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( Pageni Binod Babu ),( Tae Jin Oh ),( Kwang Kyoung Liou ),( Yeo Joon Yoon ),( Jae Kyung Sohng ) 한국미생물 · 생명공학회 2008 Journal of microbiology and biotechnology Vol.18 No.1
Two sugar biosynthetic cassette plasmids were used to direct the biosynthesis of a deoxyaminosugar. The pOTBP1 plasmid containing TDP-glucose synthase (desIII), TDPglucose-4,6-dehydratase (desIV), and glycosyltransferase (desVII/desVIII) was constructed and transformed into S. venezuelae YJ003, a strain in which the entire gene cluster of desosamine biosynthesis is deleted. The expression plasmid pOTBP3 containing 4-aminotransferase (gerB) and 3,5-epimerase (orf9) was transformed again into S. venezuelae YJ003-OTBP1 to obtain S. venezuelae YJ003-OTBP3 for the production of 4-amino-4,6-dideoxy-L-glucose derivatives. The crude extracts obtained from S. venezuelae ATCC 15439, S. venezuelae YJ003, and S. venezuelae YJ003-OTBP3 were further analyzed by TLC, bioassay, HPLC, ESI/MS, LC/MS, and MS/MS. The results of our study clearly shows that S. venezuelae YJ003-OTBP3 constructs other new hybrid macrolide derivatives including 4-amino-4,6-dideoxy-L-glycosylated YC-17 (3, [M+ Na+] m/z=464.5), methymycin (4, m/z=480.5), novamethymycin (6, m/z=496.5), and pikromycin (5, m/z=536.5) from a 12-membered ring aglycon (10-deoxymethynolide, 1) and a 14-membered ring aglycon (narbonolide, 2). These results suggest a successful engineering of a deoxysugar pathway to generate novel hybrid macrolide derivatives, including deoxyaminosugar.
Biosynthesis of Dihydrochalcomycin: Characterization of a Deoxyallosyltransferase(gerGTI)
Pageni, Binod Babu,Simkhada, Dinesh,Oh, Tae-Jin,Sohng, Jae-Kyung Korean Society for Molecular and Cellular Biology 2010 Molecules and cells Vol.29 No.2
Through an inactivation experiment followed by complementation, the gerGTII gene was previously characterized as a chalcosyltransferase gene involved in the biosynthesis of dihydochalcomycin. The glycosyltransferase gerGTI was identified as a deoxyallosyltransferase required for the glycosylation of D-mycinose sugar. This 6-deoxyhexose sugar was converted to mycinose, via bis-O-methylation, following attachment to the polyketide lactone during dihydrochalcomycin biosynthesis. Gene sequence alignment of gerGTI to several glycosyltransferases revealed a consensus sequence motif that appears to be characteristic of the enzymes in this sub-group of the glycosyltransferase family. To characterize its putative function, genetic disruption of gerGTI in the wild-type strain Streptomyces sp. KCTC 0041BP and in the gerGTII-deleted mutant (S. sp. ${\Delta}$gerGTsss, as well as complementation of gerGTII in S. sp. ${\Delta}$gerGTss-GTs, were carried out, and the products were analyzed by LC/MS. S. sp. ${\Delta}$gerGTss-GTs mutant produced dihydrochalconolide macrolide. S. sp. ${\Delta}$gerGTs and S. sp. ${\Delta}$gerGTss-GTs complementation of gerGTII yielded dihydrochalconolide without the mycinose sugar. The intermediate shows that gerGTI encodes a deoxyallosyltransferase that acts after gerGTII.
Characterization of a Chalcosyltransferase (gerGTII) in Dihydrochalcomycin Biosynthesis
Pageni, Binod Babu,Oh, Tae-Jin,Thuy, Ta Thi Thu,Sohng, Jae Kyung Korean Society for Molecular Biology 2008 Molecules and cells Vol.26 No.3
An open reading frame, designated GerGTII and located downstream of the polyketide synthase genes, has been identified as a chalcosyltransferase by sequence analysis in the dihydrochalcomycin biosynthetic gene cluster of Streptomyces sp. KCTC 0041BP. The deduced product of gerGTII is similar to several glycosyltransferases, authentic and putative, and it displays a consensus sequence motif that appears to be characteristic of a sub-group of these enzymes. Specific disruption of gerGTII within the S. sp. KCTC 0041BP genome by insertional in-frame deletion method, resulted complete abolishment of dihydrochalcomycin and got the 20-O-mycinosyl-dihydrochalconolide as intermediate product in dihydrochalcomycin biosynthesis which was confirmed by electron spray ionization-mass spectrometry and liquid chromatography-mass spectrometry. Dihydrochalcomycin also was recovered after complementation of gerGTII.
Characterization of a Chalcosyltransferase (gerGTII) in Dihydrochalcomycin Biosynthesis
Binod Babu Pageni,오태진,Ta Thi Thu Thuy,송재경 한국분자세포생물학회 2008 Molecules and cells Vol.26 No.3
An open reading frame, designated GerGTII and located downstream of the polyketide synthase genes, has been identified as a chalcosyltransferase by sequence analysis in the dihydrochalcomycin biosynthetic gene cluster of Streptomyces sp. KCTC 0041BP. The deduced product of gerGTII is similar to several glycosyltransferases, authentic and putative, and it displays a consensus sequence motif that appears to be characteristic of a sub-group of these enzymes. Specific disruption of gerGTII within the S. sp. KCTC 0041BP genome by insertional in-frame deletion method, resulted complete abolishment of dihydrochalcomycin and got the 20-O-mycinosyl-dihydrochalconolide as intermediate product in dihydrochalcomycin biosynthesis which was confirmed by electron spray ionization-mass spectrometry and liquid chromatography-mass spectrometry. Dihydrochalcomycin also was recovered after complementation of gerGTII.
Binod Babu Pageni,오태진,유진철,송재경 한국생물공학회 2008 Biotechnology and Bioprocess Engineering Vol.13 No.6
Two genes, orf6 and orf9 located in the L-oleandrose sugar biosynthetic gene cluster of Streptomyces antibioticus Tü99. NovU has been characterized as C-5 methyltrnaferase involved in noviose biosynthetic pathway. We have cloned and heterologously expressed the orf6, orf9, and novU genes in S. venezuelae YJ003-OTBP1. This established the function of orf6 and orf9 as 4-ketoreductase and 3-epimerase, respectively. All of analytical data of the noviosylated 10-deoxymethynolide also is in support of proving their functions. Furthermore biosynthetic pathway 5,5-gem-dimethyl-6-deoxyglucose (TDP-L-noviose) has been proposed.
Biosynthesis of Dihydrochalcomycin: Characterization of a Deoxyallosyltransferase (gerGTI)
Binod Babu Pageni,Dinesh Simkhada,오태진,송재경 한국분자세포생물학회 2010 Molecules and cells Vol.29 No.2
Through an inactivation experiment followed by comple-mentation, the gerGTII gene was previously characterized as a chalcosyltransferase gene involved in the biosynthesis of dihydochalcomycin. The glycosyltransferase gerGTI was identified as a deoxyallosyltransferase required for the gly-cosylation of D-mycinose sugar. This 6-deoxyhexose sugar was converted to mycinose, via bis-O-methylation, following attachment to the polyketide lactone during dihydrochalco-mycin biosynthesis. Gene sequence alignment of gerGTI to several glycosyltransferases revealed a consensus se-quence motif that appears to be characteristic of the en-zymes in this sub-group of the glycosyltransferase family. To characterize its putative function, genetic disruption of gerGTI in the wild-type strain Streptomyces sp. KCTC 0041BP and in the gerGTII-deleted mutant (S. sp. ΔgerGTII), as well as complementation of gerGTII in S. sp. ΔgerGTII-GTI, were carried out, and the products were analyzed by LC/MS. S. sp. ΔgerGTII-GTI mutant produced dihydrochal-conolide macrolide. S. sp. ΔgerGTI and S. sp. ΔgerGTII-GTI complementation of gerGTII yielded dihydrochalconolide without the mycinose sugar. The intermediate shows that gerGTI encodes a deoxyallosyltransferase that acts after gerGTII.