• YAKHAK HOEJI
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• v.21 no.2
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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.

• The Korean Journal of Food And Nutrition
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• v.12 no.1
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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.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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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.

• Korean Journal of Food Science and Technology
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• v.33 no.3
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• pp.361-365
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• 2001

The effects of purine catabolites in growth media on the biosynthesis of Serratia marcescens and Lactobacillus plantarum purine nucleoside phosphorylase (PNP) activity were examined. Serratia PNP activity was decreased approximately by 30% in the presence of high concentrations of inosine $(5{\sim}15\;mM)$, but was not affected at low concentrations of inosine $(0.1{\sim}1\;mM)$. However, Lactobacillus PNP activity was increased above 60% by inosine among the range from 5 to 15 mM. Serratia PNP activity was decreased approximately by 45% in the presence of high concentrations of hypoxanthine $(5{\sim}15\;mM)$, but was not affected at low concentrations of hypoxanthine $(0.1{\sim}0.5\;mM)$. Lactobacillus PNP activity was increased approximately by 20% in the presence of low concentrations of hypoxanthine $(0.1{\sim}0.5\;mM)$, and increased approximately by $50{\sim}65%$ in the presence of concentrations of hypoxanthine $(1{\sim}15\;mM)$. Serratia and Lactobacillus PNP activity was increased 20% by low concentrations of uric acid (0.5 mM), but was decreased $40{\sim}80%$ at high concentrations of same purine catabolite $(10{\sim}15\;mM)$. These data suggest that purine nucleoside phosphorylase in Serratia marcescens ATCC 25419 and Lactobacillus plantarum ATCC 8014 is positively regulated by a low uric acid concentration, and then may play a regulatory role in a purine nucleotide catabolic pathway.

• Korean Journal of Microbiology
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• v.29 no.3
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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.

• Proceedings of the PSK Conference
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• 2003.10b
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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)

• The Korean Journal of Mycology
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• v.22 no.4
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• pp.366-377
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• 1994

The base composition of DNA of Aspergillus phoenicis, Rhizopus acidus and Candida albicans treated with cycloheximide and nalidixic acid during the culture was analyzed to compare with the control. The contents of base in the DNA were inhibited by cycloheximide, 20.4% of adenine, 43.1% of thymine, 40.9% of cytosine, 35.3% of guanine, 32.2% of purine, and 42.7% of pyrimidine for A. phoenicis. In R. acidus, 34.2% of adenine, 42.1% of thymine, 38.0% of cytosine, 18.1% of guanine, 24.1% of purine and 40.0% of pyrimidine were depressed by cycloheximide. In the antibiotic treatment of C. albicans, 58.3% of adenine, 58.5% of thymine, 58.1% of cytosine, 42.4% of guanine, 46.8% of purine and 58.8% of pyrimidine were inhibited to compare with the control. The nalidixic acid treatments were showed that, in A. phoenicis 41.6% of adenine, 47.1% of thymine, 59.3% of cytosine, 46.3% of guanine, 45.6% of purine and 57.2% of pyrimidine were inhibited. When R. acidus was treated with nalidixic acid, 59.1% of adenine, 54.7% of thymine, 35.3% of cytosine, 37.4% of guanine, 45.9% of purine and 44.9% of pyrimidine decreased. In treatment of nalidixic acid, the content of DNA was depressed 60.1% of adenine, 68.6% of thymine, 60.7% of cytosine, 40.0% of guanine, 45.8% of purine and 63.5% of pyrimidine for C. albicans In the DNA synthesis of three fungal cells, cycloheximide and nalidixic acid treatments were analyzed obviously that the biosynthesis of pyrimidine was depressed than that of purine. Therefore, it was showed that the DNA contents in the various fungal cells were inhibited remarkably in nalidixic acid treatment than cycloheximide.

• Korean Journal of Microbiology
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• v.45 no.3
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• pp.233-238
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• 2009

The expression of Corynebacterium ammoniagenes purF was analyzed by utilizing a plasmid carrying a cat gene fused to the purF promoter region. Adenine and guanine repressed the expression of the purF gene by 20~30% but hypoxanthine did not exert such repressive effect. The expression purF was maximal at the late log phase and remained constant throughout the stationary phase. Promoter $P_{180}$ which was developed in C. glutamicum was also functional in C. ammoniagenes, achieving maximal activity at the late log phase. The promoter outperformed Escherichia coli $P_{tac}$ promoter by 40~50% level. DNA-affinity purification identified a protein which could bind to the promoter region of the purF gene. The protein showed high similarity to the CRP-family transcriptional regulator encoded by NCgl0120 in C. glutamicum. The size of the screened protein agreed with the expected protein size from the ORF NCgl0120. The corresponding gene in C. ammoniagenes encoded a 42 kDa polypeptide composed of 400 amino acids with expected pI of 4.9. The encoded protein showed 14.1% and 15.8% identity with E. coli and Bacillus subtilis PurR, respectively, suggesting that the isolated protein might be a novel type of regulatory protein involved in the regulation of purine metabolism.

• Journal of Microbiology and Biotechnology
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• v.18 no.8
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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.

• Journal of Microbiology
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• v.44 no.4
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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.