Nonribosomal peptide
synthetase (NRPS)-like enzymes comprising
A–T–TE architectures catalyze the dimerization of α-keto
carboxylic acids leading to the formation of hydroxybenzoquinones
or lactones. Domain change experiments with five enzymes revealed
that A and A–T domains of phenyl or 4-hydroxyphenyl pyruvate-using
enzymes can be effectively used by the TE domains of other enzymes.
Even the A and A–T domains of an indolyl hydroxybenzoquinone
synthase were successfully recombined with TE domains of a phenyl
and a 4-hydroxyphenyl pyruvate-activating enzyme.
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