The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine

Marsha A. Gaston, Liwen Zhang, Kari B. Green-Church and Joseph A. Krzycki ()
Additional contact information
Marsha A. Gaston: 484 West 12th Avenue, Ohio State University
Liwen Zhang: CCIC/Mass Spectrometry and Proteomics Facility, 460 West 12th Avenue, Ohio State University
Kari B. Green-Church: CCIC/Mass Spectrometry and Proteomics Facility, 460 West 12th Avenue, Ohio State University
Joseph A. Krzycki: 484 West 12th Avenue, Ohio State University

Nature, 2011, vol. 471, issue 7340, 647-650

Abstract: Biosynthesis of the twenty-second amino acid Pyrrolysine, the latest addition to the ranks of the genetically encoded amino acids, is found in methanogenic archaea and bacteria, in which it is a necessary component of the enzymes involved in the formation of methane from methylamines. Its biosynthetic pathway remains poorly characterized. Joseph Krzycki and colleagues now show that lysine is the sole precursor for the pyrrolysine synthesis system of Methanosarcina sp. Archaea. The radical S-adenosyl-L-methionine protein PylB converts lysine to 3-methylornithine, which then undergoes a PylC-catalysed condensation with a second lysine to generate a product that is oxidized by PylD to generate pyrrolysine. The authors suggest that synthetic analogues of intermediates in this pathway may provide useful pyrrolysine derivatives that could be incorporated into tailored recombinant proteins.

Date: 2011
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature09918 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:471:y:2011:i:7340:d:10.1038_nature09918

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature09918

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().