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Bacillus sp. E1이 생성하는 Cyclodextrin Glucanotransferase의 정제 및 특성
박천석,우의전,국승욱,서병철,박관화,임훈,Park, Cheon-Seok,Woo, Eui-Jeon,Kuk, Seung-Uk,Seo, Byung-Cheol,Park, Kwan-Hwa,Lim, Hoon 한국미생물·생명공학회 1992 한국미생물·생명공학회지 Vol.20 No.2
Bacillus sp. was isolated from soil for its strong activity of cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19). The enzyme was purified by gel filtration and anion exchange column chromatography using FPLC. The purified enzyme exhibited its maximum CGTase activity in the pH range of 6~8 and the temperature range of 50~$70^{\circ}C$. The molecular weight was estimated as 114,000 by SDS-PAGE. The isoelectric point of the enzyme was 4.3. The CGTase of Bacillus sp. E l produced $\beta$-cyclodextrin mainly and did not produce a-cyclodextrin. The product ratio of $\beta$-cyclodextrin to $\gamma$-cyclodextrin was 7:l. Cyclodextrin glucanotransferase 생산균주 선발배지를 이용하여 국내 토양으로부터 CGTase 활성이 우수한 Bacillus sp. E1균주를 분리하였다. FPLC를 이용하여 gel filtration과 anion exchange column chromatography를 한 결과 순수 정제된 단일 단백질을 얻을 수 있었으며, 정제된 효소의 최적 작용 pH 범위는 6에서 8까지 였고, 온도는 $60^{\circ}C$에서 최적을 나타냈다. 정제된 단백질의 분자량은 114,000, 등전점은 4.3이었다. 생성된 cyclodextrin은 $\beta$와 $\gamma$-cyclodextrin이 주였으며, 특이하게도 $\alpha$-cyclodextrin은 거의 생성되지 않았다. 작용 후 25시간 후 최대의 $\beta$-cyclodextrin이 생성되었으며, 이때 $\beta$-cyclodextrin과 $\gamma$-cyclodextrin의 생성비율은 7:1이었다.
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Bacillus sp. E1이 생성하는 Cytlodextrin Glucanotransferase의 정제 및 특성
박천석,우의전,국승욱,서병철,박관화,임훈 한국산업미생물학회 1992 한국미생물·생명공학회지 Vol.20 No.2
Cyclodextrin glucanotransferase 생성균주 선발배지를 이용하여 국내 토양으로부터 CGTase 활성이 우수한 Bacillus sp. E1 균주를 분리하였다. FPLC를 이용하여 gel filtration과 anion exchange column chromatography를 한 결과 순수 정제된 단일 단백질을 얻을 수 있었으며, 정제된 효소의 최적 작용 pH 범위는 6에서 8까지였고, 온도는 60℃에서 최적을 나타냈다. 정제된 단백질의 분자량은 114,000, 등전점은 4.3이었다. 생성된 cyclodextrin은 β-와 γ-cyclodextrin이 주였으며, 특이하게도 α-cyclodextrin은 거의 생성되지 않았다. 작용 후 25시간 후 최대의 β-cyclodextrin이 생성되었으며, 이때 β-cyclodextrin과 γ-cyclodextrin의 생성비율은 7:1이었다. Bacillus sp. was isolated from soil for its strong activity of cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19). The enzyme was purified by gel filtration and anion exchange column chromatography using FPLC. The purified enzyme exhibited its maximum CGTase activity in the pH range of 6∼8 and the temperature range of 5O∼70℃ The molecular weight was estimated as 114,000 by SDS-PAGE. The isoelectric point of the enzyme was 4.3. The CGTase of Bacillus sp. El produced β-cyclodextrin mainly and did not produce α-cyclodextrin. The product ratio of β-cyclodextrin to γ-cyclodextrin was 7:1.
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Structural features of archaeal β-phosphoglucomutase from hyperthermophilic Pyrococcus sp. ST 04
박광현,정종현,박천석,우의전 한국구조생물학회 2014 Biodesign Vol.2 No.3
β-Phosphoglucomutase (β-PGM) catalyzes the conversion of β-glucose-1-phosphate (β-G1P) to glucose-6-phosphate(G6P). Upon binding to the substrate, β-PGM adopts a conformational change of cap domain over the core domain withconcomitant closure of the active sites located at the domain interface. Recently we have identified a novel β-PGM fromPyrococcus sp. ST04 (PsPGM) that is highly thermostable, with an optimal temperature of 95℃. The crystal structure ofPsPGM shows two domains: the core domain with a typical β/α barrel-fold of haloacid dehalogenase (HAD) family, and thecap domain with α-helical bundles. The core domain contains the active site with the conserved Asp7 and cofactor Mg2+,exposing the catalytic residue to the surface. Unlike bacterial β-PGMs, the cap domain of PsPGM exists in a significantlytilted, half-closed conformation, which positions Lys82 in close proximity to the substrate binding in the absence of ligand. This unique configuration of the cap domain distinguishes this archaic enzyme from typical bacterial β-PGMs and providesa molecular basis for its enzymatic characteristics at high temperature.
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이수진,백인영,Yan An,안우찬,박광현,우의전 한국구조생물학회 2019 Biodesign Vol.7 No.2
DmpR is a Pseudomonas-derived σ54-dependent transcription regulator in the presence of aromatic compounds. As asingle component regulator and a bacterial enhancer binding protein in the AAA+ ATPase family, the activation mechanismof the DmpR protein has long remained elusive. The AAA+ ATPase domain of the protein is known to be essential in itsoligomerization and interaction with the RNA polymerase sigma factor σ54. However, the structure of the ATPase domain ofDmpR is still unknown. Thus, we performed a purification, crystallization and preliminary X-ray crystallographic study of theATPase domain (residues 232−480) of DmpR from Pseudomonas putida KCTC 1452. The ATPase domain was crystallizedusing hanging-drop vapor diffusion from a reservoir solution containing 20% w/v PEG 3350, 280 mM Ammonium sulfate,and 100 mM Tris pH 8.5 and 30% 1,6-Hexanediol. The diffraction data to a ~3.0 Å resolution show that the crystal belongsto the space group P622 with unit cell parameters of a = 104.366 Å, b = 104.366 Å, c = 46.865 Å, α = β = 90° and γ = 120°. The structure of the ATPase would help to understand the DmpR oligomerization mechanism and interaction with σ54 intranscriptional initiation.
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Lin Ying Li,Thi Minh Nguyet Nguyen,우의전,박종태,황인규 충남대학교 농업과학연구소 2020 Korean Journal of Agricultural Science Vol.47 No.2
Integrins such as lymphocyte function-associated antigen -1 (LFA-1) have an essential role in T cell immunity. Integrin activation, namely, the transition from the inactive conformation to the active one, takes place when an intracellular signal is generated by specific receptors such as T cell receptors (TCRs) and chemokine receptors in T cells. In an effort to explore the molecular mechanisms underlying the TCR-mediated LFA-1 activation, we had previously established a high-throughput cell-based assay and screened a chemical library deposited in the National Institute of Health in the United States. As a result, several hits had been isolated including HIKS-1 (Benzo[b]thiophene-3-carboxylic acid, 2-[3-[(2-carboxyphenyl) thio]- 2,5-dioxo-1-pyrrolinyl]-4,5,6,7-tetrahydro-,3-ethyl ester). In an attempt to reveal the mode of action of HIKS-1, in this study, we did drug affinity responsive target stability (DARTS) assay finding that HIKS-1 interacted with the IQ motif containing GTPase activating protein 1 (IQGAP1), a 189 kDa multidomain scaffold protein critically involved in various signaling mechanisms. Furthermore, the cellular thermal shift assay (CETSA) provided compelling evidence that HIKS-1 also interacted with IQGAP1 in vivo. Taken together, it can be concluded that HIKS-1 interferes with the TCR-mediated LFA-1 activation by interacting with IQGAP1 and thereby disrupting the signaling pathway for LFA-1 activation.
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