• Microbiology and Biotechnology Letters
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• v.17 no.6
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• pp.552-555
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• 1989

A 150-fold purified preparation of NADPH-specific glutamate dehydrogenase of Corynebacterium glutamicum (1) was used for the determination of kinetic parameters of the substrates, NADPH, NH$_4$Cl, and $\alpha$-ketoglutarate in the direction of glutamate synthesis. The kinetic constants determined from this study suggest a biosynthetic role for the enzyme, Based on the analysis of the result derived from initial velocity, the reaction mechanism was postulated to be ordered addition with NADPH as a first substrate to bind in the forward direction. Of the several metabolites tested for a possible function in the regulation of glutamate dehydrogenase activity, only malate and citrate were appeared to have an appreciable influence on the enzyme, Potassium chloride showed to be the most effective for the enzyme activity.

• 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.

• 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.

• Microbiology and Biotechnology Letters
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• v.21 no.6
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• pp.577-581
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• 1993

The amino acid threonine was produced from glycine and ethanol in a reaction mixture using cell free extract of the methylotrophic bacterium isolated from soil and identified as mellthylo-bacterium sp. KJ29. Although the isolate could grow on carbon source other than methanol, only the cell free extract from the cells grown on methanol produced threonine. Methanol dehydrogenase (MDH) activity was present only in the cells grown on methanol when compared to the cells grown on heterotrophic substrates.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.160.3-161
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• 2003

Aldehyde and active form of free oxygen produced in alcohol metabolism in liver are the cause of liver cell damage. The main system of alcohol metabolism is composed of alcohol dehydrogenase(ADH), aldehyde dehydrogenase(ALDH) and cytochrome P4502E1. Alcohol dehydrogenase is reversible in alcohol metabolism. To block the backward reaction and enhance alcohol oxidation, acetaldehyde trapping agents were assayed. The assay was carried out by measuring decreasing NADH at 340nm, using acetaldcehyde and NADH as substrate and coenzyme respectively. (omitted)

• The Korean Journal of Zoology
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• v.28 no.4
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• pp.257-278
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• 1985

The effect of aromatic amino acids such as phenylalaine, tryptophan and tyrosine on somitogenesis at the early stage of chick embryo has been investigated morphologically using light and electron microscopy. Micrographs of aromatic amino acid injected chick embryo showed that an incomplete somite segmentation occurred and some decremental effect on the nervous system were observed. Somites were poorly developed and their size were variable. Electron micrograph of somatic cells from aromatic amino acid injected chick embryo showed that chromatins were coagulated, some of mitochondria were damaged, and nucleus were transformed considerably in some cases. The protein and nucleic acid levels and some enzyme activities of 15-day chick embryo which received the injection of 1mg of aromatic amino acid in 0.05 ml of saline 24 hours after the incubation were analyzed. Protein, DNA and RNA levels of the test group were not lowered significantly but the activities of enzymes for basic metabolism, such as lactate dehydrogenase, succinate dehydrogenase, malate dehydrogenase and glucose 6-phosphate dehydrogenase were considerably lowered as compared with those of control. From the present expeerimental results, it was tentatively suggested that the administration of amino acid might slow down the yolk granule degradation probably by feed back mechanism resulting in the disturbance of amino acid balance in the cell, which might give rise to impair normal metabolic pattern leading to abnormal somitogenesis to chick embryo at very early stage of development.

• BMB Reports
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• v.32 no.5
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• pp.515-520
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• 1999

Incubation of two types of glutamate dehydrogenase isoproteins from bovine brain with the arginine-specific dicarbonyl reagent phenylglyoxal resulted in a biphasic loss of enzyme activity. Reaction of the glutamate dehydrogenase isoproteins with phenylglyoxal caused a rapid loss of 53~62% of the enzyme activities and modification of two residues of arginine per enzyme subunit. Prolonged incubation of the glutamate dehydrogenase isoproteins with phenylglyoxal resulted in the modification of an additional four residues of arginine per enzyme subunit without further loss of the residual activities. Partial protection against inactivation was provided by the coenzyme NADH or substrate 2-oxoglutarate. The most marked decrease in the rate of inactivation was observed by the combined addition of NADH and 2-oxoglutarate, suggesting that the first two modified arginine residues are in the vicinity of the catalytic site. However, inactivation of the glutamate dehydrogenase isoproteins by phenylglyoxal appears to be partial with approximately 40% activity remained after an extended reaction time with excess reagent, suggesting that the modified arginine residues may not be directly involved in catalysis. The lack of complete protection by substrates also suggest the possibility that the modified arginine residues are not directly involved at the active site, and the partial loss of activity by the modification of arginine residues may be due to a conformational change. There were no significant differences between the two glutamate dehydrogenase isoproteins in sensitivities to inactivation by phenylglyoxal, indicating that the microenvironmental structures of the glutamate dehydrogenase isoproteins are very similar to each other.

• Korean Journal of Environmental Biology
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• v.20 no.2
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• pp.173-179
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• 2002

N-nitrosoethylurea (NEU) -induced changes of lipid peroxide content, aldehyde metabolic enzyme activities and antioxidant enzyme activities were examined in cultured rat liver cell. Aldehyde metabolic enzymes tested in this investigation were alcohol dehydrogenase and aldehyde dehydrogenase. Several antioxidant enzymes tested were glutathione transferase, superoxide dismutase, glutathione reductase and catalase. When the cell was exposed with various concentrations of NEU, lipid peroxide content increased about 2.5 fold with 6.25 mM NEU. Maximun 2.3 times higher alcohol dehydrogenase activity was found after NEU treatment. About 2 times higher aldehyde dehydrogenase activity could also be observed. Only slight increases of glutathione transferase and catalase activities occurred with NEU treatment. In addition mnximun 1.5 times higher superoxide dismutase activities and 3 times higher glutathione reductase activities were found after NEU treatment. Therefore, it is likely that the increases of superoxide dismutase and glutathione reductase could contribute in a antioxidative process against NEU toxicity.

• BMB Reports
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• v.38 no.5
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• pp.624-631
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• 2005

Tuberculosis, caused by Mycobacterium tuberculosis, continues to be one of the main diseases to mankind. It is urgent to discover novel drug targets for appropriate antimicrobial agents against this human pathogen. The shikimate pathway is onsidered as an attractive target for the discovery of novel antibiotics for its essentiality in bacteria and absence in mammalian cells. The Mycobacterium tuberculosis aroE-encoded shikimate dehydrogenase was cloned, expressed and purified. Sequence alignment analysis shows that shikimate dehydrogenase of Mycobacterium tuberculosis exhibit the pattern of G-X-(N/S)-V-(T/S)-X-PX-K, which is highly conserved within the shikimate dehydrogenase family. The recombinant shikimate dehydrogenase spectrum determined by CD spectroscopy showed that the percentages for $\alpha$-helix, $\beta$-sheet, $\beta$-turn, and random coil were 29.2%, 9.3%, 32.7%, and 28.8%, respectively. The enzymatic characterization demonstrates that it appears to be fully active at pH from 9.0 to 12, and temperature $63^{\circ}C$. The apparent Michaelis constant for shikimic acid and $NADP^+$ were calculated to be about $29.5\;{\mu}M$ and $63\;{\mu}M$. The recombinant shikimate dehydrogenase catalyzes the substrate in the presence of $NADP^+$ with an enzyme turnover number of $399\;s^{-1}$. Zymological studies suggest that the cloned shikimate dehydrogenase from M. tuberculosis has a pretty activity, and the work should help in the discovery of enzyme inhibitors and further of possible antimicrobial agents against Mycobacterium tuberculosis.

• Journal of Korean Society of Occupational and Environmental Hygiene
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• v.4 no.2
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• pp.148-156
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• 1994

Chloral hydrate(CH), an intermediate metabolite of trichloroethylene(TRI) is reduced to trichloroethanol(TCE-OH), and is oxidized to trichloroacetic acid(TCA) by the nicotinamide adenine dinucleotide(NAD)-dependent enzymes such as alcohol dehydrogenase(ADH) and aldehyde dehydrogenase(ALDH) in liver. This study was performed to find out the change of activity of ADH and ALDH with increasing amount of TRI. Intraperitoneal injection of TRI were done to the male Sprague Dawely rats(mean body weight, $170{\pm}10g$) in com oil at the dosage of 150, 300, 600 mg/kg for 2 days. The results of experiments are following : 1. The contents of xenobiotic metabolic enzymes in liver are tended to be decreased with increasing amount of, but not significantlly (p>0.05). 2. Activity of ADH in microsome is decreased(p<0.05), and activity of ALDH is increased with amount of TRI(P<0.05). 3. Total trichloro-compounds(TTC) concentration in urine are increased with amount of TRI, but the ratio of between the TCE-OH and the TCA were not shown any critical change. These results suggests that the ALDH in microsome may be related to metabolism of TRI, but ADH was nothing less than the effected to metabolism of TRI.