| Delta-amino group hydroxylation of L-ornithine during coelichelin biosynthesis. | |
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MedLine Citation:
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PMID: 18452021 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Verena Pohlmann; Mohamed A Marahiel |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-04-04 |
Journal Detail:
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Title: Organic & biomolecular chemistry Volume: 6 ISSN: 1477-0520 ISO Abbreviation: Org. Biomol. Chem. Publication Date: 2008 May |
Date Detail:
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Created Date: 2008-05-02 Completed Date: 2008-08-05 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101154995 Medline TA: Org Biomol Chem Country: England |
Other Details:
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Languages: eng Pagination: 1843-8 Citation Subset: IM |
Affiliation:
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Chemistry/Biochemistry Department, Philipps-University Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amination Chromatography, High Pressure Liquid Hydrogen Peroxide / chemistry Hydrogen-Ion Concentration Hydroxylation Kinetics Mass Spectrometry Molecular Structure Oligopeptides / biosynthesis*, chemistry* Ornithine / chemistry* Oxygenases / isolation & purification, metabolism Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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0/Oligopeptides; 0/coelichelin; 7006-33-9/Ornithine; 7722-84-1/Hydrogen Peroxide; EC 1.13.-/Oxygenases; EC 1.14.13.8/dimethylaniline monooxygenase (N-oxide forming) |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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