• International Journal of Industrial Entomology and Biomaterials
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• v.18 no.2
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• pp.91-95
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• 2009

The presence of considerable amount of enzymes of TCA cycle isocitrate dehydrogenase (ICDH-NADP+, EC1.1.1.42), $\alpha$-ketogluterate dehydrogenase ($\alpha$-KGD, EC1.2.4.2) and malate dehydrogenase (MDH, EC1.1.1.37) in fresh control and in vitro starved adult Isoparorchis hypselobagri establish the functional TCA cycle in this fluke. The major metabolic end products are pyruvate, lactate, oxaloacetate and malate. The ratio of oxaloacetate/malate assess that oxaloacetate is reduced to malate and in this fluke the reverse TCA cycle is active. The pyruvate/lactate ratio shows pyruvate is reduced to lactate and the fluke is homolactate farmenters.

• Korean Journal of Microbiology
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• v.26 no.2
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• pp.93-100
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• 1988

In order to understand the regulation of glutamate dehydrogenase(GDH) synthesis in Brevibacterium flavum, we have isolated a mutant lacking NADP-linked GDH activity by ethlmethane sulfonate treatment. The $gdh^-$ mutant was grown on the minimal plate with 1mM ammonium chloride and not that with 300mM ammonium chloride. The cell-free extracts from $gdh^-$ mutant and prototroph were also examined with glutamine synthetase(GS) and glutamate synthase (GOGAT) production by niteogen sources. The growth of $gdh^-$ mutant in presence of 20mM ammonium chloride means that GOGAT synthesis is sufficient to allow growth in this condition. GS production of $gdh^-$ mutant as well as parental strain was induced by 1mM urea and ammonium tartrate, but it was repressed by higher concentration of ammonia, and also induced by 20mM to 50mM glutamate as a substrate. It was special attention that GOGAT synthesis from $gdh^-$ strain was more repressed by higher concentration of ammonia than prototroph as described in E. coli system.

• Journal of Pharmaceutical Investigation
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• v.9 no.4
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• pp.23-28
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• 1979

The effect of maltitol admininstration to rat was studied on breakdown of ${\alpha}-glycoside$ linkage with intestinal mucosa or pancreatic enzymes and induction of hepatic polyol dehydrogenase activities. Maltitol was contained as 13% or 26% in diet, and was administrated to rat for 9 weeks. This report carried out that ${\alpha}-glycoside$ linkage of maltitol was not hydrolyzed with pancreatic enzymes and intestinal mucosa. Maltitol dehydrogenase was not obeserved in liver cytoplasm, and hepbtic sorbitol dehydrogenase was not induced by maltitol administsation. Also, the effect of maltitol on aging of aluminum hydroxide gel, prepared by the reaction of aluminum chloride solution with strong ammonia solution to final pH 7.0, was studied by potentiometric titration, pH and acid-consuming capacity. Gel containing 1% or 2% maltitol was lost less than 2% of their acid-consuming capacity during a 120 days aging period compared with a loss of more than for an identical gel without maltitol and gel containing 0.5% maltitol.

• BMB Reports
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• v.45 no.2
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• pp.91-95
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• 2012

Glutamate dehydrogenase from axenic bacterial cultures of a new microorganism, called GWE1, isolated from the interior of a sterilization drying oven, was purified by anion-exchange and molecular-exclusion liquid chromatography. The apparent molecular mass of the native enzyme was 250.5 kDa and was shown to be an hexamer with similar subunits of molecular mass 40.5 kDa. For glutamate oxidation, the enzyme showed an optimal pH and temperature of 8.0 and $70^{\circ}C$, respectively. In contrast to other glutamate dehydrogenases isolated from bacteria, the enzyme isolated in this study can use both $NAD^+$ and $NADP^+$ as electron acceptors, displaying more affinity for $NADP^+$ than for $NAD^+$. No activity was detected with NADH or NADPH, 2-oxoglutarate and ammonia. The enzyme was exceptionally thermostable, maintaining more than 70% of activity after incubating at $100^{\circ}C$ for more than five hours suggesting being one of the most thermoestable enzymes reported in the family of dehydrogenases.

• Parasites, Hosts and Diseases
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• v.34 no.4
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• pp.239-246
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• 1996

The usefulness of malaria diagnosis by Plusmodium JaLcipawn-GDH (NADP+), obtained by affinity chromatography. is demonstrated in ELISA assays, testing IgG antibodies against GDH (NADP+) from patients with acute malaria, who have had two or more episodes of malaria. or from sera of hyperimmune patients. GDH (NADP+) thermal stability was demonstrated in a high heat resistance assay. The immunofluorescence assay demonstrated that anti-culture (P. falciporum) supernatant serum and anti-GDH (NADP+) of Proton app. recognized epitopes in Venezuelan isolates and Colombian and Brazilian malarial strains. The antigen is soluble, with high specificity is a potent imnlunogen and is thermoresistant. Key words: antigenic enzymes. glutamate dehydrogenase, malaria diagnosis, Plasmodium berghei, Plcswlodium ccthemelum, PlusmoniumJnlcipnmm, Plosmonium uiuox. soluble antigens.

• Journal of Microbiology and Biotechnology
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• v.10 no.4
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• pp.564-567
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• 2000

A recombinant Saccharomyces cerevisiae, transformed with the genes encoding xylose reductase (XYL1) and xylitol dehydrogenase (XYL2) orginated from Pichia stipitis CBS 5776, was developed to directly convert xylose to ethanol. A fed-batch fermentation with the recombinant yeast produced 8.7 g ethanol/l with a yield of 0.13 g ethanol/g xylose consumed.

• Microbiology and Biotechnology Letters
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• v.19 no.6
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• pp.610-613
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• 1991

Some of the Kinetic properties of crystallic xanthine dehydrogenase form Pseudomonas synxantha A3 were studied. The enzyme activity was strongly inhibited by adenine, 8-azaadenine, 2-methyladenine, guanine, and 8-azaguanine, but not by caffeine, and the inhibitions by adenine and guanine were observed to be of noncompetitive type. The $K_i$ values for adenine and guanine were 0.037 and 0.098 mM, respectively. Michaelis constants were found to be 0.33 and 0.06 rnM for hypoxanthine and xanthine with $NAD^+$ as the second substrate, respectively, and 0.1 rnM for $NAD^+$ with either hypoxanthine or xanthine as the second substrate.

• International Journal of Industrial Entomology and Biomaterials
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• v.7 no.1
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• pp.51-57
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• 2003

A cDNA encoding a putative alcohol dehydrogenase (ADH) class III was cloned from the silkworm, Bombyx mono The full length cDNA is 1,385 nucleotides long and contains an open reading frame of 1,128 bp encoding 376 amino acid residues. The B. mon ADH III protein sequence was aligned with ADH III known from various organisms. Interestingly, the protein sequence of B. mon ADH III showed 87% and 85% identity to ADH III from marine fish Sparus aurata and Branchiostoma floridae, respectively, whereas rather low sequence identity (83%) to Drosophila melanogaster ADH III was observed. Northern blot analysis revealed that B. mon ADH III mRNA is expressed in all tissues from larva examined: fat body, midgut, epidermis, silk gland and ovary, with the highest level found in the fat body.

• The Korean Journal of Ecology
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• v.21 no.3
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• pp.301-307
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• 1998

Intraspecific and interspecific isozyme variations and their relationship of 16 local populations in 3 species of Phyllostachys, that is, P. bambusoides, P. nigra var. henonis and P. pubescens were investigated by multi-variate analysis. Leaf isozymes of Phyllostachys such as 6-PGD (6-phosphogluconate dehydrogenase), MDH (malate dehydrogenase), PGI (phosphoglucoisomerase), PRX (peroxidase), PGM (phosphoglutamase), IDH (isocitrate dehydrogenase) showed electrophoretic variations in the number of zymotypes (7, 6, 6, 9, 3 and 5, respectively). In the cluster analysis on the isozymic characteristics, 16 populations were classified into 3 species at the euclid genetic distance of 2.041. P. nigra var. henonis and P. bambusoides were clustered first at 2.813 and then P. pubescens at 3.001. So far, 3 local types of intraspecific ariation were found in P. nigra var. henonis and P. bambusoides.

• BMB Reports
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• v.35 no.4
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• pp.437-441
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• 2002

Dihydrolipoamide dehydrogenase (E3) is a member of the pyridine nucleotide-disulfide oxidoreductase family. Thr residues are highly conserved. They are at the active site disulfide-bond regions of most E3s and other oxidoreductases,. The crystal structure of Azotobacter vinelandii E3 suggests that the hydroxyl group of Thr that are involved in the FAD binding interact with the adenosine phosphate of FAD. However, several prokaryotic E3s have Val instead of Thr. To investigate the meaning and importance of the Thr conservation in many E3s, the corresponding residue, Thr-44, in human E3 was substituted to Val by site-directed mutagenesis. The mutant’s E3 activity showed about a 2.2-fold decrease. Its UV-visible and fluorescence spectra indicated that the mutant might have a slightly different microenvironment at the FAD-binding region.