• Title/Summary/Keyword: Dehydrogenase

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Expression of Human Mitochondiral Aldehyde Dehydrogenase 2 in Mammalian Cells using Vaccinia Virus-T7 RNA Polymerase

  • Kang, Su-Min;Yoo, Seung-Ku;Lee, Ki-Hwan
    • Journal of Microbiology
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    • v.37 no.1
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    • pp.41-44
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    • 1999
  • Human mitochondrial aldehyde dehydrogenase 2 (ALDH2) is mainly responsible for oxidation of acetaldehyde generated during alcohol oxidation in vivo. A full-length cDNA of human liver ALDH2 was successfully expressed using a vaccinia virus-T7 RNA polymerase system. The expressed ALDH2 had an enzymatic activity as high as the native human liver ALDH2 enzyme.

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Nucleotide Sequencing Analysis of a Gene Coding for 3-Isopropylmalate Dehydrogenase of Kluyveromyces fragilis

  • Hong, Soon-Duck;Kim, Jong-Guk;Lee, Dong-Sun;Woo, Ju-Hyung;Lee, Sang-Yong
    • Journal of Microbiology and Biotechnology
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    • v.3 no.2
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    • pp.91-94
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    • 1993
  • A 3-isopropylmalate dehydrogenase (3-IPMD) gene was cloned from Kluyveromyces fragilis. pJK104 could complement Escherichia coli leuB and Saccharomyces cerevisiae leu2 auxotrophs. The coding region was subcloned and the nucleotide sequence was determined. A 1.8 Kb EcoRI/SphI fragment of pJK104 subcloned in pUC18 could still complement the leuB mutation. An open reading frame of 1164 bp that corresponds to a polypeptide of 387 amino acids was found in the cloned fragment. The homology between the 3-isopropylmalate dehydrogenase of S. cerevisiae and that of K. fragilis was 68.13% in nucleotides.

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Genetic Divergence between Two Marine Catfish of Family Ariidae - Arius maculatus and Osteogeneiosus militaris

  • Chaudhari, Aparna;Alam, Afaque
    • Asian-Australasian Journal of Animal Sciences
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    • v.17 no.9
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    • pp.1188-1191
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    • 2004
  • Two species of marine catfish, Arius maculatus and Osteogeneiosus militaris, belonging to family Ariidae were analysed electrophoretically for genetic variation in 6 enzymes, alcohol dehydrogenase (ADH), malate dehydrogenase (MDH), lactate dehydrogenase (LDH), glucose dehydrogenase (GDH), malic enzyme (ME) and superoxide dismutase (SOD). Eighteen individuals of each species were studied. Two loci MDH and ADH were polymorphic in both. Average heterozygosity in A. maculatus was 1.46, while it was 2.5 in O. militaris. The allele frequencies were used to estimate Nei's genetic distance (D). The D value was calculated to be 0.6879. Two isozyme loci, ME and SOD, were found to be the most reliable species specific markers. No tissue specific loci were observed for the enzymes studied, the bands being identical in each case. The genetic distance observed between O. militaris and A. maculatus in this study suggests that they would be more appropriately classified as species of the same genus rather than being assigned separate genera.

Inhibitory Activities of Three Compounds from Mucuna birdwoodiana on $3{\alpha}-Hydroxysteroid\;dehydrogenase$ (계혈등(Mucuna birdwoodiana)의 $3{\alpha}-Hydroxysteroid\;dehydrogenase$억제 성분)

  • Kwon, Yong-Soo;Lee, Jin-Hun;Kim, Chang-Min
    • Korean Journal of Pharmacognosy
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    • v.30 no.2
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    • pp.216-221
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    • 1999
  • The NAD(P)-linked $3{\alpha}-Hydroxysteroid$ $dehydrogenase(3{\alpha}-HSD)$ of rat liver cytosol is powerfully inhibited by the non-steroidal anti-inflammatory drugs in rank-order of their therapeutic potency, and this observation has now been developed into a rapid screen for predicting the potency of products that show anti-inflammatory effect. Five-plants were screened by using this method. Among them, BuOH-fraction of Mucuna birdwoodiana showed strong inhibitory effect on $3{\alpha}-HSD$, and three isoflavone compounds were isolated. Inhibitory activates of isolated compounds were compared.

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Effect of simazine on nitrogen assimilation of rhodopseudomonas sphaeroides (Rhodopseudomonas sphaeroides의 질소 동화작용에 미치는 simazine의 영향)

  • 이혜주;이진애;박인호;선우양일
    • Korean Journal of Microbiology
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    • v.27 no.3
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    • pp.304-309
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    • 1989
  • The effects of simazine [2-chloro-4, 6-bis(methylamino)-s-triazine] on in vivo nitrogenase, glutamine synthetase, glutamate synthase, and glutamate dehydrogenase which are important in nitrogen assimilation of Rhodopseudomonas sphaeroides were investigated. Simazine inhibited the synthesis of nitrogenase and glutamine synthetase. The activity of glutamine synthetase in crude extracts of Rhodopseudomonas sphaeroides is less inhibited by simazine than that of glutamate synthase and glutamate dehydrogenase. These results suggest the possibility that simazine inhibits photosynthetic activity and so inhibits the synthesis of nitrogenase and glutamine synthetase in Rhodopseudomonas sphaeroides.

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Effects of Ginseng Saponins on Morphine 6-Dehydrogenase

  • 김학성;정인숙;이명구;오기완
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1994.04a
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    • pp.304-304
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    • 1994
  • The possible mechanisms of ginseng saponins on the inhibition of development of morphine tolerance and physical dependence were investigated in the aspects of morphine metabolism by morphine 6-dehydrogenase. Administration of morphine causes a reduction of non-protein sulfhydryl contents in liver, because morphinone is metabolized from morphine by morphine 6-dehydrogenase conjugates with sulfhydryl compounds. However, ginseng saponins inhibited the activity of morphine 6-dehydrogenase which catalized the production of morphinone from morphine. In addition, ginseng' saponins inhibited the reduction of non-protein sulfhydryl levels by Increasing the level of hepatic glutathione. These results suggest that the dual action of the above plays an important role in the inhibition of development of morphine tolerance and physical dependence. On the other hand, it was observed that less polar components of ginseng saponins with parent structures were more active components in vitro.

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Ethanol이 allyl alcohol 독성에 미치는 영향

  • 이주영;정진호
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1994.04a
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    • pp.323-323
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    • 1994
  • Allyl alcohol은 간에서 두 단계의 효소 반응을 거쳐 대사되는데, 먼저, alcohol dehydrogenase (ADH)에 의해 독성 활성체인 acrolein으로 바뀌고, 이후 계속하여 aldehyde dehydrogenase (ALDH)에 의해 acrylic acid로 무독화되어 배설된다. Ethanol 역시 간에서 대사되는데 있어 같은 효소들을 공유하므로 allyl alcohol과 경쟁적으로 반응할 것이다. 따라서, 본 실험에서는 ethanol에 의한 대사 효소 경쟁반응에 의해 allyl alcohol 의 간독성이 어떻게 변화하는지를 연구하였다. 우선 ethanol과 allyl alcohol을 동시 투여할 경우 5시간째에 allyl alcohol에 의해 증가된 ALT level을 낮춘다는 보고를 확인하고자 ethanol 2 g/kg과 allyl alcohol 40 mg/kg을 동시투여했으나 오히려 치사율이 증가했고, ethanol을 2시간 전처리한 군에서도 역시 치사율이 증가되고, 간의 glutathione 양은 allyl alcohol 단독 처리군에 비해 현저히 감소되는 양상을 보였다.

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Degradation of Polyvinyl Alcohol by Brevibacillus laterosporus: metabolic Pathway of Polyvinyl Alcohol to Acetate

  • Lim, Joong-Gyu;Park, Doo-Hyun
    • Journal of Microbiology and Biotechnology
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    • v.11 no.6
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    • pp.928-933
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    • 2001
  • Approximately 0.1 mg/ml of polyvinyl alcohol (PVA) was degraded by the growing cell, Brevibacillus laterospours, for 30 h, and 0.2 mg/ml of PVA was degraded by the cell-free extract that was isolated from Brevibacillus laterosporus. Approximately $0.29{\mu}g$/ml of acetic acid was produced from PVA by using the cell-free extract as a catalyst for 40 min. $V_{max}\;and\;K_m$ value of purified PAV-degradation enzyme was 3.75g/l and 2.75 g/l/min in reaction with EDTA and 3.99 g/l and 2.98 g/l/min in reaction without EDTA, respectively. Molecular weight of the purified enzyme determined by SDS-PAGE was 63,000 Da. Alcohol dehydrogenase and aldehyde dehydrogenase activities were qualitatively detected on a native acrylamide gel by an active staining method, indicating the existence of the metabolic pathway to use PVA as a substrate.

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Purification and Characterization of Trypsin Inhibitor from Alismatis Rhizoma and its Binding Protein, 10-Formyltetrahydrofolate Dehydrogenase (택사(Alismatis Rhizoma)로부터 트립신 저해제의 정제와 특성 규명 및 이와 결합하는 단백질, 10-Formyltetrahydrofolate Dehydrogenase에 관한 연구)

  • Kim, Ji-Man;Park, Jong-Ok;Shin, Young-Hee
    • YAKHAK HOEJI
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    • v.52 no.1
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    • pp.79-84
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    • 2008
  • Alismatis Rhizoma has been used as diuretics and antiphlogistics in the Chinese oriental medicine. A trypsin inhibitor was isolated from Alismatis Rhizoma using DEAE ion exchange column, trypsin affinity column, and FPLC chromatography, and its activity and characteristics were studied. The purifed Alismatis Rhizoma trypsin inhibitor (ARTI) was estimated to be about 22 kDa. The sequence determination on N-terminal amino acid residues and 84 amino acid residues has been completed, yet no homology has been found with trypsin inhibitors reported at NCBI. ARTI did not show inhibitory activities on chymotrypsin and elastase, however it exhibited a significant inhibitory activity on bovine trypsin, and formed a complex with rat liver 10-formyltetrahydrofolate dehydrogenase.

Effect of Ethanol on Allyl alcohol-Induced Toxicity (Ethanol이 Allyl alcohol 독성에 미치는 영향)

  • Lee, Joo-Young;Kim, Dae-Byung;Moon, Chang-Kiu;Chung, Jin-Ho
    • YAKHAK HOEJI
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    • v.38 no.2
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    • pp.107-113
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    • 1994
  • Ally alcohol is metabolized in the liver through two steps, first to reactive acrolein by alcohol dehydrogenase(ADH), subsequently to acrylic acid by aldehyde dehydrogenase(ALDH). Since ethanol could compete the same enzymes to be metabolized in the liver, we have studied the interaction between allyl alcohol and ethanol on liver toxicity. Simultaneous treatment of 2 g/kg ethanol by ip administration with 40 mg/kg allyl alcohol to rats increased the lethality significantly, accompanied by potentiation of the loss of hepatic glutathione. Collectively, these findings suggested that ethanol potentiated the hepatotoxicity and lethality induced by allyl alcohol probably through competing two metabolizing enzymes, ADH and ALDH.

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