Cofactor biosynthesis through protein post-translational modification

Erik T. Yukl, Carrie M. Wilmot

Research output: Contribution to journalReview articlepeer-review

12 Scopus citations

Abstract

Post-translational modifications of amino acids can be used to generate novel cofactors capable of chemistries inaccessible to conventional amino acid side chains. The biosynthesis of these sites often requires one or more enzyme or protein accessory factors, the functions of which are quite diverse and often difficult to isolate in cases where multiple enzymes are involved. Herein is described the current knowledge of the biosynthesis of urease and nitrile hydratase metal centers, pyrroloquinoline quinone, hypusine, and tryptophan tryptophylquinone cofactors along with the most recent work elucidating the functions of individual accessory factors in these systems. These examples showcase the breadth and diversity of this continually expanding field.

Original languageEnglish (US)
Pages (from-to)54-59
Number of pages6
JournalCurrent opinion in chemical biology
Volume16
Issue number1-2
DOIs
StatePublished - Apr 2012

Bibliographical note

Funding Information:
This work was supported by National Institutes of Health grants GM-66569 (CMW) and GM-97779 (ETY). Computing was provided by the Minnesota Supercomputing Institute for Advanced Computational Research.

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