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( Nguyen Duc Anh ),( Nguyen Thi Thu ),( Nguyen Thi Ngoc Diep ),황인엽,이은열 한국공업화학회 2016 한국공업화학회 연구논문 초록집 Vol.2016 No.0
Natural one-carbon metabolic pathways in native hosts such as methylotrophs have recently been reconstructed in non-native hosts mainly in methanol. Engineering strategy for methanol bioconversion was the implementation of NAD-dependent methanol dehydrogenase (MDH) and co-expressing two key enzymes in ribulose monophosphate cycle (RuMP) were hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi). MDH and several Hps-Phi gene clusters as well as artificial fusion forms from different type I methanotrophs were cloned and screened. As a results, in vitro activity of mdh and Hps-Phi were detected. The data provided new opportunities for reconstruction of methanol metabolic pathway from methanotrophs into non-native hosts.
Hyung Il Lee,Hwa Jeong Cho,Jung A Han,장소영,Kyoung Min Wang,강현태,황은성 생화학분자생물학회 2008 Experimental and molecular medicine Vol.40 No.2
Nicotinamide at millimolar concentrations affects cell survival in various conditions, and is being utilized therapeutically in many human diseases. However, the effect of an acute treatment of nicotinamide at such high dose on gene expression and cellular metabolism has rarely been determined previously. In this study, we found that levels of O-N-acetylglucosamin(OGlcNAc) ylated proteins including Sp1 acutely decreased upon treatment of 10 mM nicotinamide. Concomitantly, Sp1 protein level decreased rapidly through accelerated proteasome-mediated proteolysis. Cotreatment of glucosamine or 2-deoxyglucose, which inhibits protein deGlcNAcylation, effectively blocked the decrease induced by nicotinamide. Interestingly, the decline in the levels of Sp1 and protein OGlcNAcylation was only transient lasting for two days post treatment, and this pattern matched closely the rapid fluctuation of the cellular [NAD+]. Our results suggest a possible link between cellular nicotinamide metabolism and protein O-GlcNAcylation, and an existence of cellular [NAD+] homeostasis.
이지나,최재원,한혜영,김우식,송하연,Eui-Baek Byun,Eui-Hong Byun,이영하,육재민 대한기생충학ㆍ열대의학회 2020 The Korean Journal of Parasitology Vol.58 No.1
Toxoplasma gondii is an intracellular protozoan parasite that infects approximately one third of the human population worldwide. Considering the toxicity and side effects of anti-toxoplasma medications, it is important to develop effective drug alternatives with fewer and less severe off-target effects. In this study, we found that 4-hydroxybenzaldehyde (4-HBA) induced autophagy and the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1) in primary murine bone marrow-derived macrophages (BMDMs). Interestingly, treatment of BMDMs with 4-HBA significantly reduced the number of macrophages infected with T. gondii and the proliferation of T. gondii in infected cells. This effect was impaired by pretreating the macrophages with 3-methyladenine or wortmannin (selective autophagy inhibitors) or with sirtinol or EX527 (SIRT1 inhibitors). Moreover, we found that pharmacological inhibition of SIRT1 prevented 4-HBA-mediated expression of LC3-phosphatidylethanolamine conjugate (LC3-II) and the colocalization of T. gondii parasitophorous vacuoles with autophagosomes in BMDMs. These data suggest that 4-HBA promotes antiparasitic host responses by activating SIRT1-mediated autophagy, and 4-HBA might be a promising therapeutic alternative for the treatment of toxoplasmosis.
Sinorhizobium meliloti 유래 Mannitol Dehydrogenase 유전자의 클로닝 및 대장균 내 발현과 효소특성 규명
장명운 ( Myoung Uoon Jang ),박정미 ( Jung Mi Park ),김민정 ( Min Jeong Kim ),이소원 ( So Won Lee ),강정현 ( Jung Hyun Kang ),김태집 ( Tae Jip Kim ) 한국미생물생명공학회(구 한국산업미생물학회) 2013 한국미생물·생명공학회지 Vol.41 No.2
Sinorhizobium meliloti 1021 (KCTC 2353) 유전체로부터 mannitol dehydrogenase (SmMDH)로 추정되는 유전자를 클로닝하고, 대장균에서 대량 발현하였다. 이 유전자는 494개의 아미노산(약 54 kDa)을 암호화하는 1,485 bp의 염기로 구성되며, 기존에 보고된 long-chain dehydrogenase/reductase 계열 MDH 효소들과 약 35-55%의 아미노산 서열상동성을 나타내었다. 재조합 SmMDH의 최적 반응온도는 40oC이며, pH 7.0의 조건에서 최대의 D-fructose 환원활성, 그리고 pH 9.0에서 최대의 D-mannitol 산화활성을 보였다. 특히, 이 효소는 NAD+/NADH 조효소의 존재 하에서 산화· 환원 활성을 나타내며, NADP+/NADPH는 조효소로 이용하지 못하였다. 결론적으로 SmMDH는 전형적인 NAD+/NADH-의존형 mannitol dehydrogenase (EC 1.1.1.67)임을 확인하였다. A mannitol dehydrogenase (MDH; EC 1.1.1.67) gene was cloned from the Sinorhizobium meliloti 1021 (KCTC 2353) genome and expressed in Escherichia coli. It was seen to have an open reading frame consisting of 1,485 bp encoding 494 amino acids (about 54 kDa), which shares approximately 35-55% of amino acid sequence identity with some known long chain dehydrogenase/ reductase family enzymes. The recombinant S. meliloti MDH (SmMDH) showed the highest activity at 40oC, and pH 7.0 (D-fructose reduction) and pH 9.0 (D-mannitol oxidation), respectively. SmMDH could catalyze the oxidative/reductive reactions between D-mannitol and D-fructose in the presence of NAD+/NADH as a coenzyme, but not with NADP+/NADPH. These results indicate that SmMDH is a typical NAD+/NADH-dependent mannitol dehydrogenase.
Bacillus cereus에서 유래한 Lactate Dehydrogenase 동질효소 유전자의 대장균 내 발현 및 효소특성 규명
장명운,박정미,이홍균,이소라,김태집,Jang, Myoung-Uoon,Park, Jung-Mi,Lee, Hong-Gyun,Lee, So-Ra,Kim, Tae-Jip 한국미생물학회 2010 미생물학회지 Vol.46 No.2
Lactate dehydrogenases (LDHs)는 세포 내의 생화학적 대사경로에서 중요한 역할을 담당하는 효소로서 오랜 동안 많은 관심을 받았다. 본 연구에서는 다양한 미생물 genome database의 탐색을 통해 Bacillus cereus ATCC 14579 genome으로부터 LDH로 추정되는 3종의 유전자를 발견하고, 대장균에서 클로닝 및 대량 발현하였다. 모든 BcLDH 동질효소들의 상동부위 아미노산 잔기 대부분이 기존의 $NAD^+$-의존형 LDH와 높은 상동성을 보였다. 한편 314개의 아미노산으로 이루어진 BcLDH1과 2는 86%의 서열 상동성을 보였으나, BcLDH3와는 49%의 상동성을 나타냈다. 흥미롭게도 BcLDH1만이 $NAD^+$ 조효소 존재 하에서 L-lactate와 pyruvate 간의 상호전환 활성을 나타냈으며, 그 외의 동질효소들은 거의 활성을 보이지 않았다. 결론적으로 BcLDH1은 전형적인 $NAD^+$-의존형이며, L-lactate에 특이적인 dehydrogenase 효소임을 확인하였다. Lactate dehydrogenases (LDHs) have been highly focused for long time, due to their important roles in biochemical and metabolic pathways of cells. On the basis of genome-wide searching results, three putative LDH genes from Bacillus cereus ATCC 14579 genome have been PCR-amplified, cloned, and well-expressed in E. coli. All three BcLDH isozymes are supposed to share highly conserved catalytic amino acid residues in common $NAD^+$-dependent LDHs. Meanwhile, BcLDH1 consisting of 314 amino acids shares 86 and 49% of identities with BcLDH2 and 3, respectively. Interestingly, only BcLDH1 showed the converting activities between L-lactate and pyruvate in the presence of $NAD^+$ coenzyme, while the other isozymes are likely to have almost no activity. As a result, it was revealed that BcLDH1 can be a typical $NAD^+$-dependent L-lactate-specific dehydrogenase.
Kanamasa, Shin,Tajima, Satoshi,Park, Enoch Y. Korean Society for Biotechnology and Bioengineerin 2007 Biotechnology and Bioprocess Engineering Vol.12 No.2
For this study, we hypothesized that mitochondrial $NAD^+-dependent$ isocitrate dehydrogenase 1 (ICDH1) and isocitrate lyase (ICL 1) were important enzymes for riboflavin synthesis in the fungus Ashbya gossypii. Here, the genes encoding ICDH1 and ICL1 were disrupted in order to analyze the enzymes' functions on riboflavin production by the fungus. The riboflavin production resulting from these disruptants was markedly decreased compared to the concentration produced by its parental strain when cultured in a rich nutrient medium used to optimize riboflavin production. Furthermore, when comparing the transcription levels of the genes encoding ICDH1 and ICL1, between wild-type A. gossypii and an itaconate resistant mutant of A. gossypii obtained by UV irradiation, the mRNA levels in the mutant were 1.8- and 2.0-fold higher than those in the wild-type strain, respectively. These results indicate that ICDH1 and ICL1 are key enzymes for riboflavin synthesis in A. gossypii.
Salmonella typhimurium에서 유래한 Mannitol Dehydrogenase 유전자의 대장균 내 발현 및 효소특성 규명
장명운,박정미,김민정,강정현,이소원,김태집,Jang, Myoung-Uoon,Park, Jung-Mi,Kim, Min-Jeong,Kang, Jung-Hyun,Lee, So-Won,Kim, Tae-Jip 한국미생물학회 2012 미생물학회지 Vol.48 No.2
Salmonella typhimurium LT2 (KCTC 2421)로부터 mannitol dehydrogenase (StMDH)로 추정되는 유전자를 클로닝하고, 대장균에서 대량 발현하였다. 이 유전자는 488개의 아미노산 서열(약 54 kDa)을 암호화하는 1,467 bp의 염기로 구성되며, 이미 보고된 long-chain dehydrogenase/ reductase (LDR) 계열 효소들과 약 36%의 아미노산 서열 상동성을 나타내었다. 재조합 StMDH의 최적 반응온도는 $30^{\circ}C$이며, pH 5.0의 조건에서 최대의 D-fructose 환원활성, 그리고 pH 10.0에서 최대의 D-mannitol 산화활성을 보인다. 반면에 glucose, galactose, xylose, arabinose 등의 기질에 대해서는 활성을 보이지 않았다. 이 효소는 $NAD^+$/NADH 존재 하에서만 산화 환원 활성을 가지며, $NADP^+$/NADPH는 조효소로 이용하지 못하였다. 결론적으로 StMDH는 전형적인 $NAD^+$/NADH 의존형의 mannitol dehydrogenase (EC 1.1.1.67)임을 확인하였다. A mannitol dehydrogenase (StMDH) gene was cloned from Salmonella typhimurium LT2 (KCTC 2421) and overexpressed in Escherichia coli. It has a 1,467 bp open reading frame encoding 488 amino acids with deduced molecular mass of 54 kDa, which shares approximately 36% of amino acid identity with known long-chain dehydrogenase/reductatse (LDR) family enzymes. The recombinant StMDH showed the highest activity at $30^{\circ}C$, and pH 5.0 and 10.0 for D-fructose reduction and D-mannitol oxidation, respectively. On the contrary, it has no activity on glucose, galactose, xylose, and arabinose. StMDH can catalyze the oxidative/reductive reactions between D-fructose and D-mannitol only in the presence of $NAD^+$/NADH as coenzymes. These results indicate that StMDH is a typical $NAD^+$/NADH-dependent mannitol dehydrogenase (E.C. 1.1.1.67).