scholarly journals Divergent effects of glutathione depletion on isocitrate dehydrogenase 1 and the pentose phosphate pathway in hamster liver

2020 ◽  
Vol 8 (16) ◽  
Author(s):  
Eunsook S. Jin ◽  
Min H. Lee ◽  
Craig R. Malloy
Keyword(s):  
Pentose Phosphate Pathway ◽  
Isocitrate Dehydrogenase ◽  
Pentose Phosphate ◽  
Glutathione Depletion ◽  
Isocitrate Dehydrogenase 1

Enzyme Activities in Prickly Sida(Sida spinosa)Seeds of Different Developmental Stages

Weed Science ◽  
1978 ◽  
Vol 26 (4) ◽  
pp. 349-351 ◽  
Author(s):  
E. W. Smith ◽  
B. J. Reger ◽  
G. H. Egley
Keyword(s):  
Dehydrogenase Activity ◽  
Pentose Phosphate Pathway ◽  
Isocitrate Dehydrogenase ◽  
Enzyme Activities ◽  
Developmental Stages ◽  
Pentose Phosphate ◽  
Sida Spinosa ◽  
Prickly Sida ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Days After Anthesis

Key metabolic enzymes and germination were studied in developing and mature, dormant and nondormant prickly sida(Sida spinosaL.) seeds. Isocitrate dehydrogenase, glucose-6-phosphate dehydrogenase, fructose-1,6-diphosphatase, and phosphofructokinase activities were determined in developing and mature prickly sida seeds. Developing seeds less than 7 days after anthesis and at 17 days or greater after anthesis were unable to germinate. The 7-day-old seeds lacked all but fructose-1,6-diphosphatase activity. The 17-day-old seeds demonstrated all enzyme activities but failed to germinate because dehydration had occurred and seeds were unable to imbibe sufficient water without an afterripening period. Comparison of enzyme activities of dormant and nondormant seeds on incubation showed that only glucose-6-phosphate dehydrogenase was considerably different within the first 8 h of incubation. Nondormant seeds had considerable glucose-6-phosphate dehydrogenase activity before germination (radical protrusion at 8 h), suggesting an active pentose phosphate pathway.

scholarly journals Identification of Enzymes and Quantification of Metabolic Fluxes in the Wild Type and in a Recombinant Aspergillus oryzae Strain

1999 ◽  
Vol 65 (1) ◽  
pp. 11-19 ◽  
Author(s):  
Henrik Pedersen ◽  
Morten Carlsen ◽  
Jens Nielsen
Keyword(s):  
Growth Rate ◽  
Pentose Phosphate Pathway ◽  
Isocitrate Dehydrogenase ◽  
Type Strain ◽  
Wild Type Strain ◽  
Specific Growth ◽  
Pentose Phosphate ◽  
Central Metabolism ◽  
Wild Type ◽  
Metabolic Fluxes

ABSTRACT Two α-amylase-producing strains of Aspergillus oryzae, a wild-type strain and a recombinant containing additional copies of the α-amylase gene, were characterized with respect to enzyme activities, localization of enzymes to the mitochondria or cytosol, macromolecular composition, and metabolic fluxes through the central metabolism during glucose-limited chemostat cultivations. Citrate synthase and isocitrate dehydrogenase (NAD) activities were found only in the mitochondria, glucose-6-phosphate dehydrogenase and glutamate dehydrogenase (NADP) activities were found only in the cytosol, and isocitrate dehydrogenase (NADP), glutamate oxaloacetate transaminase, malate dehydrogenase, and glutamate dehydrogenase (NAD) activities were found in both the mitochondria and the cytosol. The measured biomass components and ash could account for 95% (wt/wt) of the biomass. The protein and RNA contents increased linearly with increasing specific growth rate, but the carbohydrate and chitin contents decreased. A metabolic model consisting of 69 fluxes and 59 intracellular metabolites was used to calculate the metabolic fluxes through the central metabolism at several specific growth rates, with ammonia or nitrate as the nitrogen source. The flux through the pentose phosphate pathway increased with increasing specific growth rate. The fluxes through the pentose phosphate pathway were 15 to 26% higher for the recombinant strain than for the wild-type strain.

Glucose metabolism in Xanthomonas campestris and influence of methionine on the carbon flow

1988 ◽  
Vol 34 (12) ◽  
pp. 1333-1337 ◽  
Author(s):  
P. Pielken ◽  
K. -L. Schimz ◽  
L. Eggeling ◽  
H. Sahm
Keyword(s):  
Carbon Dioxide ◽  
Glucose Metabolism ◽  
Dehydrogenase Activity ◽  
Pentose Phosphate Pathway ◽  
Isocitrate Dehydrogenase ◽  
Xanthomonas Campestris ◽  
Glucose Dehydrogenase ◽  
Dry Weight ◽  
Pentose Phosphate ◽  
The Other

The glucose flow in Xanthomonas campestris was investigated with radio-labelled glucose and by enzymological studies. Only 7% of the radioactivity was incorporated into the cell material, but 41% was oxidized to carbon dioxide and 28% transformed to xanthan. Up to 16% of cell dry weight consisted of the polysaccharide glycogen. In the presence of 2.7 mM methionine, which is an inhibitor of xanthan formation, increased carbon dioxide formation (51%) occurred. This increase was in accordance with a twofold increase in the NAD-dependent isocitrate dehydrogenase activity. The other carbon dioxide liberating enzyme, 6-P-gluconate dehydrogenase, was not influenced by methionine, but its occurrence indicates the presence of an active pentose phosphate pathway in X. campestris. Among the other enzymes detected in X. campestris was glucose dehydrogenase. The presence of this enzyme together with hexokinase indicates the operation of two different glucose metabolizing steps: one oxidative, the other phosphorylative. Only the latter directly provides phosphorylated glucose as a precursor for the activated sugars required for xanthan synthesis.

scholarly journals Development of NADPH-producing pathways in rat heart

1980 ◽  
Vol 186 (3) ◽  
pp. 799-803 ◽  
Author(s):  
A Andrés ◽  
J Satrústegui ◽  
A Machado
Keyword(s):  
Pentose Phosphate Pathway ◽  
Isocitrate Dehydrogenase ◽  
Malic Enzyme ◽  
Rat Heart ◽  
Pentose Phosphate ◽  
Mitochondrial Enzyme ◽  
Physiological Functions ◽  
Phosphogluconate Dehydrogenase ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Mitochondrial Malic Enzyme

The behaviours of the principal NADPH-producing enzymes (glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, cytoplasmic and mitochondrial ‘malic’ enzyme and NAPD+-dependent isocitrate dehydrogenase) were studied during the development of rat heart and compared with those in brain and liver. 1. The enzymes belonging to the pentose phosphate pathway exhibit lower activities in heart than in other tissues throughout development. 2. The pattern of induction of heart cytoplasmic and mitochondrial ‘malic’ enzymes does not parallel that found in liver. Heart mitochondrial enzyme is slowly induced from birth onwards. 3. NADP+-dependent isocitrate dehydrogenase has similar activities in all tissues in 18-day foetuses. 4. Heart mitochondrial NADP+-dependent isocitrate dehydrogenase is greatly induced in the adult, where it attains a 10-fold higher activity than in liver. 5. The physiological functions of mitochondrial ‘malic’ enzyme and NADP+-dependent isocitrate dehydrogenase are discussed.

scholarly journals Systematic Identification of Regulators of Oxidative Stress Reveals Non-canonical Roles for Peroxisomal Import and the Pentose Phosphate Pathway

Cell Reports ◽  
2020 ◽  
Vol 30 (5) ◽  
pp. 1417-1433.e7 ◽  
Author(s):  
Michael M. Dubreuil ◽  
David W. Morgens ◽  
Kanji Okumoto ◽  
Masanori Honsho ◽  
Kévin Contrepois ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Pentose Phosphate Pathway ◽  
Pentose Phosphate ◽  
Systematic Identification
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