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Oxidative tailoring reactions catalyzed by nonheme iron-dependent enzymes : streptorubin B biosynthesis as an example

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Sydor, Paulina K. and Challis, Gregory L. (2012) Oxidative tailoring reactions catalyzed by nonheme iron-dependent enzymes : streptorubin B biosynthesis as an example. Methods in Enzymology, Volume 516 (Chapter 10). pp. 195-218. doi:10.1016/B978-0-12-394291-3.00002-2 ISSN 0076-6879.

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Official URL: http://dx.doi.org/10.1016/B978-0-12-394291-3.00002...

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Abstract

Tailoring enzymes catalyze reactions that modify natural product backbone structures before, during, or after their biosynthesis to create a final product with specific biological activities. Such reactions can be catalyzed by a myriad of different enzyme families and are responsible for a wide variety of transformations including regio- and/or stereospecific acylation, alkylation, glycosylation, halogenation, and oxidation. Within a broad group of oxidative tailoring enzymes, there is a rapidly growing family of nonheme iron- and oxygen-dependent enzymes that catalyze a variety of remarkable hydroxylation, desaturation, halogenation, and oxidative cyclization reaction in the biosynthesis of several important metabolites, including carbapenems, penicillins, cephalosporins, clavams, prodiginines, fosfomycin, syringomycin, and coronatine. In this chapter, we report an expedient method for analyzing tailoring enzymes that catalyze oxidative cyclization reactions in prodiginine biosynthesis via expression of the corresponding genes in a heterologous host, feeding of putative biosynthetic intermediates to the resulting strains, and liquid chromatography–mass spectrometry analyses of the metabolites produced.

Item Type: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Journal or Publication Title: Methods in Enzymology
Publisher: Academic Press
ISSN: 0076-6879
Book Title: Natural Product Biosynthesis by Microorganisms and Plants, Part B
Official Date: 2012
Dates:
DateEvent
2012Published
Volume: Volume 516
Number: Chapter 10
Page Range: pp. 195-218
DOI: 10.1016/B978-0-12-394291-3.00002-2
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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