TY - JOUR. T1 - Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. AU - Smith, Thomas. AU - Peterson, Peter E.. AU - Schmidt, Timothy. AU - Fang, Jie. AU - Stanley, Charles A.. PY - 2001/3/23. Y1 - 2001/3/23. N2 - Glutamate dehydrogenase is found in all organisms and catalyses the oxidative deamination of L-glutamate to 2-oxoglutarate. However, only animal GDH utilizes both NAD(H) or NADP(H) with comparable efficacy and exhibits a complex pattern of allosteric inhibition by a wide variety of small molecules. The major allosteric inhibitors are GTP and NADH and the two main allosteric activators are ADP and NAD+. The structures presented here have refined and modified the previous structural model of allosteric regulation inferred from the original boGDH·NADH·GLU·GTP complex. The boGDH·NAD+·α-KG complex structure clearly demonstrates that the second coenzyme-binding site lies directly under the "pivot helix" of the NAD+ binding domain. In ...
TY - JOUR. T1 - Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. AU - Fang, Jie. AU - Hsu, Betty Y L. AU - MacMullen, Courtney M.. AU - Poncz, Mortimer. AU - Smith, Thomas. AU - Stanley, Charles A.. PY - 2002/4/1. Y1 - 2002/4/1. N2 - Glutamate dehydrogenase (GDH) catalyses the reversible oxidative deamination of L-glutamate to 2-oxoglutarate in the mitochondrial matrix. In mammals, this enzyme is highly regulated by allosteric effectors. The major allosteric activator and inhibitor are ADP and GTP, respectively; allosteric activation by leucine may play an important role in amino acid-stimulated insulin secretion. The physiological significance of this regulation has been highlighted by the identification of children with an unusual hyperinsulinism/hyperammonaemia syndrome associated with dominant mutations in GDH that cause a loss in GTP inhibition. In order to determine the effects of these mutations on the function of the ...
Variations in ambient temperature are a common phenomenon in nature that influences the microbial growth and metabolism. Temperature drops modifies the molecular topology, the enzyme kinetics, and increases the molecular order of membrane lipids [1, 2], affecting key cellular processes as transcription, translation and membrane-associated activities [3]. Cold is also relevant for the industrial exploitation of microorganisms. Processes involving yeasts, like brewing and some wine fermentations, take place at temperatures around 10-12°C, which is far below the optimal temperature of this organism (~28°C). Therefore, understanding the mechanisms of cold survival and adaptation is of great interest for both basic and applied aspects.. The essential coenzymes nicotinamide adenine dinucleotides, NAD and NADP, participate in key redox reactions and contribute to maintaining cell fitness and genome stability [4]. Factors regulating their metabolism and homeostasis become thus crucial in providing ...
ab Glutamate Dehydrogenase Detection Kit Instructions for Use For the rapid, sensitive and accurate measurement of Glutamate Dehydrogenase activity in various samples This product is for research
Glutamate dehydrogenase (GLDH, GDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Glutamate dehydrogenase also has a very low affinity for ammonia (high Michaelis constant K m {\displaystyle K_{m}} of about 1 mM), and therefore toxic levels of ammonia would have to be present in the body for the reverse reaction to proceed (that is, α-ketoglutarate and ammonia to glutamate and NAD(P)+). However, in brain, the NAD+/NADH ratio in brain mitochondria encourages oxidative deamination (i.e. α-ketoglutarate to glutamate). In bacteria, the ammonia is assimilated to amino acids via glutamate and ...
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[114 Pages Report] Check for Discount on China Glutamate Dehydrogenase Market Research Report 2017 report by QYResearch Group. The global Glutamate Dehydrogenase market is valued at XX million...
Glutamate has been shown to lead to neurotoxicity and subsequent neurodegeneration through changes in synaptic function, loss of glutamatergic neurons, synapses, and dendrites. All of these characteristics are also observed during aging or in age-associated neurodegenerative diseases. To probe the effects of excess glutamate and determine if these effects might contribute to the morphological and functional changes associated with aging, our laboratory generated a transgenic mouse model that over-expresses the mitochondrial glutamate dehydrogenase 1 (GLUD1) gene. This transgene was only expressed in neurons through the use of the neuron-specific enolase promoter. The Glud1 Tg mouse model generated in our laboratory demonstrated significantly increased GLUD1 levels, GLUD activity, extracellular glutamate levels, and increased glutamate release after stimulation as compared to wild type (wt). There were also many significant morphological changes observed in the Tg mice including cell layer ...
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Aravind, L., R. L. Tatusov, Y. I. Wolf, D. R. Walker, and E. V. Koonin. 1998. Evidence for massive gene exchange between archaeal and bacterial hyperthermophiles. Trends in Genetics 14:442-444.. Baldauf, S. L., J. D. Palmer, and W. F. Doolittle. 1996. The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny. Proceedings of the National Academy of Sciences of the United States of America 93:7749-7754.. Becerra, A., L. Delaye, S. Islas, and A. Lazcano. 2007. The very early stages of biological evolution and the nature of the last common ancestor of the three major cell domains. Annual Review of Ecology, Evolution, and Systematics 38:361-379.. Benachenhou, L. N., P. Forterre and B. Labedan. 1993. Evolution of glutamate dehydrogenase genes: Evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life. Journal Of Molecular Evolution 36:335-346.. Brinkmann, H. and H. Phillippe. 1999. Archaea ...
The purification of glutamate dehydrogenase from sheep rumen mucosa on DEAE-cellulose afforded two enzyme fractions with glutamate dehydrogenase activity. The enzyme fraction II (tissue glutamate dehydrogenase) was freed of contaminating proteins in the subsequent purification step on Sephadex G-200. The approximate relative molecular weight (260 000) of tissue glutamate dehydrogenase (fraction II) was determined by gel filtration on Sephadex G-200 and the approximate relative molecular weight of its polypeptide chain (48 000) was established by polyacrylamide gel electrophoresis in SDS. The pH-optimum of fraction II was 7.9. The effect of substrate concentration on the rate of the enzymatic reaction was examined and the following apparent Michaelis constants were found for the individual substrates: NADH 6.25 . 10-5 mol/l, 2-oxoglutarate 4.5 . 10-3 mol/l, and NH4+ 77 . 10-3 mol/l.. ...
Two pathways serve for assimilation of ammonia inParacoccus denitrificans. Glutamate dehydrogenase (NADP+) catalyzes the assimilation at a high NH4+ concentration. If nitrate serves as the nitrogen source, glutamate is synthesized by glutamate-ammonia ligase and glutamate synthase (NADPH). At a very low NH4+ concentration, all three enzymes are synthesized simultaneously. No direct relationship exists between glutamate dehydrogenase (NADP+) and glutamate-ammonia ligase inP. denitrificans, while the glutamate synthase (NADPH) activity changes in parallel with that of the latter enzyme. Ammonia does not influence the induction or repression of glutamate dehydrogenase (NADP+). The inner concentration of metabolites indicates a possible repression of glutamate dehydrogenase (NADP+) by the high concentration of glutamine or its metabolic products as in the case when NH4+ is formed by assimilative nitrate reduction. No direct effect of the intermediates of nitrate assimilation on the synthesis of glutamate
A simple and rapid method is described for the determination of ammonia in plasma without deproteinization, using the enzyme glutamate dehydrogenase and NADPH as coenzyme. ADP is used to stabilize glutamate dehydrogenase. The measuring principle is a kinetic one, determining the reaction rate on the "Enzyrator". The whole determination takes only ... read more 7 min, including the preincubation time. The plasma sample is only 100 μl, which makes it possible to determine the ammonia values in capillary blood. Comparing the values of venous and capillary blood, we found that capillary values are 2-3 times higher than those in venous blood. The normal range for venous plasma NHs was 6.5-35.0 μmol/l. The mean value of non-fasting persons was 22.0 μmol/l. show less ...
1. Abounit S, Bousset L, Loria F, Zhu S, de Chaumont F, Pieri L. Tunneling nanotubes spread fibrillary α-synuclein by intercellular trafficking lysosomes. EMBO J. 2016. 35: 2120-38. 2. Alam Q, Alam MZ, Mushtaq G, Damenhouri GA, Rasool M, Kamai MA, Haque A. Inflammatory process in Alzheimers and Parkinsons diseases: Central role of cytokines. Curr Pharm Des. 2016. 22: 541-8. 3. Allan SM, Rothwell NJ. Cytokines and acute neurodegeneration. Nat Rev Neurosci. 2001. 2: 734-44. 4. Alvarez-Erviti L, Couch Y, Richardson J, Cooper JM, Wood MJ. Alpha-synuclein released by neurons activate the inflammatory response in microglial cell line. Neurosci Res. 2011. 69: 337-42. 5. Ambrosi G, Cerri S, Blandini F. A further update of excitotoxicity in the pathogenesis of Parkinsons disease. J Neural Transm. 2014. 121: 849-59. 6. Aquirre J, Rodriguez R, Hansberg W. Oxidation of Neurospora crassa NADP-specific glutamate dehydrogenase by activated oxygen species. J Bacteriol. 1989. 17: 6243-50. 7. Assous M, ...
EC 1.4.1.4; systematic name: l‐glutamate:NADP+ oxidoreductase (deaminating). An enzyme that catalyses the oxidation by NADP+ of l‐glutamate to form 2‐oxoglutarate, NH3, and NADPH. Two forms exist. One is a homotetramer. ... ...
A negative result for GDH has been associated with a high value for prediction of a true negative result; however, a positive result is not necessarily associated with a toxin producing strain. A second assay on positive samples for detection of toxin production is required in these algorithms ...
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What does SLC25A22 do? Mitochondria are the cellular energy plant of the cell, and molecular transport is tightly regulated at both the outer and inner mitochondrial membrane. SCL25A22, also known as GC1, is the main glutamate transporter across the inner mitochondrial membrane. Why do the mitochondria need glutamate? Glutamate plays an important role in fuelling both the Krebs cycle and urea cycle, and impairment of glutamate import may have a devastating effect on the energy homeostasis of the cell. As demonstrated by the catastrophic epilepsy arising from SLC25A22 deficiency, the effect is particularly damaging in the developing nervous system where SLC25A22 is highly expressed. However, it remains to be shown whether the effect of recessive SLC25A22 mutations actually result in mitochondrial glutamate starvation.. The SLC25A22 phenotype. Recessive mutations in SCL25A22 were previously described in a family with neonatal epileptic encephalopathy with suppression bursts (NEESB), cerebellar ...
Hi, I have a mouse anti-bovine glutamate dehydrogenase mAb and Im curious whether anyone would know whether it will crossreact with Human GDH. I think the two proteins are fairly similiar but how similiar are humans with cows??? Please send a reply to my E-mail dsho at med.unc.edu Thanx for any thoughts. Moo Moo, Dave Shock ...
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Hayakawa Toshihiko , Sakai Takahiro , Ishiyama Keiki , HIROSE Naoya , NAKAJIMA Hiroyuki , TAKEZAWA Masae , NAITO Kazutaka , HINO-NAKAYAMA Mutsumi , AKAGAWA Takumi , GOTO Satoshi , YAMAYA Tomoyuki Plant biotechnology 20(1), 43-55, 2003-03-03 J-STAGE 参考文献37件 被引用文献2件 ...
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Nitrogen assimilation during growth of Candida boidinii on methylated amines as sole nitrogen source involves NADP-dependent glutamate dehydrogenase. Changes in enzyme activities during the adaptation of the yeast from growth on ammonium to growth on trimethylamine were examined. No ammonia, dimethylamine or monomethylamine could be detected in the medium during growth on trimethylamine. When two methylated amines were supplied together, they were used simultaneously, although monomethylamine was metabolized more quickly than the others. When cells were grown on a low concentration of ammonium plus higher concentrations of di- or trimethylamine, the ammonium was used first. NADP-dependent glutamate dehydrogenase was the first enzyme to be derepressed, followed by methylamine oxidase and formaldehyde dehydrogenase. Di- and trimethylamine mono-oxygenase activities only appeared when the ammonium concentration fell below 0.5 mM. At this point amine utilization could be detected and no diauxic lag was
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Low concentrations of hexachlorophene (HCP) inhibit a number of pyridine nucleotide-linked dehydrogenase enzymes. The I₅₀ HCP concentrations were 105 μM for pig heart isocitrate dehydrogenase (ICD), 65 μM for horse liver alcohol dehydrogenase, 39 μM for torula yeast glucose-6-phosphate dehydrogenase (G6PD), 6.0 μM for beef heart malate dehydrogenase, and 1.6 μM for bovine liver glutamate dehydrogenase (GDH) at the enzyme concentrations tested. HCP exhibited cooperative inhibition of these enzymes since the observed maximum interaction coefficient, n, between HCP binding sites ranged between 1.62 and 3.33 but it was not an allosteric effector as evidenced by Hill coefficients for the substrates of approximately 1.0 both in the absence and the presence of HCP. More detailed kinetic analysis showed that HCP in most cases exhibited mixed kinetics, giving average K[subscript i] values with G6PD of 16.6 μM for NADP⁺ and 18.2 μM for glucose -6- phosphate; with ICD of 171 µM for NADP⁺ ...
NADP-linked glutamate dehydrogenase (NADP+-GluDH, EC 1.4.1.4) has been purified to homogeneity from epimastigotes of Trypanosoma cruzi by an improved procedure, and the amino acid sequences of 11 internal peptides obtained by digestion with trypsin, endopeptidase Lys-C, endopeptidase Arg-C or CNBr have been obtained. Using oligonucleotide primers synthesized according to the amino acid sequence of the N-terminus of the mature enzyme and to the nucleotide sequence of a clone corresponding to the C-terminus, obtained by immunological screening of an expression library, two complete open reading frames (TcGluDH1 and TcGluDH2) were isolated and sequenced. The sequences obtained are most similar to that of the NADP+-GluDH of Escherichia coli (70-72% identity), and less similar (50-56%) to those of lower eukaryotes. Using TcGluDH1 as a probe, evidence for the presence of several genes and developmental regulation of the expression of NADP+-GluDH in different parasite stages was obtained. TcGluDH1 ...
The stability of two enzymes from extreme thermophiles (glutamate dehydrogenase from Thermococcales strain AN1 and beta-glucosidase from Caldocellum saccharolyticum expressed in Escherichia coli) has been exploited to allow measurement of activity over a 175 degrees C temperature range, from +90 degrees C to -85 degrees C for the glutamate dehydrogenase and from +90 degrees C to -70 degrees C for the beta-glucosidase. The Arrhenius plots of these enzymes, and those for two mesophilic enzymes (glutamate dehydrogenase from bovine liver and beta-galactosidase from Escherichia coli), exhibit no downward deflection corresponding to the glass transition, found by biophysical measurements of several non-enzymic mesophilic proteins at about -65 degrees C and reflecting a sharp decrease in protein flexibility as the overall motion of groups of atoms ceases. ...
Moreover, while most of the organs in the human body have the ability to store glucose by increasing their mass, the brain, prisoner of the cranial bones, cannot count on these variations in volume.. Unable to store its food, it depends on sugar supplied in real-time by the rest of the body. This distribution of energy is controlled by the liver.. Pierre Maechler, professor at the Faculty of Medicine at UNIGE, and his team therefore decided to verify if glutamate was indeed an energy source for the brain.. To do so, the researchers analyzed the role of the glutamate dehydrogenase enzyme in the brain. In mutant form, this enzyme, encoded by the Glud1 gene, is responsible for a congenital hyperinsulinism syndrome, a severe disease affecting at the same time the endocrine pancreas, the liver and the brain.. Individuals affected by this syndrome suffer from intellectual disability and have a high risk of epilepsy. ...
Recombinant protein of human glutamate decarboxylase 2 (pancreatic islets and brain, 65kDa) (GAD2), transcript variant 2, 20 ug available for purchase from OriGene - Your Gene Company.
Lenti ORF particles, GRIK2 (Myc-DDK tagged) - Human glutamate receptor, ionotropic, kainate 2 (GRIK2), transcript variant 2 , 200ul, >10^7 TU/mL ...
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Question: Does Cialis lower blood pressure? Answer: Cialis can lead to drop in blood pressure and at times to unsafe levels. It works by
Methylobacterium extorquens ATCC ® 14718™ Designation: NCIB 9133 TypeStrain=False Application: Produces glutamate dehydrogenase (NADP+) NADP+-dependent glutamate dehydrogenase, glutamate dehydrogenase (NADP-dependent) Biotechnology
Methylobacterium extorquens ATCC ® 14718™ Designation: NCIB 9133 TypeStrain=False Application: Produces glutamate dehydrogenase (NADP+) NADP+-dependent glutamate dehydrogenase, glutamate dehydrogenase (NADP-dependent) Biotechnology
Glutamate dehydrogenase (GDH) is a key enzyme that links amino acid and carbohydrate metabolism in cells. Regulation is likely most important when organisms are confronted with extreme stresses such as the low environmental temperatures and lack of food associated with winter. Many small mammals, such as Richardsons ground squirrels, Spermophilus richardsonii, cope with these conditions by hibernating. Animals enter long periods of profound torpor where metabolic rate is greatly suppressed, body temperature drops to near-ambient and all metabolic needs must be met from fixed internal body stores of fuels. To investigate how GDH is regulated under these conditions, kinetic properties of GDH were analyzed in liver from euthermic and torpid squirrels, revealing significant differences in Vmax, Km glutamate, Ka ADP and inhibition by urea between the two forms of GDH. These data suggested an activation of the glutamate-oxidizing activity of GDH in the hypometabolic state. Subsequent experiments ...
Oxoglutaric acid, also known as oxoglutarate or a-ketoglutarate, belongs to the class of organic compounds known as gamma-keto acids and derivatives. These are organic compounds containing an aldehyde substituted with a keto group on the C4 carbon atom. Oxoglutaric acid is an extremely weak basic (essentially neutral) compound (based on its pKa). Oxoglutaric acid exists in all living species, ranging from bacteria to humans. Within yeast, oxoglutaric acid participates in a number of enzymatic reactions. In particular, ornithine and oxoglutaric acid can be converted into L-glutamic acid and L-glutamic gamma-semialdehyde through its interaction with the enzyme ornithine aminotransferase, mitochondrial. In addition, oxoglutaric acid and ammonium can be biosynthesized from L-glutamic acid; which is catalyzed by the enzyme glutamate dehydrogenase, mitochondrial. In yeast, oxoglutaric acid is involved in the metabolic pathway called the glutamate metabolism pathway. Oxoglutaric acid is a potentially ...
The swamp eel, Monopterus albus, is an obligatory air-breathing teleost which can survive long period of emersion, has high environmental and tissue ammonia tolerance, and acclimate from fresh to brackish water. This study was undertaken to clone and sequence gdh expressed in the liver, intestine and brain of M. albus, to verify whether more than one form of gdh were expressed, and to examine the gdh mRNA expressions in these three organs in fish exposed to various adverse conditions using quantitative real-time PCR. Only one gdh gene sequence, consisted of a 133 bp 5 UTR, a CDS region spanning 1629 bp and a 3 UTR of approximately 717 bp, was obtained from the liver, intestine and brain of M. albus. The translated Gdh amino acid sequence from the liver of M. albus had 542 residues and was confirmed to be Gdh1a. It had sequence identity of |90% with Oncorhynchus mykiss Gdh1a, Salmo salar Gdh1a1, Bostrychus sinensis Gdh1a and Tribolodon hakonensis Gdh1a, and formed a monophyletic clade with B.
O-acetylhomoserine O-acetylserine sulfhydrylase; involved in sulfur amino acid biosynthesis; immunogenic; Hog1p; biofilm; Predicted ORF from Assembly 19; Gcn4p-regulatedProtein abundance is affected by URA3 expression in the CAI-4 strain background; alkaline upregulated; Gcn4p-regulatedProtein described as aspartate aminotransferase; soluble protein in hyphae; alkaline upregulated; amphotericin B repressed Malic enzyme, mitochondrial protein; transcription regulated by Mig1p and Tup1p; shows colony morphology-related gene Predicted ORF from Assembly 19; Gcn4p-regulated Large subunit of heterodimeric alpha-aminoadipate reductase; enzyme of lysine biosynthesis; contains predicted binding sites for AMP and alpha-aminoadipate; feedback inhibited by lysine or Putative NAD-specific glutamate dehydrogenase; fungal-specific (no human or murine homolog); transcription is regulated by Nrg1p, Mig1p, Tup1p, and Gcn4pSimilar to an aldose 1-epimerase-related protein; antigenic during murine systemic ...
The extremely halophilic archaeon Natrialba aegyptiaca secretes the L-homo type of poly-g-glutamate (PGA) as an extremolyte. We examined the enzymes involved in glutamate metabolism and verified the presence of L-glutamate dehydrogenases, L-aspartate aminotransferase, and L-glutamate synthase. However, neither glutamate racemase nor D-amino acid aminotransferase activity was detected, suggesting the absence of sources of D-glutamate. In contrast, D-glutamate-rich PGA producers mostly possess such intracellular sources of D-glutamate. The results of our present study indicate that the D-glutamate-anabolic enzyme
Land snails, Otala lactea, survive in seasonally hot and dry environments by entering a state of aerobic torpor called estivation. During estivation, snails must prevent excessive dehydration and reorganize metabolic fuel use so as to endure prolonged periods without food. Glutamate dehydrogenase (GDH) was hypothesized to play a key role during estivation as it shuttles amino acid carbon skeletons into the Krebs cycle for energy production and is very important to urea biosynthesis (a key molecule used for water retention). Analysis of purified foot muscle GDH from control and estivating conditions revealed that estivated GDH was approximately 3-fold more active in catalyzing glutamate deamination as compared to control. This kinetic difference appears to be regulated by reversible protein phosphorylation, as indicated by ProQ Diamond phosphoprotein staining and incubations that stimulate endogenous protein kinases and phosphatases. The increased activity of the high-phosphate form of GDH seen ...
Two electrophoretically distinct variants of supernatant nicotinamideadenine dinucleotide phosphate-dependent malate dehydrogenase exist in mice (Mus musculus). They are controlled by codominant alleles segregating at an autosomal locus. The two forms exist in a polymorphic condition in wild populations of Mus musculus and are fixed in a homozygous condition in inbred lines. These genetic electrophoretic variants are used here to study the subunit structure of this enzyme. Evidence indicating a tetrameric structure for mouse nicotinamideadenine dinucleotide phosphate-dependent malate dehydrogenase is presented. This interpretation is based on the occurrence in heterozygote tissue extracts of five electrophoretically distinct enzymes. This is the predicted phenotype for tetramers composed of two types of subunits which associate randomly in heterozygotes forming three hybrid enzymes having mobilities intermediate between the parental forms. ...
In patients with recessive, adult-onset olivopontocerebellar degeneration associated with a partial deficiency of glutamate dehydrogenase, the concentration of glutamate in plasma was significantly higher than that in controls. Plasma alpha-ketoglutarate was significantly lower. Oral administration of monosodium glutamate resulted in excessive accumulation of this amino acid in plasma and lack of increase in the ratio of plasma lactate to pyruvate in the glutamate dehydrogenase-deficient patients. Decreased glutamate catabolism may result in an excess of glutamate in the nervous system and cause neuronal degeneration. ...
Crude synaptosomes (P2 fraction) were prepared from striatum, hippocampus, or cerebral cortex of young adult male Sprague-Dawley rats (150-200 g), from cerebral cortex of adult male C57BL/6 mice (25-30 g), or from cerebral cortex of adult male guinea pigs (400-500 g) as described. 26 Synaptosomes were suspended in HEPES buffered medium (composition: 140 mm NaCl, 5 mm KCl, 1 mm MgCl2, 1.2 mm Na2HPO4, 5 mm NaHCO3, 10 mm d-glucose, and 20 mm HEPES/NaOH, pH 7.4), collected by centrifugation at 8,000 g for 10 min, and stored on ice for up to 5 h until use. Release of endogenous glutamate was measured by an enzyme-linked fluorometric method. 27 Synaptosomal pellets (0.5 mg protein, determined by the method of Bradford 28) were resuspended in HEPES buffered medium plus 16 μm bovine serum albumin, 1 mm NADP+, 100 U l-glutamate dehydrogenase, and 1.3 mm CaCl2(1.5 ml final volume). Stirred samples were equilibrated at 37°C for 4 min in a spectrofluorometer cuvette, and data acquisition was initiated ...
Redox enzymes catalyze fascinating chemical reactions with excellent regio- and stereospecificity. Nicotinamide adenine dinucleotide cofactor is essential in numerous redox biocatalytic reactions and needs to be regenerated because it is consumed as an equivalent during the enzymatic turnover. Here we report on unbiased photoelectrochemical tandem assembly of a photoanode (FeOOH/BiVO4) and a perovskite photovoltaic to provide sufficient potential for cofactor-dependent biocatalytic reactions. We obtain a high faradaic efficiency of 96.2% and an initial conversion rate of 2.4 mM h(-1) without an external applied bias for the photoelectrochemical enzymatic conversion of alpha-ketoglutarate to L-glutamate via L-glutamate dehydrogenase. In addition, we achieve a total turnover number and a turnover frequency of the enzyme of 108,800 and 6200 h(-1), respectively, demonstrating that the tandem configuration facilitates redox biocatalysis using light as the only energy source ...
The activity of aldolase, glyceraldehyde-3-phosphate dehydrogenase, 3-phospho-glycerate kinase, pyruvate phosphokinase, malic dehydrogenase, glutamic-oxalacetic transaminase was studied in extracts of green and streptomycin- or erythromycin-depigmented cells ofEuglena gracilis var.bacillaris obtained by the freezing technique. The presence of lactic dehydrogenase acting with DPN, of glutamic dehydrogenase and of glutamicpyruic-transaminase was not demonstrated. В полученных путем замораживания экстрактах из эеленых и обесцвеченных стрептомицином или эритромицином клеток Euglena gracilis var. bacillaris была определена активность следующих ферментов: альдолазы, глицеринальдегид-фосфат-дегидрогеназы, фосфоглицерат-киназы, пируат-киназы, малат-де-гидрогеназы, глутамат
Glutamate dehydrogenase (GDH) from the hyperthermophilic Archaeon ES4 (optimal growth temperature 98 degrees C and maximum growth temperature 110 degrees C) was purified to homogeneity. The purified native enzyme had an M(r) of 270,000 +/- 5,000 and was shown by gel filtration and SDS-polyacrylamide gel electrophoresis to be a hexamer with identical subunits of M(r) = 46,000 +/- 3,000. The hexameric subunit composition was also evident from electron micrographs, which show a triangular antiprism structure very similar to that of bovine GDH. The enzyme is exceptionally thermostable, with a half-time of inactivation of 3.5 h at 105 degrees C. Differential scanning calorimetry revealed a tm for denaturation of 113 degrees C, and a tm for activation at 60 degrees C. Antigenic cross-reaction with ES4 GDH was observed with the purified GDH from the thermophilic Archaea, Pyrococcus furiosus and Thermococcus litoralis as well as with bovine and yeast GDHs. The genome of ES4 was shown to contain a single ...
Various additional conserved connections were found, although these appeared far more family-specific. For instance, in the order Lactobacillales a genomic association with the genes of the two glutamine ABC transporter encoding variants glnP H Q or glnQHMP were identified, whereas this association appeared to be replaced by one with the sodium/proton amino acid symporters encoded by gltT (glutamate, [47]) and alsT[15] in various species within the family of the Bacillaceae. The AlsT protein is very similar to GlnT, a cation-glutamine symporter, i.e. showing a high degree of sequence conservation and having about the same length and the same number of predicted transmembrane helices. Although the protein is sometimes referred to as an alanine transporter, AlsT could well be a cation-glutamine or asparagine symporter.. Other associations that were conserved included that with the gdh gene (encoding glutamate dehydrogenase) and the citBZ-icd operon (encoding aconitase, citrate synthase and ...
Pathology activating regulatory mutations of glutamate dehydrogenase (GDH) in congenital hyperinsulinism with hyperammonemia (GDH-HI or HI/HA (...)