| Characterization of the PLP-dependent aminotransferase NikK from Streptomyces tendae and its putative role in nikkomycin biosynthesis. | |
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MedLine Citation:
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PMID: 21884568 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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As inhibitors of chitin synthase, nikkomycins have attracted interest as potential antibiotics. The biosynthetic pathway to these peptide nucleosides in Streptomyces tendae is only partially known. In order to elucidate the last step of the biosynthesis of the aminohexuronic building block, we have heterologously expressed a predicted aminotransferase encoded by the gene nikK from S. tendae in Escherichia coli. The purified protein, which is essential for nikkomycin biosynthesis, has a pyridoxal-5-phosphate cofactor bound as a Schiff base to lysine 221. The enzyme possesses aminotransferase activity and uses several standard amino acids as amino group donors with a preference for glutamate (Glu > Phe > Trp > Ala > His > Met > Leu). Therefore, we propose that NikK catalyzes the introduction of the amino group into the ketohexuronic acid precursor of nikkomycins. At neutral pH, the UV-Vis absorbance spectrum of NikK has two absorbance maxima at 357 and 425 nm indicative of the presence of the deprotonated and protonated aldimine with an estimated pK(a) of 8.3. The rate of donor substrate deamination is faster at higher pH, indicating that an alkaline environment favors the deamination reaction. |
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Authors:
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Alexandra Binter; Gustav Oberdorfer; Sebastian Hofzumahaus; Stefanie Nerstheimer; Georg Altenbacher; Karl Gruber; Peter Macheroux |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-9-2 |
Journal Detail:
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Title: The FEBS journal Volume: - ISSN: 1742-4658 ISO Abbreviation: - Publication Date: 2011 Sep |
Date Detail:
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Created Date: 2011-9-2 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101229646 Medline TA: FEBS J Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Journal compilation © 2011 Federation of European Biochemical Societies. |
Affiliation:
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From Graz University of Technology, Institute of Biochemistry, Graz, Austria University of Graz, Institute of Molecular Biosciences, Graz, Austria. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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