The Enzymology of Prochlorosin Biosynthesis

Methods in Enzymology
Silvia C Bobeica, Wilfred A van der Donk

Abstract

Lanthipeptides are ribosomally synthesized and posttranslationally modified peptides containing thioether cross-links formed through addition of a cysteine to a dehydroalanine (to form lanthionine) or to a dehydrobutyrine (to form 3-methyllanthionine). Genome sequencing of marine cyanobacteria lead to the discovery of 1.6 million open reading frames encoding lanthipeptides. In many cases, a genome encodes a single lanthipeptide synthetase, but a large number of substrates. The enzymatic modification process in Prochlorococcus MIT9313 has been reconstituted in vitro, and a variety of experimental approaches have been used to try and understand how one enzyme is capable of modifying 30 different substrates. The methods used to characterize this system will be described along with a brief genomic description of the lanthipeptide landscape found in Prochlorococcus and Synechococcus.

Citations

Nov 6, 2018·ChemMedChem·Shimaa A H Abdel MonaimFernando Albericio
Jul 10, 2019·Journal of Molecular Biology·Timothy A Wencewicz
Jun 10, 2021·Analytical and Bioanalytical Chemistry·Kevin Jeanne Dit FouqueFrancisco Fernandez-Lima
Aug 17, 2021·Frontiers in Bioengineering and Biotechnology·Caiyun LiAiying Li
May 3, 2019·ACS Synthetic Biology·Julian D HegemannWilfred A van der Donk
Nov 2, 2021·Journal of the American Chemical Society·Tung LeWilfred A van der Donk

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