• Journal of Life Science
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• v.9 no.2
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• pp.9-14
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• 1999

Pseudomonas iodinum IFO 3558 adenosine deaminase(ADA) gene was cloned by the polymerase chain reaction and deduced the amino acid sequence of the enzyme. DNA sequence homology of Pseudomonas iodinum IFO 3558 ADA gene was compared to those of E. coli, human and mouse ADA genes. Unambiguous sequence from both strands of pM21 was obtained for the region believed to encode ADA. The sequence included a 804-nucleotide open reading frame, bounded on one end by sense primer and on the other end by two antisense primer. This open reading frame encodes a protein of 268 amino acids having a molecular weight of 29,448. The deduced amino acid sequence shows considerable similarity to those of E. coli, mouse and human ADA. Pseudomonas iodinum IFO 3558 nucleotide sequence shows 98.5% homology with that of the E. coli ADA sequence and 51.7% homology with that of the mouse ADA sequence and 52.5% homology with that of the human ADA sequence. The ADA protein sequence of Pseudomonas iodinum IFO 3558 shows 96.9% homology with that of the E. coli and 40.7% homology with that of the mouse and 41.8% homology with that of the human. The distance between two of the conserved elements, TVHAGE and SL(1)NTDDP has veen exactly conserved at 76 amino acids for all four ADAs. Two of the four conserved sequence elements shared among the four ADAs are also present in the yeast, rat, human (M), and Human(L) AMP deaminase. The SLSTDDP sequence differs only in the conservative substitution of a serine for an asparagine. A conserved cysteine with conserved spacing between these two regions is also found. Thus, sequence analysis of four ADAs and four AMP deaminases revealed the presence of a highly conserved sequence motif, SLN(S)TDDP, a conserved dipeptide, HA, and a conserved cysteine residue.

• Proceedings of the Zoological Society Korea Conference
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• 1994.10a
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• pp.215.1-215
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• 1994

No Abstract, See Full Text

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.280.1-280
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• 1995

No Abstract, See Full Text

• Proceedings of the Plant Resources Society of Korea Conference
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• 1998.03a
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• pp.8-8
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• 1998

• Proceedings of the Botanical Society of Korea Conference
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• 1994.07a
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• pp.141-176
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• 1994

• Proceedings of the Korean Society of Applied Pharmacology
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• 1994.04a
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• pp.268-268
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• 1994

포자의 전자현미경사진과 mycelium의 광학현미경사진을 찍어 strain V-8 균주의 형태학적인 특성을 조사하였을 때 방선균 계열인 streptomyces로 확인되었다. 이 균주의 배양액은 노란색을 띠고 있고 이 노란색은 430 nm에서 특징적인 흡광을 보였다. 이 물질은 유기 용매로 추출되었다. 이 물질의 자외선 흡광스펙트럼의 특징을 기존에 보고된 화합물과 비교하여 이 물질이 actinomycin계열에 속함을 발견하였다. 이 물질의 FAB mass spectrum에서 각 분획들의 주성분들의 분자의 질량 + H 이온이 1290과 1292에서 각각 관찰되었다. 이 화합물들은 분자량이 1258인 actinomycin D와는 상이한 구조를 소유하고 있는 것으로 확인되었다. 각 분획 성분들의 proton 및 carbon HIR spectra를 얻어 기존에 알려진 화합물의 자료와 비교하였을 때 actinomycin계열에 속하는 신물질로 생각되었다. 지금까지 actinomycin 계열의 항생물질이 adenosine deaminase의 효소 활성을 저해한다는 사실은 보고된바 없다. 본 연구자는 분리한 2개의 화합물에 대하여 구조 연구를 계속하고 있다.

• Bulletin of the Korean Chemical Society
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• v.32 no.9
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• pp.3411-3420
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• 2011

Kinetic and structural studies have been carried out on the effects of meso-tetrakis(4-sulfonatophenyl)-porphyrin ($H_2TPPS_4$) as an anionic and meso-tetrakis(3-N-methyl-pyridyl)porphyrin ($H_2TMPYP$) as a cationic porphyrin with adenosine deaminase (ADA) in 25 mM citrate/phosphate buffer, pH = 4-8, at $37^{\circ}C$ using UVvis spectrophotometry, circular dichroism (CD), fluorescence spectrophotometry as well as molecular dynamics (MD) and molecular docking. Kinetic results showed that the two porphyrins are non-competitive inhibitors. Increasing pH, increases $K_I$ and cationic porphyrin has a higher $K_I$ and lower binding constant ($K_b$) at all pH ranges. Analyzing the secondary structure revealed that both ligands decrease the secondary structure and that the anionic porphyrin is more effective.

• Proceedings of the KTCVS Conference
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• 1998.10a
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• pp.139-139
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• 1998

• Microbiology and Biotechnology Letters
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• v.15 no.5
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• pp.306-311
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• 1987

After series of purification by means of ammonium sulfate fractionation, the 1st and 2nd DEAE-Cellulose, DEAE-Sephadex A-50, and Sephacryl S-200 superfine gel filtration, the activity of extracellular adenine deaminase from Streptomyces sp. J-350P increased 1764 fold and the yield was 0.3% of original activity. The enzyme was stable at the pH range 6.5 to 8.5 and at up to 5$0^{\circ}C$. The optimum pH and temperature of the enzyme were around 6.5 and 35$^{\circ}C$. The molecular weight ol the enzyme was estimated as 36, 000 by calibrated Sephacryl S-200 superfine column chromatography.

• Horticultural Science & Technology
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• v.17 no.6
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• pp.770-772
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• 1999

This study was conducted to provide a basic system to develop a molecular marker for plant cultivar protection using a recombinant DNA technology. Using Nicotiana tabacum L. plants, the potentiality in the utilization of the developed marker was examined. After homology test with several plant genomes, mouse adenosine deaminase (ADA) gene was selected as DNA source of a molecular marker for cultivar protection. As a result of the digestion of ADA gene with BamHI and Pst I, six DNA fragments were obtained, and 513 bp DNA fragment among them was selected as a possible DNA marker for cultivar protection. Selected 513 bp DNA fragment was efficiently inserted into pBI101 plasmid vector for plant transformation by using phagemid vector pBluescript II SK (+/-) as an intermediate vector. The recombinant pBI101, carrying 513 bp DNA fragment, possible markers for cultivar protection, was transformed into A. tumefaciens LBA4404. Nicotiana tabacum was transformed with A. tumefaciens LBA4404 having the recombinant pBI101 and was confirmed the transfer of 513 bp DNA fragment, a possible molecular marker for cultivar protection.