TAILIEUCHUNG - Báo cáo khoa hoc : Characterization of the PLP-dependent aminotransferase NikK from Streptomyces tendae and its putative role in nikkomycin biosynthesis

As inhibitors of chitin synthase, nikkomycins have attracted interest as potential antibiotics. The biosynthetic pathway to these peptide nucleosides in Streptomyces tendaeis 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. | IFEBS Journal Characterization of the PLP-dependent aminotransferase NikK from Streptomyces tendae and its putative role in nikkomycin biosynthesis Alexandra Binter1 Gustav Oberdorfer2 Sebastian Hofzumahaus1 Stefanie Nerstheimer1 Georg Altenbacher1 Karl Gruber2 and Peter Macheroux1 1 Graz University of Technology Institute of Biochemistry Austria 2 University of Graz Institute of Molecular Biosciences Austria Keywords aminohexuronic acid antibiotics docking homology model Correspondence Peter Macheroux Institute of Biochemistry Graz University of Technology Petersgasse 12 A-8010 Graz Austria Fax 43 316 873 6952 Tel 43 316 873 6450 E-mail Karl Gruber Institute of Molecular Biosciences University of Graz Humboldtstr. 50 3 A-8010 Graz Austria Fax 43 316 380 9897 Tel 43 316 380 5483 E-mail Received 6 July 2011 revised 29 August 2011 accepted 30 August 2011 doi 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 catalyses the introduction of the amino group into the ketohexuronic acid precursor of nikk-omycins. At neutral pH the UV-visible 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

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