MetaCyc Enzyme: indole-3-carboxylate decarboxylase

Species: Arthrobacter nicotianae FI1612

The bacterium Arthrobacter nicotianae FI1612 was isolated in an enrichment culture grown with indole-3-carboxylate as the sole carbon source. This strain demonstrated a high level of indole-3-carboxylate decarboxylase activity. Enzyme activity was strongly induced by adding indole-3-carboxylate to the medium.

The enzyme was purified, and found to be sensitive to oxygen. It did not require any cofactors, and could also catalyze the reverse reaction [Yoshida02a].

Gene-Reaction Schematic

Gene-Reaction Schematic

Created 13-Apr-2011 by Caspi R, SRI International

Enzymatic reaction of: indole-3-carboxylate decarboxylase

Inferred from experiment

EC Number:

indole-3-carboxylate + H+ ⇄ indole + CO2

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.

This reaction is reversible. [Yoshida02a]

Alternative Substrates for indole: 2-methylindole [Yoshida02a] Inhibitors (Other): N-ethylmaleimide [Yoshida02a], o-phenanthroline [Yoshida02a], phenylhydrazine [Yoshida02a]Kinetic Parameters:
Substrate Km (μM) Citations
indole 720.0 [Yoshida02a]
indole-3-carboxylate 630.0 [Yoshida02a]

T(opt): 50 °C [Yoshida02a]

pH(opt): 7 [Yoshida02a]


Yoshida02a: Yoshida T, Fujita K, Nagasawa T (2002). "Novel reversible indole-3-carboxylate decarboxylase catalyzing nonoxidative decarboxylation." Biosci Biotechnol Biochem 66(11);2388-94. PMID: 12506977

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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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