Analysis of isozymes related to energy metabolism of adult Tegillarca granosa

2007 ◽  
Vol 4 (2) ◽  
pp. 163-166
Author(s):  
Su Xiu-Rong ◽  
Lv Zhen-Ming ◽  
Li Tai-Wu ◽  
Liu Zhi-Ming ◽  
Paul K. Chien
Keyword(s):  
Energy Metabolism ◽  
Malic Enzyme ◽  
Energy Supply ◽  
Anaerobic Metabolism ◽  
Polyacrylamide Gel Electrophoresis ◽  
Pentose Phosphate ◽  
Considerable Proportion ◽  
Tegillarca Granosa ◽  
Phosphogluconate Dehydrogenase ◽  
Auxiliary Role

AbstractThe isozymes of 10 enzymes connected with energy metabolism in Tegillarca granosa were analysed by vertical polyacrylamide gel electrophoresis. Esterase and α-amylase are enzymes related to energy intake, their activities were high in the digestive gland. Malate dehydrogenase, malic enzyme, isocitrate dehydrogenase, succinate dehydrogenase, alcohol dehydrogenase, lactate dehydrogenase, 6-phosphogluconate dehydrogenase (G-6-PDH) and adenosine triphosphatase (ATPase) are enzymes related to energy metabolism. The main energy supply of T. granosa comes from aerobic respiration; anaerobic metabolism and the pentose phosphate pathway take an auxiliary role in energy metabolism. The high activity of G-6-PDH in T. granosa might mean a considerable proportion of carbohydrates metabolized through this pathway. This reaction could provide abundant NADP for metabolism in T. granosa. Compared with other shellfish, T. granosa had lower activity of ATPase, which might have some relationship with the amnicolous life and low motility of this animal.

scholarly journals Alterations in nicotinamide and adenine nucleotide systems during mixed-function oxidation of p-nitroanisole in perfused livers from normal and phenobarbital-treated rats

1977 ◽  
Vol 166 (3) ◽  
pp. 583-592 ◽  
Author(s):  
Frederick C. Kauffman ◽  
Roxanne K. Evans ◽  
Ronald G. Thurman
Keyword(s):  
Malic Enzyme ◽  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Tricarboxylic Acid Cycle ◽  
Pentose Phosphate ◽  
Phosphogluconate Dehydrogenase ◽  
Oxidation Reduction ◽  
Fructose 1,6 Bisphosphate ◽  
Tricarboxylic Acid Cycle Intermediates ◽  
Glucose 6 Phosphate Dehydrogenase

The contents of adenine nucleotides as well as steady-state concentrations of a number of glycolytic, pentose phosphate-pathway and tricarboxylic acid-cycle intermediates were measured in extracts of livers from normal and phenobarbital-treated rats that were perfused with p-nitroanisole. Metabolites were measured in livers that were freeze-clamped during periods of maximal rates of drug metabolism. Treatment of rats with phenobarbital increased rates of p-nitroanisole O-demethylation approx. fivefold. The concentrations of lactate, xylulose 5-phosphate and ribulose 5-phosphate were increased by phenobarbital treatment, whereas that of fructose 1,6-bisphosphate declined. Perfusion of livers with p-nitroanisole produced significant increases in 6-phosphogluconate and ribulose 5-phosphate in livers from phenobarbital-treated rats, but not in livers from control rats. Treatment of rats with phenobarbital caused [NADP+]/[NADPH] to change in the direction of more oxidation, as calculated from measured concentrations of 6-phosphogluconate and ribulose 5-phosphate; however, the [NADP+]/[NADPH] ratio calculated from ‘malic’ enzyme was not changed. Additions of p-nitroanisole produced a reduction of NADP+ as calculated from 6-phosphogluconate dehydrogenase activity, but did not alter the [NADP+]/[NADPH] ratio calculated from substrates assumed to be in equilibrium with ‘malic’ enzyme. Activities of both glucose 6-phosphate dehydrogenase and ‘malic’ enzyme were increased by phenobarbital treatment. NAD+ became more reduced as a result of phenobarbital treatment; however, perfusion of livers with p-nitroanisole did not cause a change in the oxidation–reduction state of this nucleotide. Concentrations of adenine nucleotides in livers were not altered significantly by treatment of rats with phenobarbital; however, a significant decline in the [ATP]/[ADP] ratio occurred during mixed-function oxidation of p-nitroanisole in livers from phenobarbital-treated rats, but not in livers from normal rats. Perfusion of livers with two other substrates for mixed-function oxidation, hexobarbital and aminopyrine, produced an increase in the [NADP+]/[NADPH] ratio calculated from ‘malic’ enzyme. In contrast with livers perfused with p-nitroanisole, there was no significant change in adenine nucleotides in livers exposed to hexobarbital or aminopyrine. Addition of 2,4-dinitrophenol (25μm) to the perfusate containing aminopyrine decreased the [ATP]/[ADP] ratio and tended to prevent the oxidation of NADPH observed with aminopyrine alone. Thus in the presence of an uncoupler of oxidative phosphorylation, NADPH generation may exceed its utilization via mixed-function oxidation.

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 Polyacrylamide-gel Electrophoresis of Enzymes during Morphogenesis of Sclerotia of Sclerotinia sclerotiorum

Microbiology ◽  
2000 ◽  
Vol 81 (1) ◽  
pp. 101-109 ◽  
Author(s):  
A. L. Wong ◽  
H. J. Willetts
Keyword(s):  
Sclerotinia Sclerotiorum ◽  
Laccase Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Krebs Cycle ◽  
Aerial Mycelium ◽  
Pentose Phosphate ◽  
Phosphogluconate Dehydrogenase ◽  
Level Of Activity ◽  
Active Laccase ◽  
Glucose 6 Phosphate Dehydrogenase

Succinate dehydrogenase (SDH) and glucose-6-phosphate dehydrogenase (Glu-6-PDH) from Sclerotinia sclerotiorum (Lib.) de Bary were moderately active in submerged mycelium while in non-sclerotial aerial mycelium arylesterase and acid phosphatase were very active. In sclerotial initials, glyceraldehyde-3-phosphate dehydrogenase (Gly-3-PDH) and SDH were at their highest level of activity, Glu-6-PDH and phosphogluconate dehydrogenase (PGDH) were moderately active, laccase activity increased markedly, and tyrosinase was detected for the first time, its activity being moderate. In young compacting sclerotia, the activities of Glu-6-PDH and PGDH increased, Gly-3-PDH and SDH showed lowered activities, and laccase activity decreased. Suppression of the glycolytic Krebs-cycle pathway and the stimulation of the pentose phosphate pathway seem important during the compaction and maturation of sclerotia. Tyrosinase may be involved in sclerotial initiation.

scholarly journals Malonyl-proteome profiles of Staphylococcus aureus reveal lysine malonylation modification in enzymes involved in energy metabolism

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Yanan Shi ◽  
Jingjing Zhu ◽  
Yan Xu ◽  
Xiaozhao Tang ◽  
Zushun Yang ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Energy Metabolism ◽  
Active Sites ◽  
Current Knowledge ◽  
Tricarboxylic Acid Cycle ◽  
Protein A ◽  
Pentose Phosphate ◽  
Post Translational Modification ◽  
Bacterial Physiology ◽  
Dihydrolipoyl Dehydrogenase

Abstract Background Protein lysine malonylation, a novel post-translational modification (PTM), has been recently linked with energy metabolism in bacteria. Staphylococcus aureus is the third most important foodborne pathogen worldwide. Nonetheless, substrates and biological roles of malonylation are still poorly understood in this pathogen. Results Using anti-malonyl-lysine antibody enrichment and high-resolution LC-MS/MS analysis, 440 lysine-malonylated sites were identified in 281 proteins of S. aureus strain. The frequency of valine in position − 1 and alanine at + 2 and + 4 positions was high. KEGG pathway analysis showed that six categories were highly enriched, including ribosome, glycolysis/gluconeogenesis, pentose phosphate pathway (PPP), tricarboxylic acid cycle (TCA), valine, leucine, isoleucine degradation, and aminoacyl-tRNA biosynthesis. In total, 31 malonylated sites in S. aureus shared homology with lysine-malonylated sites previously identified in E. coli, indicating malonylated proteins are highly conserved among bacteria. Key rate-limiting enzymes in central carbon metabolic pathways were also found to be malonylated in S. aureus, namely pyruvate kinase (PYK), 6-phosphofructokinase, phosphoglycerate kinase, dihydrolipoyl dehydrogenase, and F1F0-ATP synthase. Notably, malonylation sites were found at or near protein active sites, including KH domain protein, thioredoxin, alanine dehydrogenase (ALD), dihydrolipoyl dehydrogenase (LpdA), pyruvate oxidase CidC, and catabolite control protein A (CcpA), thus suggesting that lysine malonylation may affect the activity of such enzymes. Conclusions Data presented herein expand the current knowledge on lysine malonylation in prokaryotes and indicate the potential roles of protein malonylation in bacterial physiology and metabolism.

Metabolomic profiling of anaerobic and aerobic energy metabolic pathways in chronic obstructive pulmonary disease

2021 ◽  
pp. 153537022110088
Author(s):  
Mingshan Xue ◽  
Yifeng Zeng ◽  
Runpei Lin ◽  
Hui-Qi Qu ◽  
Teng Zhang ◽  
...  
Keyword(s):  
Chronic Obstructive Pulmonary Disease ◽  
Energy Metabolism ◽  
Pulmonary Disease ◽  
Metabolic Pathways ◽  
Energy Supply ◽  
Stable Phase ◽  
Chronic Obstructive ◽  
Obstructive Pulmonary Disease ◽  
Copd Patients ◽  
Anaerobic Energy

While there is no cure for chronic obstructive pulmonary disease (COPD), its progressive nature and the formidable challenge to manage its symptoms warrant a more extensive study of the pathogenesis and related mechanisms. A new emphasis on COPD study is the change of energy metabolism. For the first time, this study investigated the anaerobic and aerobic energy metabolic pathways in COPD using the metabolomic approach. Metabolomic analysis was used to investigate energy metabolites in 140 COPD patients. The significance of energy metabolism in COPD was comprehensively explored by the Global Initiative for Chronic Obstructive Lung Disease–GOLD grading, acute exacerbation vs. stable phase (either clinical stability or four-week stable phase), age group, smoking index, lung function, and COPD Assessment Test (CAT) score. Through comprehensive evaluation, we found that COPD patients have a significant imbalance in the aerobic and anaerobic energy metabolisms in resting state, and a high tendency of anaerobic energy supply mechanism that correlates positively with disease progression. This study highlighted the significance of anaerobic and low-efficiency energy supply pathways in lung injury and linked it to the energy-inflammation-lung ventilatory function and the motion limitation mechanism in COPD patients, which implies a novel therapeutic direction for this devastating disease.

scholarly journals The "selfish brain" hypothesis for metabolic abnormalities in bipolar disorder and schizophrenia

2012 ◽  
Vol 34 (3) ◽  
pp. 121-128 ◽  
Author(s):  
Rodrigo Barbachan Mansur ◽  
Elisa Brietzke
Keyword(s):  
Bipolar Disorder ◽  
Energy Metabolism ◽  
Energy Supply ◽  
Clinical Implications ◽  
Metabolic Abnormalities ◽  
Compensatory Mechanisms ◽  
High Prevalence ◽  
Brain Theory ◽  
The Brain ◽  
Brain Energy

Metabolic abnormalities are frequent in patients with schizophrenia and bipolar disorder (BD), leading to a high prevalence of diabetes and metabolic syndrome in this population. Moreover, mortality rates among patients are higher than in the general population, especially due to cardiovascular diseases. Several neurobiological systems involved in energy metabolism have been shown to be altered in both illnesses; however, the cause of metabolic abnormalities and how they relate to schizophrenia and BD pathophysiology are still largely unknown. The "selfish brain" theory is a recent paradigm postulating that, in order to maintain its own energy supply stable, the brain modulates energy metabolism in the periphery by regulation of both allocation and intake of nutrients. We hypothesize that the metabolic alterations observed in these disorders are a result of an inefficient regulation of the brain energy supply and its compensatory mechanisms. The selfish brain theory can also expand our understanding of stress adaptation and neuroprogression in schizophrenia and BD, and, overall, can have important clinical implications for both illnesses.

scholarly journals Glucose stimulates transcription of fatty acid synthase and malic enzyme in avian hepatocytes

1998 ◽  
Vol 274 (3) ◽  
pp. E493-E501 ◽  
Author(s):  
F. Bradley Hillgartner ◽  
Tina Charron
Keyword(s):  
Fatty Acid ◽  
High Fat Diet ◽  
Malic Enzyme ◽  
Fatty Acid Synthase ◽  
Primary Cultures ◽  
Pentose Phosphate ◽  
Mrna Abundance ◽  
Low Fat Diet ◽  
Low Carbohydrate

Transcription of fatty acid synthase (FAS) and malic enzyme (ME) in avian liver is low during starvation or feeding a low-carbohydrate, high-fat diet and high during feeding a high-carbohydrate, low-fat diet. The role of glucose in the nutritional control of FAS and ME was investigated by determining the effects of this metabolic fuel on expression of FAS and ME in primary cultures of chick embryo hepatocytes. In the presence of triiodothyronine, glucose (25 mM) stimulated an increase in the activity and mRNA abundance of FAS and ME. These effects required the phosphorylation of glucose to glucose 6-phosphate but not further metabolism downstream of the aldolase step of the glycolytic pathway. Xylitol mimicked the effects of glucose on FAS and ME expression, suggesting that an intermediate of the pentose phosphate pathway may be involved in mediating this response. The effects of glucose on the mRNA abundance of FAS and ME were accompanied by similar changes in transcription of FAS and ME. These data support the hypothesis that glucose plays a role in mediating the effects of nutritional manipulation on transcription of FAS and ME in liver.

scholarly journals The pentose phosphate pathway in Trypanosoma cruzi: a potential target for the chemotherapy of Chagas disease

2007 ◽  
Vol 79 (4) ◽  
pp. 649-663 ◽  
Author(s):  
Mariana Igoillo-Esteve ◽  
Dante Maugeri ◽  
Ana L. Stern ◽  
Paula Beluardi ◽  
Juan J. Cazzulo
Keyword(s):  
Oxidative Stress ◽  
Trypanosoma Cruzi ◽  
Pentose Phosphate Pathway ◽  
Single Copy ◽  
Pentose Phosphate ◽  
Site Directed Mutagenesis ◽  
Haploid Genome ◽  
Salt Bridges ◽  
Phosphogluconate Dehydrogenase ◽  
Genes Encoding

Trypanosoma cruzi is highly sensitive to oxidative stress caused by reactive oxygen species. Trypanothione, the parasite's major protection against oxidative stress, is kept reduced by trypanothione reductase, using NADPH; the major source of the reduced coenzyme seems to be the pentose phosphate pathway. Its seven enzymes are present in the four major stages in the parasite's biological cycle; we have cloned and expressed them in Escherichia coli as active proteins. Glucose 6-phosphate dehydrogenase, which controls glucose flux through the pathway by its response to the NADP/NADPH ratio, is encoded by a number of genes per haploid genome, and is induced up to 46-fold by hydrogen peroxide in metacyclic trypomastigotes. The genes encoding 6-phosphogluconolactonase, 6-phosphogluconate dehydrogenase, transaldolase and transketolase are present in the CL Brener clone as a single copy per haploid genome. 6-phosphogluconate dehydrogenase is very unstable, but was stabilized introducing two salt bridges by site-directed mutagenesis. Ribose-5-phosphate isomerase belongs to Type B; genes encoding Type A enzymes, present in mammals, are absent. Ribulose-5-phosphate epimerase is encoded by two genes. The enzymes of the pathway have a major cytosolic component, although several of them have a secondary glycosomal localization, and also minor localizations in other organelles.

scholarly journals Activity of Energy and Carbohydrate Metabolism Enzymes in the Juvenile Pink Salmon Oncorhynchus gorbuscha (Walb.) during the Transition from Freshwater to a Marine Environment

2021 ◽  
Vol 48 (5) ◽  
pp. 546-554
Author(s):  
M. V. Churova ◽  
N. S. Shulgina ◽  
M. Yu. Krupnova ◽  
D. A. Efremov ◽  
N. N. Nemova
Keyword(s):  
Carbohydrate Metabolism ◽  
Marine Environment ◽  
Pentose Phosphate Pathway ◽  
Anaerobic Metabolism ◽  
Pink Salmon ◽  
Atp Synthesis ◽  
Pentose Phosphate ◽  
Oncorhynchus Gorbuscha ◽  
Biochemical Adaptation ◽  
Metabolism Enzymes

Abstract Biochemical adaptations of energy metabolism and some pathways of glucose oxidation during a change in salinity of the environment in larvae and smolts of the pink salmon Oncorhynchus gorbuscha (Walb.) inhabiting the White Sea were studied. We assayed the activity of energy and carbohydrate metabolism enzymes (cytochrome c oxidase (COХ), lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G6PDH), 1-glycerophosphate dehydrogenase (1-GPDH), and aldolase) in pink salmon larvae in a short-term aquarium experiment and in pink salmon smolts in a long-term cage experiment simulating the transition of juveniles from freshwater to a marine environment. A decrease in the activity of COX, LDH, 1‑GPDH, and aldolase already in the first hour after the transfer of larvae to seawater was shown. Smolts kept in the estuary and in the sea had low levels of activity of 1-GPDH and aldolase in comparison with individuals from the river. Most likely, in the salmon juveniles studied, there was a redistribution of carbohydrates between the reactions of aerobic and anaerobic metabolism in favor of anaerobic ATP synthesis. No changes in the enzyme activity of the pentose phosphate pathway, G-6-PDH, were found in either larvae or smolts compared with the individuals kept in freshwater. Maintenance of the required levels of anaerobic metabolism and of the pentose phosphate pathway is probably one of the mechanisms of biochemical adaptation of pink salmon to changes in salinity.

scholarly journals Purification and properties of 6-phosphogluconate dehydrogenase from sheep liver

1969 ◽  
Vol 115 (4) ◽  
pp. 639-643 ◽  
Author(s):  
R. H. Villet ◽  
K. Dalziel
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sedimentation Velocity ◽  
Sedimentation Equilibrium ◽  
Equilibrium Studies ◽  
Phosphogluconate Dehydrogenase ◽  
Sheep Liver ◽  
Equilibrium Sedimentation ◽  
Purification And Properties

A method is described for the isolation of 6-phosphogluconate dehydrogenase from sheep liver. The product appears to be homogeneous in polyacrylamide-gel electrophoresis and in sedimentation-velocity and sedimentation-equilibrium studies in the ultracentrifuge. The molecular weight is estimated as 129000 from equilibrium sedimentation.

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