• Title/Summary/Keyword: CO dehydrogenase

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Effect of Allylisothiocyanate on the Enzyme Activities During the Culture of Aspergillus parasiticus R-716 (Allylisothiocyanate첨가가 Aspergillus parasiticus R-716의 배양중 효소활성에 미치는 영향)

  • 김성영
    • Journal of Food Hygiene and Safety
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    • v.12 no.2
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    • pp.97-101
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    • 1997
  • Effect of allylisothiocyanate on the enzyme activites including malate degydrogenase, isocitrate dehydrogenase, NADPH and acetyl CoA which were related to aflatoxin production of Aspergillus parasticus R-716 were invetigated. The activities of malate dehydrogenase (EC.1.1.1.37), isocitrate dehydrogenase (E.C.1.1.1.42) and NADPH oxidase (E.C.1.6.99.1) indicated relatively high in the 50 ppm allylisothiocyanate-added-culture. In contrast, the activity of acetyl CoA in the 50 ppm allylisothiocyanate-added-culture showed rather lower level through the cultivation.

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Constitutive Expression of Carbon Monoxide Dehydrogenase in Acinetobacter sp. Strain JC1 DSM 3803 (Acinetobacter sp. Strain JC1 DSM 3803에 존재하는 일산화탄소 산화효소의 구성적 발현)

  • Ro, Young T.;Kim, Young M.
    • Korean Journal of Microbiology
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    • v.31 no.3
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    • pp.214-217
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    • 1993
  • Carbon monoxide dehydrogenase (CO-DH) was found to be present in Acinetobacter sp. strain JC1 grown on CO and also on methylotrophic and heterotrophic substrates, except for pyruvate and nutrient broth. The amounts of CO-DH in cells grown on methylamine, glucose, galactose, and succinate were comparable to that of the CO-grown cells. CO-DH activity, however, was onot deteted by the dye-linked assay method in cell extracts prepared from cells grown on organic substrates, except on ethanol and succinate. THe activity was detected when the CO-DH was stained by activity using CO as a substrate. CO-DHs in cells grown on different substrates were found to be identical in immunological properties.

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Cell Biological Studies on the Mechanism of Development and Differentiation Ⅷ 3. Effects of Polyamines on the Activities of Corn Glucose-6-Phosphate Dehydrogenase, 6-Phosphogluconate Dehydrogenase, and Protein Kinase (생체발생 및 분화기구의 세포생물학적 연구 Ⅷ 3. Polyamine이 옥수수 배의 Glucose-6-Phosphate Dehydrogenase, 6-Phosphogluconate Dehydrogenase 및 Protein Kinase 활성에 미치는 영향)

  • Cho, Young Dong
    • Journal of Plant Biology
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    • v.27 no.2
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    • pp.73-80
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    • 1984
  • Palmitoyl CoA was found to inhibit corn embryo axis glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, which were also inhibites by polyamines. However, reversal of inhibition of both enzymes by palmitoyl CoA was made by spermine. Activity of corn embryo axis protein kinase was found to increase steadily after germination. Activation and inhibition of protein kinase were made by MgCl$_2$and all polymines, respectively. Suc results suggest that fatty acid biosynthesis and lypolysis could be regulated to some extent by polyamines in corn embryo axis.

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Ethylmalonic Encephalopathy

  • Yun, Hye-Ran;Han, Si-Hun;An, Yeong-Min;Sin, Yun-Jeong
    • Journal of The Korean Society of Inherited Metabolic disease
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    • v.1 no.1
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    • pp.5-12
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    • 2001
  • 아시아 및 한국에서 처음 발견된 3명의 소아 Ethylmalonic encephalopathy (EE) 환자들은 riboflavin을 이용한 치료법에 점진적인 호전을 보인 것으로 나타났다. Ethylmalonic aciduria가 3가지 효소-2-methyl-branched-chain acyl CoA dehydrogenase (2MBCAD), iso-valeryl CoA dehydrogenase (IVCAD), 그리고 short-chain acyl CoA dehydrogenase (SCAD) - 들의 부분적인 결함으로 생긴다는 가설하에 dehydrogenase (탈수효소)의 보조 효소인 riboflavin이 부분적으로 나마 치료 과정에서 어떤 역할을 수행하는지의 여부를 살펴보았다. 다음의 세 증례에서 riboflavin 혹은 coenzyme Q10을 병행하여 치료한 결과 인지 행동(cognitive behavior)과 만성 점액성 설사(chronic mucoid diarrhea)가 호전된 것으로 관찰되었다. 또한, 치료 후 운동 기능도 일부 호전되었다. EE의 질병 발생 기전이 현재까지 완전히 밝혀지지는 않았지만, 세 명의 EE 환자들의 치료경과를 관찰하여 위의 가설을 뒷받침 할 수 있었다.

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The utilization of acetate for the growth and the respiration in Dunaliella tertiolecta.―Enzymes of the tricarboxylic acid cycle and glyoxylate pathway (Dunaliella tertiolecta에 의한 acetate의 이용 -TCA cycle과 glyoxylate pathway의 활성 조사-)

  • 권영명
    • Journal of Plant Biology
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    • v.16 no.1_2
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    • pp.6-11
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    • 1973
  • The utilization of acetate by Dunaliella tertiolecta was examined, and the detections and assays of the enzymes of the tricarboxylic acid cycle and the glyoxylate pathway were described. Acetate could not be utilized as a sole carbon source for the growth. The carboxyl carbon of acetate was incorporated more rapidly into CO2 than the methyl carbon. It was identified that malate, succinate, citrate and etc., were accumulated whne [U-14C] acetate was supplied to the cell free homogenate. The following enzyme activities were measured; acetothiokinase, isocitrate dehydrogenase, fumarase, malate dehydrogenase and aconitase. Though isocitratase, malate synthetase, succinate dehydrogenase and oxoglutarate dehydrogenase could not be detected, 14C from succinate was easily contributed to CO2 and cell component. The evidence suggested that the glyoxylate pathway was not operative and showed that the TCA cycle was the all important pathway in the oxidation of acetate to CO2 in Dunaliella.

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Effect of Medicinal Plant Extracts on the Ethanol-Metabolizing Enzyme Activities (약용식물 추출물의 에탄올대사 효소활성에 미치는 영향)

  • Do, Jaeho;Gwak, Jungwon;Lee, Sunjeong;Rho, Jung Jin;Lee, Kwangseung;Kim, Dong Chung
    • Food Engineering Progress
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    • v.21 no.3
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    • pp.286-291
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    • 2017
  • This study was conducted to certify the effect of aqueous extracts from fifty medicinal plants on the activities of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) in vitro. Each aqueous extract was prepared by combining one-part medicinal plants with twenty-parts distilled water at $80^{\circ}C$ for 8 h. Among the fifty medicinal plants, Allium sativum L. and Cinnamomum cassia Presl were regarded as an effective anti-hangover substance. Allium sativum L. extract increased ALDH activity more than 2 times compared with ADH activity, enhancing the acetaldehyde degradation. Cinnamomum cassia Presl extract dramatically inhibited ADH activity compared with ALDH activity, thus potently decreasing the acetaldehyde formation. ADH and ALDH activities were proportionally inhibited according to the increased concentration of Cinnamomum cassia Presl extract. The aqueous extract of Cinnamomum cassia Presl at a concentration of $45.33{\mu}g/mL$ inhibited ADH activity by 52.8% and ALDH activity by 11.0%.

Short-chain Acyl-CoA Dehydrogenase Deficiency in an Asymptomatic Neonate (무증상 신생아에서 진단된 경쇄 acyl-CoA 탈수소효소 결핍증 1례)

  • Lee, Yeonhee;Kim, Jinsup;Huh, Rimm;Cho, Sung Yoon;Jin, Dong-Kyu
    • Journal of The Korean Society of Inherited Metabolic disease
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    • v.15 no.2
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    • pp.93-97
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    • 2015
  • Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is an autosomal recessive hereditary metabolic disorder of mitochondrial fatty acid beta-oxidation. Mutations in the ACADS gene cause short-chain acyl-CoA dehydrogenase deficiency, which is characterized by developmental delay, hypotonia, seizure, and hypoglycemia. Here, we describe one Korean pediatric case of SCAD deficiency, which was diagnosed during newborn screening by tandem mass spectrometry and confirmed by molecular analysis. The level of C4 was typically elevated 5.23 mg/dL (reference range <1.5 mg/dL). This patient had a homozygous mutation [c.1031A>G, p. E344G] in ACADS. Therefore, we present a case of SCAD deficiency in an otherwise healthy neonate and her subsequent development and growth over four years.

Isolation and Characterization of Malate Dehydrogenase Gene from Panax ginseng C.A. Meyer (고려인삼에서 Malate Dehydrogenase 유전자의 분리 및 분석)

  • Kim, Yu-Jin;Shim, Ju-Sun;Lee, Jung-Hye;Jung, Dae-Young;In, Jun-Gyo;Lee, Bum-Soo;Min, Byung-Hoon;Yang, Deok-Chun
    • Korean Journal of Medicinal Crop Science
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    • v.16 no.4
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    • pp.261-267
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    • 2008
  • Malate dehydrogenase is a ubiquitous enzyme in plants, involving in a range of metabolic processes depending on its subcellular location. A malate dehydrogenase (PgMDH) cDNA was isolated and characterized from the root of Panax ginseng C. A. Meyer. The deduced amino acid sequence of PgMDH showed high similarity with the NAD-dependent mitochondrial malate dehydrogenase from Glycinemax (P17783), Eucalyptus gunnii (P46487), and Lycopersicon esculentum (AAU29198). And the segment of a malate dehydrogenase gene was amplified through RT-PCR. The expression of PgMDH was increased after treatments of chilling, salt, UV, cadmium or copper treatment.

Effect of Fermented Sea Tangle on the Alcohol Dehydrogenase and Acetaldehyde Dehydrogenase in Saccharomyces cerevisiae

  • Cha, Jae-Young;Jeong, Jae-Jun;Yang, Hyun-Ju;Lee, Bae-Jin;Cho, Young-Su
    • Journal of Microbiology and Biotechnology
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    • v.21 no.8
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    • pp.791-795
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    • 2011
  • Sea tangle, a kind of brown seaweed, was fermented with Lactobacillus brevis BJ-20. The gamma-aminobutyric acid (GABA) content in fermented sea tangle (FST) was 5.56% (w/w) and GABA in total free amino acid of FST was 49.5%. The effect of FST on the enzyme activities and mRNA protein expression of alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) involved in alcohol metabolism in Saccharomyces cerevisiae was investigated. Yeast was cultured in YPD medium supplemented with different concentrations of FST powder [0, 0.4, 0.8, and 1.0% (w/v)] for 18 h. FST had no cytotoxic effect on the yeast growth. The highest activities and protein expressions of ADH and ALDH from the cell-free extracts of S. cerevisiae were evident with the 0.4% and 0.8% (w/v) FST-supplemented concentrations, respectively. The highest concentrations of GABA as well as minerals (Zn, Ca, and Mg) were found in the cell-free extracts of S. cerevisiae cultured in medium supplemented with 0.4% (w/v) FST. The levels of GABA, Zn, Ca, and Mg in S. cerevisiae were strongly correlated with the enzyme activities of ADH and ALDH in yeast. These results indicate that FST can enhance the enzyme activities and protein expression of ADH and ALDH in S. cerevisiae.

A Case of asymptomatic Short-chain Acyl-CoA Dehydrogenase Deficiency (무증상의 경쇄 acyl-CoA 탈수소효소 결핍증 1례)

  • Lee, Hwapyung;Kim, Jinsup;Huh, Rimm;Cho, Sung Yoon;Jin, Dong-Kyu
    • Journal of The Korean Society of Inherited Metabolic disease
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    • v.15 no.2
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    • pp.98-100
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    • 2015
  • Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a rare mitochondrial fatty-acid oxidation disorder that is inherited as an autosomal recessive pattern. SCAD deficiency is caused by mutations in the ACADS gene (Acyl-CoA Dehydrogenase, Short-chain, OMIM #606885), which encodes SCAD, the mitochondrial enzyme that catalyzes the first reaction in the beta-oxidation of fatty acids four to six carbons in length. Here, we describe one Korean pediatric case of SCAD deficiency, which was diagnosed during newborn screening through tandem mass spectrometry. An increased concentration of butyrylcarnitine was detected on the newborn screening test, and the urine organic acid analysis showed increased urinary excretion of ethylmalonic acid. The patient has been asymptomatic and has shown normal growth and development by 8 months of age without any intervention during follow-up period.