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  Oxidative transformations of amino acids and peptides catalysed by cytochromes P450

Cryle, M., Brieke, C., & Haslinger, K. (2013). Oxidative transformations of amino acids and peptides catalysed by cytochromes P450. In E. Farkas, & M. Ryadnov (Eds.), Amino Acids, Peptides and Proteins (pp. 1-36). Oxfordshire, UK: Royal Society of Chemistry.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8EA5-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8EAC-F
Genre: Book Chapter

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AminoAcidsPeptProteins_38_2013_1.pdf (Any fulltext), 2MB
 
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 Creators:
Cryle, Max1, Author              
Brieke, Clara1, Author              
Haslinger, Kristina1, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: Cytochromes P450 (P450s) are a superfamily of oxidoreductases that display not only a high degree of substrate diversity across xenobiotic and secondary metabolism but also show flexibility in the oxidation chemistry that they catalyse. The oxidative transformation of amino acids and peptides by P450s represents an important collection of transformations for this enzyme class: these transformations are used in Nature to diversify the limited range of monomers available for ribosomal peptide production, as well as altering peptides to afford desired biological properties. This chapter will highlight current examples of P450-catalysed transformations of amino acids and peptides, organised by the nature of the oxidative transformation performed by the P450.

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Language(s): eng - English
 Dates: 2013-08-31
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/9781849737081-00001
Other: 7926
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Title: Amino Acids, Peptides and Proteins
Source Genre: Book
 Creator(s):
Farkas, Etelka , Editor
Ryadnov , Maxim , Editor
Affiliations:
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Publ. Info: Oxfordshire, UK : Royal Society of Chemistry
Pages: - Volume / Issue: 38 Sequence Number: - Start / End Page: 1 - 36 Identifier: ISBN: 978-1-84973-585-8