• 제목/요약/키워드: purine biosynthesis

검색결과 12건 처리시간 0.024초

핵산 대사 길항제 (Antimetabolites in Nucleic Acid Biosynthesis)

  • 장일무
    • 약학회지
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    • 제21권2호
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    • pp.70-80
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    • 1977
  • 본고에서는 핵산 생합성과 Salvage patheway (Preformed Purine Utilization), De novo Pyrimidine Biosynthesis, Slavage patheway (Preformed Pyrimidine Utilization), Purine Base 및 Purine Nucleoside와 비슷한 구조를 가진 핵산 대사 길항제에 대한 내용으로 구성되어 있다.

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Serratia marcescens Purine Nucleoside Phosphorylase의 생합성에 대한 글리옥실산의 대사적 역할 (Metabolic Role of Glyoxylate on the Biosynthesis of Serratia marcescens Purine Nucleoside Phosphorylase)

  • 방선권
    • 한국식품영양학회지
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    • 제12권1호
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    • pp.43-49
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    • 1999
  • The effects of purine catabolites in growth media on the Serratia marcescens purine nucleoside phos-phorylase activity were examined. The enzyme activity was decreased above 60% by guanosine(5 to 15mM). The enzyme activity was not affected at low concentration of inosine (0.1∼1mM). The en-zyme activity was decreased approximately by 40∼50% in the presence of high concentrations of aden-osine hypoxanthine and xanthine (5∼15mM) but was not affected at low concentration of adenosine hypoxanthine and xanthine (0.1∼0.5mM). However the enzyme activity was increase by 20% with low concentrations of uric acid(0.5mN). but was decreased by 80% with high concentrations of same purine catabolite (15mM). Also the enxzyme activity was increased by 20% with low concentrations of glyoxylate (0.5mM) final degradative product of uric acid but was decreased by 30∼50% with high con-centrations of glyoxylate (3∼15mM). The enzyme activity was decreased approximately by 20% by the simultaneous addition of inosine hypoxanthine and uricacid at 5mM each whereas it was increased by 22 and 33% by the combination of inosine and uric acid three purine catabolites at 0.5mM respectively These data suggest that S. marcescens purine nucleoside phosphorylase is positively regulated by a glyox-ylate concentration and then may play a regulatory role in a purine catabolism.

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Identification of Potential Corynebacterium ammoniagenes Purine Gene Regulators Using the pur-lacZ Reporter in Escherichia coli

  • HAN , RI-NA;CHO, ICK-HYUN;CHUNG, SUNG-OH;HAN, JONG-KWON;LEE, JIN-HOO;KIM, SOO-KI;CHOI, KANG-YELL
    • Journal of Microbiology and Biotechnology
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    • 제14권6호
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    • pp.1249-1255
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    • 2004
  • This study has developed Corynebacterium ammoniagenes (c. ammoniagenes) purine gene transcriptional reporters (purF-lacZ and purE-lacZ) that function in Escherichia coli (E. coli) DH5a. After transformation of a C. ammoniagenes gDNA library into E. coli cells harboring either purF-lacZ or purE-lacZ, C. ammoniagenes clones were obtained that repress purF-lacZ and purE-lacZ gene expression. The potential purE and purF regulatory genes are homologous to the genes encoding transcription regulators, the regulatory subunit of RNA polymerase, and genes for purine nucleotide biosynthesis of various bacteria. The C. ammoniagenes purE-lacZ and purF-lacZ reporters were repressed by adenine and guanine within E. coli, indicating similarity in the regulatory mechanism of purine biosynthesis in C. ammoniagenes and E. coli. Gene regulation of pur-lacZ by adenine and guanine was partly abolished in cells expressing potential purine regulatory genes, indicating functionality of the purine gene regulators in repression of purE-lacZ and purF-lacZ. The purE-lacZ and purF-lacZ reporters can be used for the screening of genes involved in the regulation of the de novo synthesis of the purine nucleotides.

Serratia marsecscens 와 Lactobacillus plantarum Purine Nucleoside Phosphorylase의 생합성에 대한 요산의 조절 (The Regulation of Uric Acid on the Biosynthesis of Serratia marcescens and Lactobacillus plantarum Purine Nucleoside Phosphorylase)

  • 최병범
    • 한국식품과학회지
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    • 제33권3호
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    • pp.361-365
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    • 2001
  • 최소 배지와 MRS 배지에 여러 퓨린 뉴클레오시드을 첨가하여 각각 호기적과 혐기적 조건하에서 배양시킨 Serratia marcescens ATCC 25419와 Lactobacillus plantarum ATCC 8014 세포 추출물에서 PNP의 비활성도를 조사한 결과 이노신은 5 mM 이상의 농도에서 Serratia PNP의 비활성도를 대조군과 비교하여 30% 정도 감소시켰으나, Lactobacillus PNP의 비활성도를 60% 이상 증가시켰다. 히포잔틴은 $0.1{\sim}0.5\;mM$의 낮은 농도에서는 Serratia PNP의 비활성도에 거의 영향을 주지 않았으나, 5 mM 이상의 농도에서는 45% 정도를 감소시켰다. 하지만 히포잔틴은 $0.1{\sim}1\;mM$의 낮은 농도에서는 Lactobacillus PNP의 비활성도를 20%, $1{\sim}15\;mM$의 농도에서는 $50{\sim}65%$ 정도 증가시켰다. 한편, 요산은 0.5 mM의 농도에서 Serratia와 Lactobacillus PNP의 비활성도를 20% 정도 증가시킨 반면, $5{\sim}10\;mM$의 농도에서 $20{\sim}25%$ 정도, 그리고 15 mM의 농도에서는 $60{\sim}80%$ 감소시켰다. 이러한 결과들로부터 5 mM 이상 농도의 이노신과 히포잔틴은 Serratia PNP의 비활성도를 30%이상 감소시킨 반면, Lactobacillus PNP의 비활성도를 60% 이상 증가시켰으며 낮은 농도(0.5 mM)의 요산은 효소의 비활성도를 증가시키고 높은 농도(15 mM)의 요산은 감소시키는 등 퓨린 뉴클레오티드 분해 대사 과정에서 요산은 Serratia marcescens와 Lactobacillus plantarum PNP 생합성의 조절 역할을 하는 것으로 사료된다.

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Streptomyces tubercidicus에서 Adenine과 Histidine에 의한 Tubercidin 생합성 조절 (Regulation of Tubercidin Biosynthesis in Streptomyces tubercidicus by Adenine and Histidine)

  • 유진철;하영칠
    • 미생물학회지
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    • 제29권3호
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    • pp.160-166
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    • 1991
  • The regulatory mechanism of tubercidin biosynthesis in Streptomyces tubercidicus was studied. In a wild type strain, addition of adenine and histidine into the medium decreased the tubercidin production by 60-65% and 40%, respectively. The effects of adenine and histidine were alleviated by the addition of inosine monophosphate and 5-aminoimidazole-4-carboxamide ribotide. The production of tubercidin in S. tubercidicus K115 strain ($ade^{-}$ ) was nearly shut off by histidine. In contrast with K115 strain, adenine inhibited the tubercidin biosynthesis in S. tubercidicus K412 strain ($his^{-}$. In S. tubercidicus F667 strain ($ade^{-}$ , $his^{-}$ ), tubercidin production was increased by adenine and histidine. From the effects of adenine and histidine on tubercidin biosynthesis in S. tubercidicus wild type and mutant strains, it became known that feedback control by adenine and histidine of biosynthetic pathwat for purine ribonucleotide and histidine are involved in the regulation of tubercidin biosynthesis.

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Synthesis of 1,2,3-and 1,2,4-Triazole Isonucleosides as Potential antiviral agents

  • Jeong, Soon-Yong;Kim, Myong-Jung;Chun, Moon-Won
    • 대한약학회:학술대회논문집
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    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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    • pp.181.2-181.2
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    • 2003
  • Inosine monophosphate dehydrogenase(IMPDH) catalyzes the $NAD^+$-dependent oxidation of IMP to XMP, the rate limiting step in the de novo biosynthesis of guanine nucleotide. Its critical role at the metabolic branch point in purine nucleotide biosynthesis makes it a useful target in the development of drugs for antiviral and anticancer chemotherapy and in immunosupressant area. Several compound with antiviral activity have been found to be inhibitors of IMPDH. For example, ribavirin, a competitive inhibitor of IMPDH, has broad spectrum antiviral activities against DNA and RNA viruses. (omitted)

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진균류의 DNA 생합성 및 염기조성에 미치는 항생물질의 효과 (The Effect of Antibiotics on the DNA Synthesis and Base Composition in Fungal Cells)

  • 박규연;이종삼
    • 한국균학회지
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    • 제22권4호
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    • pp.366-377
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    • 1994
  • Cycloheximide와 nalidixic acid를 각각 처리한 배지에 Aspergillus phoenicis, Rhizopus acidus, Candida albicans를 배양하는 동안에 이들 세포에서 항생물질이 DNA 합성에 어떠한 영향을 미치는 가를 대조구와 비교 분석하였다. Cycloheximide 처리구에서의 DNA 염기 함량은 A. phoenicis에서 대조구에 비해 adenine 20.4%, thymine 43.1%, cytosine 40.9%, guanine 35.3%가 감소되어 purine기, pyrimidine기가 각각 32.2%, 42.7% 억제 현상을 나타내었다. R. acidus에서는 adenine이 34.2%, thymine이 42.1%, cytosine은 38.0%, guanine은 18.1%가 감소됨으로 purine기와 pyrimidine기가 24.1%와 40.0%로 저해되었다. 그리고 C. albicans의 염기 조성은 adenine이 58.3%, thymine이 58.5%로 대조구에 비해 억제되었고 cytosine은 58.1%, guanine은 42.4%가 감소되어 purine기 46.8%, pyrimidine기 58.8%의 억제를 보여주었다. Nalidixic acid 처리구에서는 A. phoenicis에서 adenine 41.6%, thymine 47.1%, cytosine 59.3%, guanine 46.3%가 저해되어 purine기 45.6%, pyrimidine기 57.2%가 감소되었다. R. acidus에서의 염기함량은 adenine 59.1%, thymine 54.7%, cytosine 35.3%, guanine 37.4% 감소로 purine기 45.9%, pyrimidine기 44.9%가 대조구에 비해 억제 효과를 보여주었다. C. albicans에서는 adenine이 60.1%, thymine이 68.6%, cytosine이 60.7%, guanine이 40.0% 저해되어 purine기는 45.8%, pyrimidine기는 63.5% 감소현상을 보였다. 이들 3 균주의 DNA 생합성에서 purine기 보다는 pyrimidine기가 cycloheximide와 nalidixic acid에 의해 뚜렷한 저해 효과를 나타내는 것으로 조사되었다. 본 실험에서 cycloheximide보다는 nalidixic acid가 DNA 생합성에 현저한 억제작용을 하는 것으로 분석되었다.

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Corynebacterium ammoniagenes에서 purF 유전자의 조절 및 이에 특이적인 조절 단백질의 분리 (Regulation of Corynebacterium ammoniagenes purF and Isolation of purF-Specific Regulatory Proteins)

  • 이석명;김연희;이흥식
    • 미생물학회지
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    • 제45권3호
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    • pp.233-238
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    • 2009
  • Corynebacterium ammoniagenes의 purF 유전자의 발현을 purF의 프로모터 추정 부위에 cat 유전자를 융합시킨 transcriptional fusion 플라스미드를 제작하여 분석하였다. 유전자 purF는 adenine과 guanine에 의해 20~30%의 전사 저해효과를 나타내지만, hypoxanthine에는 저해를 받지 않는 것으로 나타났다. 또한 purF의 발현은 대수기중반에 최대에 달한 후 정체기 후반부까지 일정한 것으로 나타났다. 동시에, C. glutamicum에서 사용되는 강력한 프로모터인 $P_{180}$이 Escherichia coli의 $P_{tac}$보다 C. ammoniagenes에서 모든 성장 단계에서 40~50%의 향상된 프로모터 활성을 나타내었고 대수기 후반부에 최고 활성에 달해, C. ammoniagenes의 연구에도 활용 가능함을 확인하였다. DNA-affinity purification에 의해 C. ammoniagenes의 purF 프로모터에 결합하는 단백질로서 C. glutamicum의 Crp-family transcriptional regulator (NCgl0120)와 상동성이 높은 단백질을 검출하였다. 이 단백질은 크기가 40.1 kDa으로서 PAGE에서 관찰된 단백질 크기와 일치하였다. 이에 상응하는 C. ammoniagenes의 단백질은 400개의 아미노산으로 구성되어 있고, 42 kDa의 단백질을 만들며, pI는 4.9일 것으로 추정되었다. 이는 기존에 알려져 있는 E. coli 및 Bacillus subtilis의 PurR과 각각 14.1%, 15.8%의 아미노산 상동성을 보여, PurR과는 다른 종류의 단백질일 것으로 여겨진다.

Proteomic Analysis of Recombinant Saccharomyces cerevisiae upon Iron Deficiency Induced via Human H-Ferritin Production

  • Seo, Hyang-Yim;Chang, Yu-Jung;Chung, Yun-Jo;Kim, Kyung-Suk
    • Journal of Microbiology and Biotechnology
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    • 제18권8호
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    • pp.1368-1376
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    • 2008
  • In our previous study, the expression of active H-ferritins in Saccharomyces cerevisiae was found to reduce cell growth and reactive oxygen species (ROS) generation upon exposure to oxidative stress; such expression enhanced that of high-affinity iron transport genes (FET3 and FTR1). The results suggested that the recombinant cells expressing H-ferritins induced cytosolic iron depletion. The present study analyzes metabolic changes under these circumstances via proteomic methods. The YGH2 yeast strain expressing A-ferritin, the YGH2-KG (E62K and H65G) mutant strain, and the YGT control strain were used. Comparative proteomic analysis showed that the synthesis of 34 proteins was at least stimulated in YGH2, whereas the other 37 proteins were repressed. Among these, the 31 major protein spots were analyzed via nano-LC/MS/MS. The increased proteins included major heat-shock proteins and proteins related to endoplasmic reticulum-associated degradation (ERAD). On the other hand, the proteins involved with folate metabolism, purine and methionine biosynthesis, and translation were reduced. In addition, we analyzed the insoluble protein fractions and identified the fragments of Idh1p and Pgk1p, as well as several ribosomal assembly-related proteins. This suggests that intracellular iron depletion induces imperfect translation of proteins. Although the proteins identified above result from changes in iron metabolism (i.e., iron deficiency), definitive evidence for iron-related proteins remains insufficient. Nevertheless, this study is the first to present a molecular model for iron deficiency, and the results may provide valuable information on the regulatory network of iron metabolism.

Proteomic Analysis of Protein Expression in Streptococcus pneumoniae in Response to Temperature Shift

  • Lee Myoung-Ro;Bae Song-Mee;Kim Tong-Soo;Lee Kwang-Jun
    • Journal of Microbiology
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    • 제44권4호
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    • pp.375-382
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    • 2006
  • From its initial colonization to causation of disease, Streptococcus pneumoniae has evolved strategies to cope with a number of stressful in vivo environmental conditions. In order to analyze a global view of this organism's response to heat shock, we established a 2-D electrophoresis proteome map of the S. pneumoniae D39 soluble proteins under in vitro culture conditions and performed the comparative proteome analysis to a 37 to $42^{\circ}C$ temperature up-shift in S. pneumoniae. When the temperature of an exponentially growing S. pneumoniae D39 culture was raised to $42^{\circ}C$, the expression level of 25 proteins showed changes when compared to the control. Among these 25 proteins, 12 were identified by MALDI-TOF and LC-coupled ESI MS/MS. The identified proteins were shown to be involved in the general stress response, energy metabolism, nucleotide biosynthesis pathways, and purine metabolism. These results provide clues for understanding the mechanism of adaptation to heat shock by S. pneumoniae and may facilitate the assessment of a possible role for these proteins in the physiology and pathogenesis of this pathogen.