Document Detail

Delta-amino group hydroxylation of L-ornithine during coelichelin biosynthesis.
MedLine Citation:
PMID:  18452021     Owner:  NLM     Status:  MEDLINE    
The nonribosomally produced hydroxamate siderophore coelichelin from Streptomyces coelicolor contains the nonproteinogenic amino acids N(5)-hydroxyornithine and N(5)-hydroxyformylornithine that are important for iron assembly. The hydroxylation of the delta-amino group of L-ornithine is catalyzed by the flavin-dependent monooxygenase CchB. During the redox reaction nicotinamide adenine dinucleotide phosphate (NADPH) and molecular oxygen are consumed and flavin adenine dinucleotide (FAD) is needed as a cofactor. During this work the monooxygenase was biochemically characterized and it could be shown that the hydroxylation of l-ornithine is most likely the first step in the biosynthesis of the siderophore coelichelin.
Verena Pohlmann; Mohamed A Marahiel
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-04-04
Journal Detail:
Title:  Organic & biomolecular chemistry     Volume:  6     ISSN:  1477-0520     ISO Abbreviation:  Org. Biomol. Chem.     Publication Date:  2008 May 
Date Detail:
Created Date:  2008-05-02     Completed Date:  2008-08-05     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101154995     Medline TA:  Org Biomol Chem     Country:  England    
Other Details:
Languages:  eng     Pagination:  1843-8     Citation Subset:  IM    
Chemistry/Biochemistry Department, Philipps-University Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany.
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MeSH Terms
Chromatography, High Pressure Liquid
Hydrogen Peroxide / chemistry
Hydrogen-Ion Concentration
Mass Spectrometry
Molecular Structure
Oligopeptides / biosynthesis*,  chemistry*
Ornithine / chemistry*
Oxygenases / isolation & purification,  metabolism
Substrate Specificity
Reg. No./Substance:
0/Oligopeptides; 0/coelichelin; 7006-33-9/Ornithine; 7722-84-1/Hydrogen Peroxide; EC 1.13.-/Oxygenases; EC monooxygenase (N-oxide forming)

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