + NAD+

indole degradation to anthranil and anthranilate :
indole + oxygen → 2-formylaminobenzaldehyde

L-tryptophan biosynthesis :
L-serine + indole → L-tryptophan + H2O

Not in pathways:
indole + NADH + oxygen + H+ → indoxyl + NAD+ + H2O

Reactions known to both consume and produce the compound:

DIBOA-glucoside biosynthesis , L-tryptophan biosynthesis :
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate ↔ indole + D-glyceraldehyde 3-phosphate

L-tryptophan degradation II (via pyruvate) :
L-tryptophan ↔ indole + 2-aminoprop-2-enoate + H+

Not in pathways:
indole-3-carboxylate + H+indole + CO2

In Reactions of unknown directionality:

Not in pathways:
L-tryptophan + H2O = indole + pyruvate + ammonium
indole + hydrogen peroxide = indolin-3-one + H2O
indole + hydrogen peroxide = indolin-2-one + H2O
indole + acetate + an oxidized unknown electron acceptor = indole-3-acetate + an reduced unknown electron acceptor

In Transport reactions:
indole[periplasm] + H+[periplasm]indole[cytosol] + H+[cytosol]

Enzymes activated by indole, sorted by the type of activation, are:

Activator (Allosteric) of: tryptophanase [Hoch66]

Enzymes inhibited by indole, sorted by the type of inhibition, are:

Inhibitor (Mechanism unknown) of: tryptophan dioxygenase [Matsumura84]

This compound has been characterized as an alternative substrate of the following enzymes: styrene monooxygenase


Hoch66: Hoch JA, Simpson FJ, DeMoss RD (1966). "Purification and some properties of tryptophanase from Bacillus alvei." Biochemistry 5(7);2229-37. PMID: 4959960

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

Matsumura84: Matsumura M, Osada K, Aiba S (1984). "L-tryptophan 2,3-dioxygenase of a moderate thermophile, Bacillus brevis. Purification, properties and a substrate-mediated stabilization of the quaternary structure." Biochim Biophys Acta 786(1-2);9-17. PMID: 6712960

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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