• 제목/요약/키워드: deamination

검색결과 49건 처리시간 0.024초

Presence of an Inducible Semicarbazide-Sensitive Amine Oxidase in Mycobacterium sp. Strain JC1 DSM 3803 Grown on Benzylamine

  • Ro Young-Tae;Lee Hyun-Il;Kim Young-Min
    • Journal of Microbiology
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    • 제44권2호
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    • pp.243-247
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    • 2006
  • Mycobacterium sp. strain JC1 was capable of growth on benzylamine as a sole source of carbon and energy. The primary deamination of benzylamine was mediated by an inducible amine oxidase, which can also oxidize tyramine, histamine, and dopamine. Inhibitor study identified this enzyme as a copper-containing amine oxidase sensitive to semicarbazide.

N,N-디아실, O-아실 키토산 올리고머의 물리화학적 특성에 관한 연구 (Study of Physico-Chemical Properties of N,N-Diacyl, O-Acyl Chitosan Oligomer)

  • 이옥섭;하병조;김준오;박성규;이윤식
    • 공업화학
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    • 제8권3호
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    • pp.365-373
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    • 1997
  • 천연 고분자인 키토산의 1차 아민기를 아질산 나트륨에 의해 oxidative-deamination 반응을 일으켜 reducing end에 알데히드기를 갖는 키토산 올리고머를 얻었으며, 이를 수소화붕소산나트륨으로 환원하여 2,5-anhydro-D-mannitol로 전환하였다. 얻어진 피토산 올리고머의 평균 중합도는 겔 투과 크로마토그래피를 통해 2정도임을 알 수 있었고, 키토산에 비해 친유성 유기 용매에 대한 높은 용해성을 나타내었다. 키토산 올리고머에 아실클로라이드를 4-디메틸아미노피리딘 촉매하에서 반응시켜 N,N-디아실, O-아실 키토산 올리고머를 합성하였다. 시차주사열량 분석을 실시한 결과 N,N-디라우로일, O-라우로일 키토산 올리고머의 경우 액정 영역을 나타내었고, 편광현미경을 통해 이를 확인할 수 있었다. X-선 회절분석 실험결과 키토산 올리고머와 달리 N,N-디라우로일, O-라우로일 키토산 올리고머는 높은 결정성 구조를 나타냄을 알 수 있었다.

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키토산 올리고당의 보습성과 생리활성에 관한 연구 (Moisturizing Property and Physiological Activity of Chitosan Oligosaccharide)

  • 하병조;이옥섭
    • 대한화장품학회지
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    • 제25권1호
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    • pp.6-22
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    • 1999
  • 천연고분자인 키틴으로부터 저분자 키토산을 얻은 후 이를 아질산을 이용한 분해반응에 의해 세포증식효과 및 상처치유효과 등의 생리적인 효과가 있는 키토산 올리고당을 합성하였다 이를 위해 아질산을 이용하여 deamination한 후, sodium borohydride로 환원시켜 reducing-end residue들을 alditol unit로 치환하였으며 MBTH시약을 사용하여 반응이 진행하였음을 확인하였다. 얻어진 키토산 올리고 당의 분자량 분포를 HPLC로 확인한 결과 중합도가 2∼6 인 올리고당이 얻어졌음 을 알 수 있었다. 상대습도 43%와 81%에서 측정한 흡습력 실험결과, 글리세린 에 대해 각각 63%, 57%의 흡습력을 보였으며, 상대습도 43%와 실리카겔 분위기 하의 보습력 측정결과, 각각 98%, 91%의 수분잔존률을 나타내었다 키토산 올리고당은 0,000032∼0.01% 농도 범위에서 세포증식효과를 보였으며, 2%와 20%로 처리한 경우 상처치유효과를 나타내었다.

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Fluorescent Probes for Analysis and Imaging of Monoamine Oxidase Activity

  • Kim, Dokyoung;Jun, Yong Woong;Ahn, Kyo Han
    • Bulletin of the Korean Chemical Society
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    • 제35권5호
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    • pp.1269-1274
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    • 2014
  • Monoamine oxidases catalyze the oxidative deamination of dietary amines and amine neurotransmitters, and assist in maintaining the homeostasis of the amine neurotransmitters in the brain. Dysfunctions of these enzymes can cause neurological and behavioral disorders including Parkinson's and Alzheimer's diseases. To understand their physiological roles, efficient assay methods for monoamine oxidases are essential. Reviewed in this Perspective are the recent progress in the development of fluorescent probes for monoamine oxidases and their applications to enzyme assays in cells and tissues. It is evident that still there is strong need for a fluorescent probe with desirable substrate selectivity and photophysical properties to challenge the much unsolved issues associated with the enzymes and the diseases.

Isolation of the Threonine Dehydratase Gene from a Tylosin-Producing Strain of Streptomyces fradiae

  • Lee, Sang Hee;Kye Joon Lee
    • Journal of Microbiology and Biotechnology
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    • 제5권5호
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    • pp.305-308
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    • 1995
  • From the plasmid library made from Sstl and San-digested genomic DNA of Streptomyces fradiae NRRL 2702, four positive clones were selected using an oligodeoxynucleotide probe from the N-terminal amino acid sequence of purified threonine dehydratase. The cloned gene for threonine dehydratase was a 2.0 kilo-base pair DNA fragment. The deduced amino acid sequence of PCR product (PCR245) was matched to that of the N-terminal part of threonine dehydratase from S. fradiae and this showed a high similarity to the threonine dehydratases of other organisms. This indicated that amino acid sequences of threonine dehydratases were highly conserved and the polypeptide product of the PCR245 was likely to be involved in the deamination of threonine.

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비타민 C가 가용성 콜라겐의 성숙과정에서 Pyridinoline 생성 효소계에 미치는 영향 (The Effect of Ascorbic Acid on the Enzyme Reaction in Pyridinoline Formation during Soluble Collagen Maturation)

  • 김미향
    • 한국식품영양과학회지
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    • 제27권2호
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    • pp.305-312
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    • 1998
  • Normal tensile strength in collagen fibrils is due to intermolecular and intramolecular crosslinks which are known to be altered in aging. Pyridinoline, a mature crosslink which is stable and nonreducible, is derived from two hydroxyallysine and one hydroxylysine residues of collagen fibrils. The excess formation of pyridinoline in collagen is associated with making the tissue stiffer, less soluble and less digestible by enzymes. Lysyl oxidase is the enzyme that initiates the biosynthesis or crosslinks in collagen by catalyzing the oxidative deamination of the lysyl and hydroxylysyl residues in these molecules, and its activity is inhibited by $\beta$-aminopropionitrile(BAPN). Our previous work demonstrated that the pyridinoline content of bone collagen significantly was increased during incubation for 5 weeks at 37$^{\circ}C$ invitro, but it was diecrased by the addition of ascorbic acdi(AsA). In this study, we clarified the specific action of AsA in aging process in vitro enzymatic reaction.

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Kinetic Studies of Aspartase from Hafnia alvei byTemperature Dependence Activity Changes

  • 윤문영
    • Bulletin of the Korean Chemical Society
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    • 제21권4호
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    • pp.379-382
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    • 2000
  • The temperature dependence of the kinetic parameters of the aspartase-catalyzed reaction has been examined in the direction of deamination. The pK1values at 37$^{\circ}C$, 25$^{\circ}C$, 16$^{\circ}C$ and 7$^{\circ}C$ were 6.2 $\pm$ 0.1, 6.3 $\pm$ 0.1, $6.7{\pm}0.3$ and 6.9 $\pm$ 0.3, respectively. On the other hand, the pK2 values at 37$^{\circ}C$,25$^{\circ}C$, 16$^{\circ}C$ and 7$^{\circ}C$ were 8.1 $\pm0.2$, 8.3 $\pm$ 0.2, 8.2 $\pm$ 0.3 and 8.0 $\pm$ 0.2,respectively. The enthalpy of ionization, DHion, calculated from the slope of pK1, are 6.0 $\pm$ 0.3 kcal/mol. These results validate the prediction that aspartase requires a histidine residue for a general base, and a cysteine (or having a carboxyl functional group) for a general acid.

Delftia acidovorans로부터 Aniline 분해관련 유전자의 분리 (Cloning Genes Involved in Aniline Degradation from Delftia acidovorans.)

  • 김현주;김성은;김정건;김진철;최경자;김흥태;황인규;김홍기;조광연
    • 한국미생물·생명공학회지
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    • 제31권1호
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    • pp.25-31
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    • 2003
  • 아닐린을 분해할 수 있는 Deiftia acidovoran 51-A가 기존에 분리되어 아닐린 분해능이 우수함이 보고되었다. 이 균주로부터 아닐린 분해관련 유전자를 선발하기 위하여 Tn5-B20삽입 변이체들을 유도하여 영양요구형이 아니면서 아닐린을 분해할 수 없는 변이균주 D. acidovorans 10-4-2 균주를 선발하였다. Southern hybridization 결과 이 변이균주에는 Tn5-B20이 한 copy만 삽입된 것으로 나타났다 이 변이균주의 Tn5-B20삽입의 인접 유전자들을 분리하여 염기서열을 분석한 결과 아닐린 분해의 첫 단계에 해당하는 아닐린의 catechol로의 산화적 deamination에 관련되어 있는 것으로 추정하는 tdnQ, tdnT tdnAl 유전자들이 동정되었고 Tn5-B2O은 tdnAl의 바로 밑에 삽입된 것을 알 수 있었다. TdnA2 및 downstream의 유전자 기능을 상실하여 아닐린을 catechol로 전환하는 과정에 변이가 발생하고 따라서 아닐린을 탄소원으로 이용하지 못하는 표현형을 가지게 된 것으로 결론지을 수 있었다. Tn5-B20 의 일부 DNA 조각을 probe로 Southern hybridization 결과 transposon 삽입이 대형의 플라스미드에 삽입된 것으로 나타나 tdn 유전자들이 pTDN51이라고 명명한 100-kb 이상의 대형 플라스미드에 위치함을 알 수 있었다. 이상의 결과는 D. acidovorans 51-A의 pTDN51상의 tdn유전자들이 아닐린의 분해에 관여함을 보여준다.

Production and Characterization of Phenylalanine Ammonia-lyase from Rhodotorula aurantiaca K-505

  • Cho, Dae-Haeng;Chae, Hee-Jeong;Kim, Eui-Yong
    • Preventive Nutrition and Food Science
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    • 제2권4호
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    • pp.354-359
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    • 1997
  • Optimal cultivation conditions for the production of phenylalanine ammonia-lyase(PAL) from Rhodotorula aurantiaca K-505 were selected, and the kinetic parameters of the produced PAL were determined. The most suitable carbon and nitrogen sources were glucose and tryptone, respectively. The strain expressed PAL constituttively when using the optimized semi-complex media. High cell density culture could be critical for maximal production of PAl since the PAL ynthesis was growth associated. maximum PAL activity was observed at initial pH 6.0. although the ll growth was not markedly affected by temperature between 22 and 28$^{\circ}C$, the cells yielded the maximum PAL activity when cultivated at 22$^{\circ}C$. The maximum activity for deamination of L-phenylalnine to trans-cinnamic acid was observed around pH 8.8. The PAL activity gave the maximum at 45$^{\circ}C$, and greatly decreased at higher than 5$0^{\circ}C$. Activation energy({TEX}$E_{a}${/TEX}) calculated from Arrhenius equation was 6.28 kcal/mol in the range of 22$^{\circ}C$ to 4$0^{\circ}C$. A oolf plot showed that the enzyme reaction follows Michaelis-Menten equation, whose {TEX}$K_{M}${/TEX} and {TEX}$V_{max}${/TEX} values were 4.65$\times${TEX}$10^{-3}${/TEX} M and 0.89$\mu$ mol/mg-min respectively.

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