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Streptomyces sp. GCA0001로 부터의 신규 항생물질 Cystocin의 구조분석, 생물활성 및 유도체제조
김자용,이희찬,우진석,송재경 호서대학교 반도체제조장비국산화연구센터 2001 반도체장비학술심포지움 Vol.2001 No.-
본 발명의 Puromycin 유도체인 Cystocin 화합물은 유기 합성에 의해 제조된 물질이 아니라 방선균계열의 신균주인 Streptomyces sp GCA0001로부터 추출된 신규 물질로서, 항박테리아, 항종양 및 항바이러스 활성 등의 생물학적 미생물 활성면에서 종래의 Puromycin 화합물에 비해 현저히 뛰어난 효과를 지니고 있고 Streptomyces sp GCA0001로부터 추출, 분리 및 정제 과정을 통해 제조된 자연의 선택의 과정을 거친 화합물이므로, Puromycin을 대체할 수 있는 획기적인 물질로 볼 수 있다. Cystocin, a derivative of Puromycin, is a new material derived from Streptomyces sp GCA0001, new strain of Actinomycetes spiecies.This compound has outstanding biological activities in anti-bacteria, anti-tumor and anti-virus than former Puromycin compounds.And it is chosen by natural selection processing through extraction, isolation and purification from, so it may replace old Puromycins in most applications.
Glycosylation of free sterol by whole-cell bioconversion in E. coli
Jae Kyung Sohng,Jae Kyung Sohng 한국당과학회 2011 한국당과학회 학술대회 Vol.2011 No.1
Steryl glucosides play important roles in many physiological and biochemical process in organism such as the heat shock, enhancement of immunological system, etc. The alignment of a putative sterol glucosides isolated from S. tropica CNB-440 has been shown 34%, 42% and 57% in homology with the corresponding ones from Arabidopis thaliana, Avena sativa and Salinispora arenicola CNS-205, respectively. Engineered E. coli host-high level production of the UDP-glucose was used for whole-cell bioconversion of free sterol (cholesterol and β-sistosterol) and the production of glycosylated product was only detected with β-sitosterol as substrate.
Sohng, Jae Kyung,Yoo, Jin-cheol 朝鮮大學校 1997 藥學硏究誌 Vol.18 No.2
DNA fragments, homologous to the dTDP-Dgiucose 4,6-dehydratase gene, obtained from the genomic DNA of Streptomyces antibioticus Tu¨99,a producer of the unusual macrolide antibiotic chlorothricin, were cloned and aequenced. This dehydratase gene was designated as oxil. The coding region of the oxil gene is composed of 987 bp, and analysis of the DNA sequence data reveals sequences for the gene products of 329 amino acids(molecular weight of 36.037). The deduced amino acids are 59% identical to the StrE, dTDP-D-glucose 4,6-dehydratase from the Streptomycin pathway. The oxil's function was examined by expressing it in E. coil using the T7 RNA polymerase/promoter system(pRSET) to produce an active fusion protein including a his tag. This enzyme shows apecificity of substrate, specific only to dTDP-D-glucose.
Production, Isolation and Biological Activity of Nargenicin from Nocardia sp. CS682
Sohng, Jae-Kyung,Yamaguchi, Tokutaro,Seong, Chi-Nam,Baik, Keun-Sik,Park, Seong-Chan,Lee, Hyo-Jeong,Jang, So-Young,Simkhada, Jaya Ram,Yoo, Jin-Cheol 대한약학회 2008 Archives of Pharmacal Research Vol.31 No.10
Culture broth of an actinomycete isolate, Nocardia sp. CS682 showed specifically higher antibacterial activity against methicilin resistant Staphylococcus aureus (MRSA). Purified substance from the organism, CS-682, which is active against MRSA and Micrococcus leuteus, is a $C_{28}H_{37}NO_8$ ($M+H^+$, observed: 516.83) and identified as an unusual macrolide antibiotic, nargenicin. The chemical structure of CS-682 was identified by FT-IR, $^1H$-NMR, $^{13}C$-NMR, and ($^1H-^1H$ and $^1H-^{13}H$) COSY. The anti-MRSA activity of CS-682 was stronger than that of oxacillin, vancomycin, monensin, erythromycin, and spiramycin. Phylogenetic analysis showed that strain CS682 is closely related to Nocardia tenerifensis DSM $44704^T$ (98.7% sequence similarity), followed by N. brasiliensis ATCC $19296^T$ (98.4% sequence similarity). The ability of Nocardia sp. CS682 to produce nargenicin was unique.
Sohng, Jae-Kyung,Yoo, Jin-Cheol Korean Society for Biochemistry and Molecular Biol 1996 Journal of biochemistry and molecular biology Vol.29 No.3
DNA fragments, homologous to the dTDP-D-glucose 4,6-dehydratase gene, obtained from the genomic DNA of Streptomyces antibioticus $T\ddot{u}99$, a producer of the unusual macrolide antibiotic chlorothricin, were cloned and sequenced. This dehydratase gene was designated as oxil. The coding region of the oxil gene is composed of 987 bp, and analysis of the DNA sequence data reveals sequences for the gene products of 329 amino acids (molecular weight of 36,037). The deduced amino acids are 59% identical to the StrE, dTDP-D-glucose 4,6-dehydratase from the streptomycin pathway. The oxil's function was examined by expressing it in E. coli using the T7 RNA polymerase/promoter system (pRSET) to produce an active fusion protein including a his tag. This enzyme shows specificity of substrate, specific only to dTDP-D-glucose.
Function of Lysine-148 in dTDP-D-Glucose 4,6-dehydratase from Streptomyces antibioticus Tu99
( Jae Kyung Sohng ),( Hyung Rae Noh ),( Oh Hyoung Lee ),( Sung Jun Kim ),( Ji Man Han ),( Seung Kwan Nam ),( Jin Cheol Yoo ) 한국미생물 · 생명공학회 2002 Journal of microbiology and biotechnology Vol.12 No.2
dTDP-D-glucose 4,6-dehydratase (TDPDH) catalyzes the conversion of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose, and requires NAD+ as a coenzyme for its catalytic activity. The dTDP-D-glucose 4,6-dehydratase from Streptomyces antibioticus Tu99 tightly binds NAD+ [19]. In order to determine the role of lysine-148 in the NAD+ binding, the lysine of the dTDP-D-glucose 4,6-dehydratase from Streptomyces antibioticus Tu99 was mutated to various amino acids by site-directed mutagenesis. The catalytic activity of the four mutated enzymes of TDPDH did not recover after addition of NAD+. However, the activity of K159A, the mutated enzyme of UDP-D-glucose 4-epimerase (UDPE), recovered after the addition of NAD+ [15]. Although dTDP-glucose 4,6-dehydratase, and UDP-galactose (glucose) 4-epimerase are members of the short-chain dehydrogenase/reductase SDR family and the lysine-148 of TDPDH was highly conserved as in UDPE (Lys-l59), the function of the lysine-148 of TDPDH was different from that of UDPE. The mutated enzymes showed that the lysine-l48 of the dTDP-D-glucose 4,6-dehydratase played no role in the NAD+ binding. Accordingly, it is suggested that the lysine-l48 of the dTDP-D-glucose 4,6-dehydratase is involved in the folding of TDPDH.
Sohng, Jae-Kyung,Oh, Tae-Jin,Kim, Chun-Gyu Korean Society for Biochemistry and Molecular Biol 1998 Journal of biochemistry and molecular biology Vol.31 No.5
Many antibiotics contain partially deoxygenated sugar components that are usually essential for biological activity, affinity, structural stability, and solubility of antibiotics. Gene probes of the biosynthetic genes related with the deoxysugar were obtained from PCR. Primers were designed from the conserved peptide sequences of the known dTDP-D-glucose 4,6-dehydratases, which are the key step enzymes in the biosynthesis of deoxysugar. The primers were applied to amplify parts of dehydratase genes to 27 actinomycetes that produce the metabolites containing deoxysugar as structural constituents. About 180 and 340 bp DNA fragments from all of the actinomycetes were produced by PCR and analyzed by Southern blot and DNA sequencing. The PCR products were used as gene probes to clone the biosynthetic gene clusters for the antibiotic mithramycin, rubradirin, spectinomycin, and elaiophyrin. This method should allow for detecting of the biosynthetic gene clusters of a vast array of secondary metabolites isolated from actinomycetes because of the widespread existence of deoxysugar constituents in secondary metabolites.