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Indoleacetate decarboxylase (IAD) is a glycyl radical enzyme (therefore member of the GRE superfamily ) that catalyses the decarboxylation of indoleacetate to form skatole, which is a malodorous organic compound that gives animal faeces their characteristic smell. This decarboxylation is the last step of the tryptophan fermentation in some types of anaerobic bacteria.

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  • Indoleacetate decarboxylase (IAD) is a glycyl radical enzyme (therefore member of the GRE superfamily ) that catalyses the decarboxylation of indoleacetate to form skatole, which is a malodorous organic compound that gives animal faeces their characteristic smell. This decarboxylation is the last step of the tryptophan fermentation in some types of anaerobic bacteria. Tryptophan (Trp), Tyrosine (Tyr) and Phenylalanine (Phe) are aromatic aminoacids that can be degraded by certain types of fermenting bacteria. These bacteria create indoleacetate, p-hydroxyphenylacetate and phenylacetate, respectively. In addition, some bacteria carry out a further step, decarboxylating these compounds and creating skatole, cresol and toluene, respectively, which are volatile aromatic compounds. Out of these three compounds, skatole is the most noticeable as its distinct faecal malodour is detectable at the lowest concentration of 0.00056 parts per million (0.0030 mg/m3). (en)
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  • 4.1.1.115
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  • Indoleacetate decarboxylase (en)
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  • Indoleacetate decarboxylase (IAD) is a glycyl radical enzyme (therefore member of the GRE superfamily ) that catalyses the decarboxylation of indoleacetate to form skatole, which is a malodorous organic compound that gives animal faeces their characteristic smell. This decarboxylation is the last step of the tryptophan fermentation in some types of anaerobic bacteria. (en)
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  • Indoleacetate decarboxylase (en)
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