Dark modulation of NADP-dependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast

1981 ◽  
Vol 636 (1) ◽  
pp. 58-64 ◽  
Author(s):  
Renate Scheibe ◽  
Louise E. Anderson
Keyword(s):  
Malate Dehydrogenase ◽  
Glucose 6 Phosphate Dehydrogenase

scholarly journals Changes in activity of some enzymes involved in glucose utilization and formation in developing rat liver

1968 ◽  
Vol 106 (2) ◽  
pp. 321-329 ◽  
Author(s):  
R. G. Vernon ◽  
D G Walker
Keyword(s):  
Malate Dehydrogenase ◽  
Rat Liver ◽  
Postnatal Period ◽  
Supernatant Fraction ◽  
Atp Citrate Lyase ◽  
Carboxylase Activity ◽  
Phosphogluconate Dehydrogenase ◽  
Citrate Lyase ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Developing Rat

1. The activities of some enzymes involved in both the utilization of glucose (pyruvate kinase, ATP citrate lyase, NADP-specific malate dehydrogenase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and NADP-specific isocitrate dehydrogenase, all present in the supernatant fraction of liver homogenates) and the formation of glucose by gluconeogenesis (glucose 6-phosphatase in the whole homogenate and fructose 1,6-diphosphatase, phosphopyruvate carboxylase, NAD-specific malate dehydrogenase and fumarase in the supernatant fraction) have been determined in rat liver around birth and in the postnatal period until the end of weaning. 2. The activities of those enzymes involved in the conversion of glucose into lipid are low during the neonatal period and increase with weaning. NADP-specific malate dehydrogenase first appears and develops at the beginning of the weaning period. 3. The marked increase in cytoplasmic phosphopyruvate carboxylase activity at birth is probably the major factor initiating gluconeogenesis at that time. 4. The results are discussed against the known changes in dietary supplies and the known metabolic patterns during the period of development.

Enzyme polymorphism in Schistosoma mattheei from cattle in the Eastern Transvaal Lowveld

1989 ◽  
Vol 63 (3) ◽  
pp. 191-196 ◽  
Author(s):  
F. J. Kruger
Keyword(s):  
Adult Worm ◽  
Malate Dehydrogenase ◽  
Enzyme Polymorphism ◽  
The Other ◽  
Enzyme Electrophoresis ◽  
Weinberg Equilibrium ◽  
Hardy Weinberg Equilibrium ◽  
Glucose 6 Phosphate Dehydrogenase

ABSTRACTEnzyme electrophoresis was conducted on 10 Schistosoma mattheei adult worm samples, comprising 270 individuals, collected from cattle in the Eastern Transvaal Lowveld. Glucose-6-phosphate dehydrogenase (G6PDH) was studied in all the samples and phosphoglucomutase (PGM) and malate dehydrogenase (MDH) in five populations each. Only one population was polymorphic for G6PDH. In this population, in addition to the allele found in all the other samples, a second allele occurred with a similar Rf value to S. haematobium. The two alleles were in Hardy-Weinberg equilibrium. MDH-1 exhibited two alleles. However, these alleles were not in equilibrium. In certain populations, heterozygotes occurred together with homozygotes of one of the alleles only. PGM was monomorphic in all the populations studied.

Interactions of 2-furylethylenes with thiol enzymes

1983 ◽  
Vol 48 (1) ◽  
pp. 327-335 ◽  
Author(s):  
Ernest Šturdík ◽  
Ľudovít Drobnica ◽  
Štefan Baláž
Keyword(s):  
Catalytic Activity ◽  
Chemical Modification ◽  
Glutathione Reductase ◽  
Malate Dehydrogenase ◽  
Cysteine Residues ◽  
Sh Groups ◽  
Inhibition Constants ◽  
Glucose 6 Phosphate Dehydrogenase

Furylethylenes are inhibitors of glyceraldehyde 3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12), glucose 6-phosphate dehydrogenase (EC 1.1.1.49), glutathione reductase (GR; EC 1.6.4.2), and, in part, also malate dehydrogenase (EC 1.1.1.37). These four enzymes served as model thiolproteins employing the SH groups of the embodied cysteine for catalytic activity. The inhibition degree of the afore-mentioned enzymes is proportional to the reactivity of furylethylenes towards thiols. The inhibition of GAPDH and GR with 1-(5-nitro-2-furyl)-2-nitro-2-methoxycarbonylethylene (I) was characterized by inhibition constants Ki and also, its type was estimated. A direct chemical modification of SH groups of cysteine residues was found in GAPDH, a fact that could be closely connected with the inactivation of the enzyme.

scholarly journals The kinetics of enzyme changes in yeast under conditions that cause the loss of mitochondria

1968 ◽  
Vol 107 (4) ◽  
pp. 455-465 ◽  
Author(s):  
C. Chapman ◽  
W Bartley
Keyword(s):  
Cytochrome C ◽  
Glutamate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Nadh Oxidase ◽  
Isocitrate Lyase ◽  
Lag Phase ◽  
Glutamate Oxaloacetate Transaminase ◽  
Oxoglutarate Dehydrogenase ◽  
Nadh Cytochrome ◽  
Glucose 6 Phosphate Dehydrogenase

1. Aerobically grown yeast having a high activity of glyoxylate-cycle, citric acid-cycle and electron-transport enzymes was transferred to a medium containing 10% glucose. After a lag phase of 30min. the yeast grew exponentially with a mean generation time of 94min. 2. The enzymes malate dehydrogenase, isocitrate lyase, succinate–cytochrome c oxidoreductase and NADH–cytochrome c oxidoreductase lost 45%, 17%, 27% and 46% of their activity respectively during the lag phase. 3. When growth commenced pyruvate kinase, pyruvate decarboxylase, alcohol dehydrogenase, glutamate dehydrogenase (NADP+-linked) and NADPH–cytochrome c oxidoreductase increased in activity, whereas aconitase, isocitrate dehydrogenase (NAD+- and NADP+-linked), α-oxoglutarate dehydrogenase, fumarase, malate dehydrogenase, succinate–cytochrome c oxidoreductase, NADH–cytochrome c oxidoreductase, NADH oxidase, NADPH oxidase, cytochrome c oxidase, glutamate dehydrogenase (NAD+-linked), glutamate–oxaloacetate transaminase, isocitrate lyase and glucose 6-phosphate dehydrogenase decreased. 4. During the early stages of growth the loss of activity of aconitase, α-oxoglutarate dehydrogenase, fumarase and glucose 6-phosphate dehydrogenase could be accounted for by dilution by cell division. The lower rate of loss of activity of isocitrate dehydrogenase (NAD+- and NADP+-linked), glutamate dehydrogenase (NAD+-linked), glutamate–oxaloacetate transaminase, NADPH oxidase and cytochrome c oxidase implies their continued synthesis, whereas the higher rate of loss of activity of malate dehydrogenase, isocitrate lyase, succinate–cytochrome c oxidoreductase, NADH–cytochrome c oxidoreductase and NADH oxidase means that these enzymes were actively removed. 5. The mechanisms of selective removal of enzyme activity and the control of the residual metabolic pathways are discussed.

scholarly journals The dependence of nitrate reductase activity on the level of soluble sugars in wheat and cucumber roots growing in the presence of simazine, in light or in darkness

2014 ◽  
Vol 55 (4) ◽  
pp. 589-600 ◽  
Author(s):  
Józef Buczek ◽  
Jacek Borkowski ◽  
Irena Jarzyńska
Keyword(s):  
Nitrate Reductase ◽  
Malate Dehydrogenase ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Soluble Sugars ◽  
Inhibitory Effect ◽  
Wheat Roots ◽  
Cucumber Roots ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Complex Influence

At concentrations of 25 and 5 µM, simazine inhibited nitrate reductase activity in wheat and cucumber roots, respectively. It also lowered the content of soluble sugars and decreased the activities of NADH malate dehydrogenase and NADP<sup>+</sup> glucose-6-phosphate dehydrogenase. The inclusion of 50 mM glucose into the medium partially reversed the inhibitory effect of simazine on the activity of nitrate reductase in cucumber roots and slightly increased the activity of this enzyme in wheat roots These results suggest a complex influence of the herbicide on the activity of nitrate reductase: simazine lowers the level of soluble sugars in roots and decreases the activity of the dehydrogenases supplying the reduced nucleotides indispensable for reduction of nitrates.

The influence of drought stress on the development of maize seedlings and the dynamics of activity of enzymes in their tissues

2020 ◽  
Vol 02 (03) ◽  
pp. 39-42
Author(s):  
Ziyaddin Mahmud Mammadov ◽  
Naila Zahir Aliyeva
Keyword(s):  
Drought Stress ◽  
Key Words ◽  
Malate Dehydrogenase ◽  
Malic Enzyme ◽  
Maize Seedling ◽  
Maize Seedlings ◽  
Noticeable Increase ◽  
Key Words Maize ◽  
Activity Of Enzymes ◽  
Glucose 6 Phosphate Dehydrogenase

Investigated the dynamics of the activity of glucose-6-phosphate dehydrogenase (G6PDG, EC 1.1.1.49) and malate dehydrogenase decarboxylating (MDHD, malic- enzyme, EC 1.1.1.40) enzymes that play an important role in the formation of NADPH pool of cells, under drought stress. It has been established that the development of maize seedlings is accompanied by a weakening of the activity of the G6PDH and a noticeable increase in the activity of MDHD. A drought stress causes activation of both of enzymes, in particular G6PGH, both in the root and in the stem tissues of the seedlings. An increase in the concentration is accompanied by the induction of MDHD activity to a greater extent, than that of G6PDH. Key words: maize seedling, drought stress, glucose-6-phosphate dehidrogenase, malate dehydrogenase decarboxylating

TPNH GENERATION IN THE HUMAN OVARY

1965 ◽  
Vol 49 (1) ◽  
pp. 58-64 ◽  
Author(s):  
M. H. Nielson ◽  
J. C. Warren
Keyword(s):  
Life Cycle ◽  
Corpus Luteum ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Relative Activity ◽  
Human Ovary ◽  
Phosphogluconate Dehydrogenase ◽  
Glucose 6 Phosphate Dehydrogenase

ABSTRACT The endogenous activities of four major supernatant enzymes which produce TPNH (glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, malate dehydrogenase and isocitrate dehydrogenase) were quantitated in both normal and pathologic human ovarian tissues. The atrophic ovary demonstrated the lowest relative activity of the pentose shunt dehydrogenases, whereas luteinized tissues displayed the highest. During the course of its life cycle, the corpus luteum of the nonpregnant female displayed a progressive rise in isocitrate dehydrogenase and a concomitant fall in glucose-6-phosphate dehydrogenase activities. The corpus luteum of pregnancy, studied at term, demonstrated the highest levels of activity of all the four enzymes quantitated.

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