The Enzymology of Prochlorosin Biosynthesis

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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.

Original languageEnglish (US)
Title of host publicationMethods in Enzymology
EditorsBradley S. Moore
PublisherAcademic Press Inc.
Pages165-203
Number of pages39
ISBN (Print)9780128139592
DOIs
StatePublished - Jan 1 2018

Publication series

NameMethods in Enzymology
Volume604
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

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Keywords

  • Combinatorial biosynthesis
  • Lanthipeptide
  • Macrocyclic peptides
  • Marine cyanobacteria
  • Prochlorococcus

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Bobeica, S. C., & van der Donk, W. A. (2018). The Enzymology of Prochlorosin Biosynthesis. In B. S. Moore (Ed.), Methods in Enzymology (pp. 165-203). (Methods in Enzymology; Vol. 604). Academic Press Inc.. https://doi.org/10.1016/bs.mie.2018.01.038