Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.4.1.2 (glutamate dehydrogenase)
4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The enzyme pattern of Saccharomyces cerevisiae was followed during batch growth and in continuous culture in a synthetic medium limited for glucose under aerobic conditions. Seven enzymes were measured: succinate-cytochrome c oxidoreductase, malate dehydrogenase, nicotinamide adenine dinucleotide-linked glutamate dehydrogenase, malate synthase, isocitrate lyase, aldolase, and nicotinamide adenine dinucleotide phosphate (NADP(+))-linked glutamate dehydrogenase. During fermentation of glucose and high growth rate (mu) during the first log phase in batch experiments, the first five enzymes (group I) were repressed, and aldolase and NADP(+)-linked glutamate dehydrogenase (group II) were derepressed. During growth on the accumulated ethyl alcohol and lower mu, the group I enzymes were preferentially formed and the other two were repressed. A sequence of derepression of the group I enzymes was found during the shift from glucose to ethyl alcohol metabolism, which can be correlated with a strong increase in the percentage of single (nonbudding) cells in the population. A correlation between the state of cells in the budding cycle and enzyme repression and derepression is suggested. In continuous culture, the enzyme pattern was shown to be related to the growth rate. The group I enzymes were repressed at high growth rates, while the group II enzymes were derepressed. Each enzyme exhibits a different dependence. The enzyme pattern is shown to depend on the rate of substrate consumption as well as on the type of metabolism and to be correlated with the budding cycle. The enzyme pattern is considered to be controlled by changes of intracellular catabolic or metabolic conditions inherent in the division cycle.
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PMID:Enzyme pattern and aerobic growth of Saccharomyces cerevisiae under various degrees of glucose limitation. 438 90

Changes in the activity of 13 enzymes are described in the process of cytodifferentiation of the nerve cells of spinal ganglion, the motor neurons of spinal cord and large nerve cells of the III layer of tectum opticum in 7, 10 and 21 day old chick embryos. Cytophotometry was performed with MZFV-1 (LOMO) by means of plug-method. A relatively high activity of glucose-6-phosphat dehydrogenase, diaphorase, alpha-glycerophosphate dehydrogenase and, partially, acetylcholine esterase was found already in the 7 days old embryo. The activity of monoamine oxidase, aldolase-glyceroaldehyde phosphate dehydrogenase, isocitrate dehydrogenase, glutamate dehydrogenase increased markedly on the 21st day. When studying the reciprocal distribution of two enzymes in separate cells, pairs of enzymes with a high value of correlation coefficient were found. The cytodifferentiation was found to be accompanied by changes in the coefficient of correlation of the same pair of enzymes.
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PMID:[Enzymes in the process of neuronal differentiation of the hen spinal ganglion, spinal cord and tectum opticum. A cytophotometric histochemical study]. 683 47

Two sensitive assays, one which fluorometrically measures only the L isomer of 2-keto-4-hydroxyglutarate after decarboxylation to L-malate and the other which spectrophotometrically determines both enantiomers by reductive amination with glutamate dehydrogenase, are described. By use of these assays, the steady-state kinetics of the aldol condensation of pyruvate with glyoxylate, as catalyzed by 2-keto-4-hydroxyglutarate aldolase from either bovine liver or Escherichia coli, were studied as was the inhibition of this reaction by glyoxylate and other anions. For the E. coli aldolase, double-reciprocal plots are linear except at high (above 5 mM) glyoxylate concentrations; apparent Km values increase with increasing concentrations of the fixed substrate. The data are consistent with an ordered reaction sequence. Inhibition by halides follows the lyotropic or Hofmeister series. Esters are not good inhibitors; mono-, di-, and tricarboxylic acids are increasingly inhibitory. Of the substrate analogues tested, hydroxypyruvate is the most potent inhibitor. Inhibition studies with citrate, acetaldehyde, and glyoxylate (all competitive inhibitors) suggest there are two domains at the active site-the Schiff base forming lysyl residue which interacts with carbonyl analogues (like acetaldehyde) and a center of positive charge which binds anions (like citrate). In contrast to the bacterial enzyme, liver 2-keto-4-hydroxyglutarate aldolase is inhibited in a competitive manner by much lower concentrations (0.1 mM or even lower) of glyoxylate. Many salts and some carboxylic acids activate the liver enzyme. Similarly, substrate analogues like 2-ketobutyrate and fluoropyruvate are mild activators; no effect is seen with acetaldehyde. Besides glyoxylate, only glyoxal, 2-ketoglutarate, and hydroxypyruvate inhibit the aldol condensation reaction. A uniform value of 1 is found for the number of inhibitor molecules bound per active site of either liver or E. coli 2-keto-4-hydroxyglutarate aldolase.
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PMID:Steady-state kinetics and inhibition studies of the aldol condensation reaction catalyzed by bovine liver and Escherichia coli 2-keto-4-hydroxyglutarate aldolase. 701 77

Activities of 14 enzymes were determined in psoas muscle, smooth muscle, diaphragm, heart, brain, liver, kidney, spleen, pancreas, salivary glands, zygomatic gland, intestinal mucosa, subcellular fractions, and plasma of the dog. In pups, plasma activity of most enzymes was high, except iditol dehydrogenase (ID), glutamate dehydrogenase (GLD), alanine aminotransferase (ALT), aspartate aminotransferase (AST), and D-fructose-1,6-diphosphate aldolase (ALS). Alkaline phosphatase (ALP), ALS, cholinesterase (CHS), creatine kinase (CK), alpha-hydroxybutyrate dehydrogenase (HBD), lactate dehydrogenase (LD), and malate dehydrogenase (MD) decreased significantly (P less than 0.01) with increasing age, but in dogs greater than 7 months, all enzymes except CK, HBD, and ALT revealed reasonably constant plasma values. Enzymes ALT, GLD, CHS, and ID are specific for liver, CK and ALS for muscle, HBD to some degree for myocardium, and alpha-amylase for pancreas. The ALP and gamma-glutamyltransferase were located in microsomes, GLD in mitochondria, MD and AST in mitochondria and cytoplasm, and isocitric dehydrogenase, LD, and the other enzymes only in cytoplasm.
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PMID:Enzyme activities in the dog: tissue analyses, plasma values, and intracellular distribution. 703 2

During a long-term study in the rat some enzyme activities were determined in plasma, lung, spleen and skeletal muscle. Twelve rats of each sex were investigated every 49 days from 35 until 1115 days of life. Lactate dehydrogenase in lung and spleen decreases; in muscle and plasma, however, the activity varies considerably. Malate dehydrogenase in the tissues remains nearly unchanged apart from distinct peaks in the first year of life; in plasma the activity takes an M-shaped course. In contrast to the changes of glutamate dehydrogenase in the tissues with a tendency to diminish, this enzyme increases in plasma during the lifetime. Aspartate aminotransferase activity in the tissues, except muscle, varies with a rhythmical behaviour, and in plasma shows a gradual increase. Alanine aminotransferase in lung and spleen has two activity peaks. In muscle this enzyme varies only slightly after a steep initial decrease. In plasma the activity has a tendency to rise. Creatine kinase in the tissues reveals several activity peaks. In plasma the activity course is U-shaped. Adenylate kinase in spleen and lung rises, whereas in muscle the activity varies considerably. The nearly identical decrease of alkaline phosphatase activity in the tissues during ageing is also reflected by a concomitant behaviour in plasma. Leucine arylamidase in lung and muscle both have a U-shaped characteristic, whereas in spleen the activity changes in a shorter period. In plasma, a rhythmical behaviour is apparent. Aldolase in plasma tripled during the observation period. Except for lactate dehydrogenase and aldolase, distinct sex-differences are observed in plasma. With progressive age the animals suffer increasingly from characteristic diseases, which beside experimental components have influenced the enzyme pattern. Enzyme activities in plasma and tissues show a complex pattern and are only of limited importance in understanding the ageing process.
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PMID:Long-term observation of plasma and tissue enzyme activities in the rat. 720 25

The activities of 13 liver and 6 brain enzymes were studied in 7-12 week old CD2F1 male mice that had been fed ad libitum and standardized either to 12 hours of light (0600-1800) alternating with 12 hours of darkness (1800-0600) (LD12:12); or to a reversed light-dark cycle (darkness 0600-1800; light 1800-0600) (DL12:12). Three separate studies were performed on two different days; in each experiment, subgroups of 14 animals were sacrificed at 3-hour intervals. Livers were assayed for: isocitrate dehydrogenase, glutamate dehydrogenase, lactate dehydrogenase, alcohol dehydrogenase, glutathione reductase, glyoxylate reductase, L-alanine aminotransferase, glutamate oxalacetate transaminase, pyruvate decarboxylase, fructose-1-phosphate aldolase, fructose diphosphate aldolase, fructose 1,6-diphosphatase, and fatty acid synthetase. Brains were assayed for phosphoglucose isomerase, adenosine triphosphatase, creatine phosphokinase, pyruvate kinase, adenylate kinase, and malate dehydrogenase. All 19 enzymes demonstrated a prominent circadian rhythm in at least one experiment. Moreover, each rhythmic variable showed a statistically significant fit to a 24-hour cosine (sine) curve by the method of least squares. In general, peak activities of the liver enzymes analyzed were associated with the beginning of the dark cycle and initiation of the animal's activity, while the group of brain enzymes had peak activities which occurred at the beginning of the animals' rest span and were near the beginning of the light cycle. The phasing of each of the rhythms could be reversed within a two-week span after reversing the environmental light-dark cycle 180 degrees.
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PMID:Circadian organization of thirteen liver and six brain enzymes of the mouse. 731 49

The internal amino acid residues of proteins are almost always non-polar since the hydrophobic effect is very important in stabilizing the three-dimensional structure. This fact suggests several new criteria for judging the correctness of structures predicted from sequence data. The dinucleotide binding domain has been used as a test structure for these criteria. The percentage of ionic residues, mutation data, hydrophobicity, dipole moments, and internal preferences of the residues on the interiors of the known dinucleotide binding folds are consistent with expectations. On the other hand, the values of these parameters for predicted domains in glutamate dehydrogenase (Wootton, J.C. (1974) Nature 252, 542--546) and aldolase (Stellwagen, E. (1976) J. Mol. Biol. 106, 903--911) differ significantly from the expected values indicating that these predictions are not entirely correct. The internal residue criteria can then be used to test modifications of the predictions for a better correlation with the internal residue pattern of the domain.
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PMID:Internal residue criteria for predicting three-dimensional protein structures. 737 53

Mature mitochondrial proteins (aspartate aminotransferase, malate dehydrogenase, hydroxyacyl coenzyme A dehydrogenase, creatine kinase) and cytosolic proteins (aldolase, glyceraldehyde-3-phosphate dehydrogenase) with a basic pI were found to bind to isolated mitochondria, electrostatic interactions being mainly responsible for their binding. Mitochondrial aspartate aminotransferase bound with a Kd' of 30 nM in 0.6 M sorbitol, 20 mM Hepes/KOH, pH 7.4, at 25 degrees C. Cytosolic aspartate aminotransferase and glutamate dehydrogenase (a protein located in the mitochondrial matrix) both with an acidic pI, did not bind to mitochondria. Treatment of mitochondria with proteinases did not affect the subsequent binding of imported mitochondrial proteins. Their association with both intact and proteinase-treated mitochondria resulted in a marked increase in their susceptibility toward proteinase K. In contrast, the basic cytosolic proteins tested bound only to intact mitochondria and thereby did not become more susceptible toward proteolytic attack. Treatment of mitochondria with adriamycin, a drug binding to acidic phospholipids, prevented the subsequent association of mitochondrial aspartate aminotransferase with mitochondria and the ensuing conformational labilization. Apparently, the mature moiety of imported mitochondrial proteins is partially unfolded upon interaction with the lipid component of the mitochondrial envelope. Both the binding of the mitochondrial proteins and their conformational labilization is independent of ATP and the electrochemical potential across the inner membrane.
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PMID:The mature form of imported mitochondrial proteins undergoes conformational changes upon binding to isolated mitochondria. 828 42

The pregnant rats were treated with formaldehyde (0.5 mg/kg daily per os) during whole period of pregnancy. The activity of cytochrome-c-oxidase, malate dehydrogenase, nucleotidase, glucose-6-phosphatase, beta-glucuronidase, N-acetyl-beta-glucosaminidase, beta-galactosidase, H(+)-ATPase, glutamate dehydrogenase, NAD- and NADP-isocitrate dehydrogenase, fructose-bisphosphate aldolase, glucose-6-phosphate dehydrogenase and content of protein in liver celts of offsprings (newborns, 2 weeks age and 2 months age) were studied. It was shown differences in development enzyme systems of control and experimental animals during ontogenesis.
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PMID:[Experimental study of the effect of formaldehyde during embryogenesis on the activity of rat liver enzyme systems in ontogenesis]. 913 53

The compartmentation of key processes in sugar, organic acid and amino acid metabolism was studied during the development of the flesh and seeds of grape (Vitis vinifera L.) berries. Antibodies specific for enzymes involved in sugar (cell wall and vacuolar invertases, pyrophosphate: fructose 6-phosphate phosphotransferase, aldolase, NADP-glyceraldehyde-P dehydrogenase, cytosolic fructose 1,6-bisphosphatase), photosynthesis (Rubisco, fructose 1,6-bisphosphatase, sedoheptulose 1,7-bisphosphatase), amino acid metabolism (cytosolic and mitochondrial aspartate aminotransferases, alanine aminotransferase, glutamate dehydrogenase, glutamine synthetase), organic acid metabolism (phosphoenolpyruvate carboxylase, NAD- and NADP-dependent malic enzyme, ascorbate peroxidase), and lipid metabolism (acetyl CoA carboxylase, isocitrate lyase) were used to determine how their abundance changed during development. There were marked changes in the abundance of many of these enzymes in both the flesh and seeds. The intercellular location of some enzymes was investigated using immunohistochemistry. Several enzymes (e.g. phosphoenolpyruvate carboxylase and those involved in amino acid metabolism) were associated with tissues likely to function in the transport of imported assimilates, such as the vasculature. Although other enzymes (e.g. NADP-malic enzyme and soluble acid invertase, involved in the metabolism of sugars and organic acids) were largely present in the parenchyma cells of the flesh, their distribution was extremely heterogeneous. This study shows that when considering the metabolism of complex structures such as fruit, it is essential to consider how metabolism is compartmentalized between and within different tissues, even when they are apparently structurally homogeneous.
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PMID:An immunohistochemical study of the compartmentation of metabolism during the development of grape (Vitis vinifera L.) berries. 1093 59


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