Ligases;
Forming carbon-carbon bonds;
Ligases that form carbon-carbon bonds (only sub-subclass identified to date)
BRITE hierarchy

(indol-3-yl)pyruvate:(indol-3-yl)pyruvate ligase (didemethylasterriquinone D-forming)

2 ATP + 2 (indol-3-yl)pyruvate = 2 AMP + 2 diphosphate + didemethylasterriquinone D (overall reaction) [RN:R13526];
(1a) ATP + (indol-3-yl)pyruvate + [didemethylasterriquinone D synthase] = AMP + diphosphate + (indol-3-yl)pyruvoyl-[didemethylasterriquinone D synthase] [RN:R13527];
(1b) ATP + (indol-3-yl)pyruvate + (indol-3-yl)pyruvoyl-[didemethylasterriquinone D synthase] = AMP + diphosphate + didemethylasterriquinone D + [didemethylasterriquinone D synthase] [RN:R13528]

R13526 R13527 R13528
Reaction

ATP [CPD:C00002];
(indol-3-yl)pyruvate [CPD:C00331];
[didemethylasterriquinone D synthase];
(indol-3-yl)pyruvoyl-[didemethylasterriquinone D synthase]

Requires Mg2+. The enzyme, characterized from the fungus Aspergillus nidulans, is a non-ribosomal peptide synthase-like enzyme comprising three domains: an adelylation (A) domain, an ayl-carrier protein (ACP) domain and a thioesterase (TE) domain. The enzyme activates (indol-3-yl)pyruvate by adenylation and catalyses the dimerization/cyclization of two such molecules to form didemethylasterriquinone D. Didemethylasterriquinone D is subsequently converted to terrequinone A, a cytotoxic compound that displays a broad range of bioactivities.

EC 6.4.1.12 created 2025

1  [PMID:16426969]

2  [PMID:17584611]

3  [PMID:17704773]