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Influence of Apoproteins for Enediyne Production
Vu Thi Thu Hang,김태수,오태진,송재경 한국생물공학회 2011 Biotechnology and Bioprocess Engineering Vol.16 No.3
Kedarcidin and neocarzinostatin belong to the chromoprotein family of endiyene antibiotics and have potent antitumor activity. Their structures consist of an apoprotein and a nonpeptide chromophore. Apoprotein has been known to be essential to stabilize and regulate the availability of a labile chromophore. Here, we have identified the complete kedarcidin apoprotein gene (kedA) from Streptoalloteichus sp. ATCC 53650 (Actinomycete L585-6). KedA was characterized by a comparative study with neocarzinostatin apoprotein (NcsA). Overexpression of kedA resulted in a ~ 2-fold enhanced production of kedarcidin in Streptoalloteichus sp., whereas overexpression of ncsA resulted in a ~ 1.6-fold enhanced production of neocarzinostatin in Streptomyces carzinostaticus ATCC 15944. Moreover, the apoprotein-overexpressed strain showed a high growth rate, which demonstrates that the apoprotein not only protects the labile chromophore, but also tolerates the toxicity of endiyene antibiotics in the host strain.
강옥주,서명자,이안종,김세권,Kang, Ok-Ju,Suh, Myung-Ja,Lee, An-Jong,Kim, Se-Kwon Korean Society of Life Science 1995 생명과학회지 Vol.5 No.4
A carotennnoprotein from the skin of Ascidian(Halocynthia roretzi) was extracted by Triton X-100 and purified by ammonium sulfate fraction, SephadexG-200 charomatography and DEAE-cellulose ion exchange chromatography. The carotenoprotein was redwith broad $\lambda$$_{max}$ between 495, 467 and 318nm. The red carotenoprotein had an approximate molecular weight of 326KDa(gel filtration). SDS-PAGE indicated the presence of two polypeptodes of 84.1KDa and 74.4KDa, with different mobility in polyacrylamide gel electrophoresis. In the presence of denaturing agents such as organic solvent aand extreme pH, the red complex readily disociates to liberate the yellow carotenoid($\lambda$$_{max}$ 452nm) and a colourless apoprotein. The amino acid composition of carotenoprotein were mainly threonine(15.2%), aspartic acid(12.2%), glutamic acid(11.9%) and serine(9.6%), while proline was not found. The carotenoprotein consisted of lipids as structure units. Its major fatty acids composion were C$_{18:1}$, C$_{16:1}$, and C$_{16:0}$. The monounsaturated fatty acids(41.5%) contained abundant content compared to other fatty aacids(polyunsaturated fatty acids 37.4%, saturated fatty acids 20.6%).
Activation of Urease Apoprotein of Helicobacter pylori
Cho, Myung-Je,Lee, Woo-Kon,Song, Jae-Young,An, Young-Sook,Choi, Sang-Haeng,Choi, Yeo-Jeong,Park, Seong-Gyu,Choi, Mi-Young,Baik, Seung-Chul,Lee, Byung-Sang,Rhee, Kwang-Ho The Korea Society for Microbiology 1999 大韓微生物學會誌 Vol.34 No.6
H. pylori produces urease abundantly amounting to 6% of total protein of bacterial mass. Urease genes are composed of a cluster of 9 genes of ureC, ureD, ureA, ureB, ureI, ureE, ureF, ureG, ureH. Production of H. pylori urease in E. coli was studied with genetic cotransformation. Structural genes ureA and ureB produce urease apoprotein in E. coli but the apoprotein has no enzymatic activity. ureC and ureD do not affect urease production nor enzyme activity ureF, ureG, and ureH are essential to produce the catalytically active H. pylori urease of structural genes (ureA and ureB) in E.coli. The kinetics of activation of H. pylori urease apoprotein were examined to understand the production of active H. pylori urease. Activation of H. pylori urease apoprotein, pH dependency, reversibility of $CO_2$ binding, irreversibility of $CO_2$ and $Ni^{2+}$ incorporation, and $CO_2$ dependency of initial rate of urease activity have been observed in vitro. The intrinsic reactivity (ko) for carbamylation of urease apoprotein co expressed with accessory genes was 17-fold greater than that of urease apoprotein expressed without accessory genes. It is concluded that accessory genes function in maximizing the carbamylating deprotonated ${\varepsilon}$-amino group of Lys 219 of urease B subunit and metallocenter of urease apoprotein is supposed to be assembled by reaction of a deprotonated protein side chain with an activating $CO_2$ molecule to generate ligands that facilitate productive nickel binding.
New, Novel Lipid-Lowering Agents for Reducing Cardiovascular Risk: Beyond Statins
김규호,Henry N. Ginsberg,최성희 대한당뇨병학회 2022 Diabetes and Metabolism Journal Vol.46 No.4
Statins are the cornerstone of the prevention and treatment of atherosclerotic cardiovascular disease (ASCVD). However, even under optimal statin therapy, a significant residual ASCVD risk remains. Therefore, there has been an unmet clinical need for novel lipid-lowering agents that can target low-density lipoprotein cholesterol (LDL-C) and other atherogenic particles. During the past decade, several drugs have been developed for the treatment of dyslipidemia. Inclisiran, a small interfering RNA that targets proprotein convertase subtilisin/kexin type 9 (PCSK9), shows comparable effects to that of PCSK9 monoclonal antibodies. Bempedoic acid, an ATP citrate lyase inhibitor, is a valuable treatment option for the patients with statin intolerance. Pemafibrate, the first selective peroxisome proliferator-activated receptor alpha modulator, showed a favorable benefit-risk balance but the large clinical phase 3 trial (Pemafibrate to Reduce Cardiovascular OutcoMes by Reducing Triglycerides IN patiENts With diabe- Tes [PROMINENT]) was recently stopped due to the underperformance from interim analysis. High dose icosapent ethyl, a modified eicosapentaenoic acid preparation, shows cardiovascular benefits. Evinacumab, an angiopoietin-like 3 (ANGPTL3) monoclonal antibody, reduces plasma LDL-C levels in patients with refractory hypercholesterolemia. Novel antisense oligonucleotides targeting apolipoprotein C3 (apoC3), ANGPTL3, and lipoprotein(a) have significantly attenuated the levels of their target molecules with beneficial effects on associated dyslipidemias. Apolipoprotein A1 (apoA1) is considered as a potential treatment to exploit the athero-protective effects of high-density lipoprotein cholesterol (HDL-C), but solid clinical evidence is necessary. In this review, we discuss the mode of action and clinical outcomes of these novel lipid-lowering agents beyond statins.