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Issue 75, 2020
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Increasing cytochrome P450 enzyme diversity by identification of two distinct cyclodipeptide dimerases

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Abstract

Genome mining revealed the presence of two cdps-p450 operons in Saccharopolyspora antimicrobica. Heterologous expression, biochemical characterisation and structure elucidation proved that the two P450 enzymes catalyse distinct regio- and stereospecific dimerizations of cyclo-(L-Trp-L-Trp), which significantly expands the repertoire of diketopiperazine-tailoring enzymes. TtpB1 connects the monomers via C3–C3′, both from the opposite side of H-11/H-11′, while TtpB2 is characterised as the first P450 to mainly catalyse the unusual linkage between N1′ and C3 from the H-11 side.

Graphical abstract: Increasing cytochrome P450 enzyme diversity by identification of two distinct cyclodipeptide dimerases

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Article information


Submitted
10 Jul 2020
Accepted
07 Aug 2020
First published
07 Aug 2020

Chem. Commun., 2020,56, 11042-11045
Article type
Communication

Increasing cytochrome P450 enzyme diversity by identification of two distinct cyclodipeptide dimerases

J. Liu, X. Xie and S. Li, Chem. Commun., 2020, 56, 11042
DOI: 10.1039/D0CC04772D

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