• Glutamate participates in the combined deamination centered on glutamate dehydrogenase. (mgm-biochem.com)
  • This requires a continuous de novo synthesis of glutamate, likely involving the action of both pyruvate carboxylase (PC) and glutamate dehydrogenase (GDH). (123dok.net)
  • That means that AKG can neither be synthesized by the citrate cycle nor from glutamate since the genes encoding aconitase (EC 4.2.1.3), isocitrate dehydrogenase (EC 1.1.1.41), and glutamate dehydrogenase (EC 1.4.1.2) are not present. (springeropen.com)
  • About 20% of the glutamate produced by proline oxidation is usually in turn oxidized by glutamate dehydrogenase [6], whereas the remainder undergoes transamination by reaction with pyruvate and the producing alanine accumulates as the proline is usually utilized. (nuche.org)
  • Ammonia incorporation in animals occurs through the actions of glutamate dehydrogenase and glutamine synthase. (medmuv.com)
  • A pair of principal enzymes, glutamate dehydrogenase and glutamine synthatase, are found in all organisms and effect the conversion of ammonia into the amino acids glutamate and glutamine, respectively. (medmuv.com)
  • 1. Frieden, C. L -Glutamate dehydrogenase. (qmul.ac.uk)
  • 3. Pahlich, E. and Joy, K.W. Glutamate dehydrogenase from pea roots: purification and properties of the enzyme. (qmul.ac.uk)
  • Alanine aminotransferase measurements are used in the diagnosis and treatment of certain liver diseases (e.g., viral hepatitis and cirrhosis) and heart diseases. (cdc.gov)
  • The aminotransferase catalyzes the reversible transfer of an amino group to α-keto butyrate to form α-aminobutyrate. (springeropen.com)
  • Blood samples were collected at the end of the study to measure serum lipid profile, alanine aminotransferase, aspartate aminotransferase, lactate dehydrogenase, and tissue oxidative stress level. (hindawi.com)
  • Serum aminotransferases such as aspartate aminotransferase, AST and alanine transaminase, ALT have been used as clinical markers of tissue damage, with increasing serum levels indicating an increased extent of damage. (medmuv.com)
  • Two millimeter of venous blood was collected from all the participants and processed for urea, cholesterol, triglyceride (TG), serum glutamate-oxaloacetate transaminase (SGOT) (aspartate aminotransferase), and serum glutamate-pyruvate transaminase (SGPT) (alanine aminotransferase) by using standard kits (ERBA) in semiauto analyzer (Transasia Erba Chem5X by Calbiotech Inc. USA, semiautomated clinical chemistry analyzer) and the fully automatic analyzer (Cobas Integra 400 Roche, Germany) method. (mouldmedical.com)
  • Lactate formation is catalyzed by lactate dehydrogenase in a reversible reaction. (vegfinhibitors.com)
  • The glutathione, glutathione-s-transferase, catalase, superoxide dismutase, lipid peroxidation, lactate dehydrogenase, aspartic acid transaminase, and alanine aminotransaminase levels were estimated in the liver of iron treated mice after 30 days post-iron treatment. (biomedres.us)
  • The feeding of different concentrations of iron for 30 days led to an increase in the oxidative stress as indicated by a decline in the glutathione concentration, and glutathione-s-transferase, catalase, and superoxide dismutase activities accompanied by the rise in the lactate dehydrogenase, aspartic acid transaminase, and alanine aminotransaminase levels. (biomedres.us)
  • Treatment of hesperidin for 5 days before iron overload elevated the activities of glutathione-s-transferase, catalase, and superoxide dismutase and glutathione concentration, whereas the activities of lactate dehydrogenase, aspartic acid transaminase, and alanine aminotransaminase and lipid peroxidation declined significantly. (biomedres.us)
  • Our study demonstrates that pre-treatment of hesperidin for five days reduced the iron induced oxidative stress indicated by the reduction in lipid peroxidation, lactate dehydrogenase, aspartic acid transaminase, and alanine aminotransaminase activities and a rise in the glutathione-s-transferase, catalase, and superoxide dismutase and glutathione contents in the mice liver. (biomedres.us)
  • The kidney was not able to balance the NADH excess even though an increase in malate dehydrogenase, lactate dehydrogenase, aspartate and alanine transaminase activities was noted [23]. (precisionfda.org)
  • Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH. (proteopedia.org)
  • And then under the catalysis of alanine transaminase, glutamate with pyruvate can form α-ketoglutarate and alanine. (mgm-biochem.com)
  • These reaction steps are similar to the ones used in the engineered bacteria, where either a transaminase or a dehydrogenase catalyzes the final step of AABA synthesis (Fotheringham et al. (springeropen.com)
  • Alanine transaminase has an important function in the delivery of skeletal muscle carbon and nitrogen (in the form of alanine) to the liver. (medmuv.com)
  • In the liver, alanine transaminase transfers the ammonia to α-KG and regenerates pyruvate. (medmuv.com)
  • This reaction is catalyzed by alanine transaminase, ALT. (medmuv.com)
  • Using site-directed mutagenesis we have shown that both PPDK and PEPS in which the serine and cysteine residues, respectively, were substituted with an alanine the enzymes could be regulated indicating that the serine and cysteine residues, respectively, are not essential for regulation. (scirp.org)
  • Carbon Monoxide Dehydrogenase (CODH), also known as Acetyl-CoA synthase (ACS), is one of seven known Ni containing enzymes. (tamu.edu)
  • They are also of few mononuclear and polynuclear clusters in less than two potential technological interest for construction of the anodes dozen different types of enzymes catalyzing diverse biological of (implantable) biofuel cells (10). (docslib.org)
  • Over 20 copper-containing enzymes that the active site of a not previously described enzyme, thiocya- catalyze a wide-ranging group of chemical reactions have been nate dehydrogenase. (docslib.org)
  • As well as being an integral cofactor for succinate dehydrogenase, FAD also assists other enzymes that require oxidation-reduction support. (histocutup.co.uk)
  • ADH catalyzes the oxidation of retinol to retinal, which is converted to retinoic acid by ALDH. (precisionfda.org)
  • 2004). Betaine aldehyde dehydrogenase (BADH) belongs to the ALDH9 family and catalyses the irreversible oxidation of betaine aldehyde to glycine betaine (N, N, N-trimethyl amine), a vital osmolyte accumulated in cells under osmotic stress (Chen and Murata, 2011). (precisionfda.org)
  • MDH_HALMA ] Catalyzes the reversible oxidation of malate to oxaloacetate. (proteopedia.org)
  • Glucose oxidation produces pyruvate which can undergo transamination to alanine. (medmuv.com)
  • Choline dehydrogenase catalyzes the oxidation of choline to glycine betaine via betaine aldehyde in glycine betaine biosynthesis. (scialert.net)
  • Choline dehydrogenase ( betA ) of E . coli catalyses the first step in glycine betaine biosynthesis, the oxidation of choline. (scialert.net)
  • 2005). One of the most important osmoprotectants is betaine aldehyde dehydrogenase (Kumar et al. (precisionfda.org)
  • betaine biosynthesis is catalyzed by choline monooxygenase in combination with betaine aldehyde dehydrogenase. (scialert.net)
  • The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui was determined by x-ray crystallography. (proteopedia.org)
  • Structural Features That Stabilize Halophilic Malate Dehydrogenase from an Archaebacterium. (proteopedia.org)
  • This process is referred to as the glucose-alanine cycle. (medmuv.com)
  • The glucose-alanine cycle is used primarily as a mechanism for skeletal muscle to eliminate nitrogen while replenishing its energy supply. (medmuv.com)
  • The expression of regulatory molecules, TGF-β1/2, phospho-Akt (Ser473), PPARα, sterol regulatory element-binding protein 1 (SREBP-1), fatty acid synthase (FASN), hormone-sensitive lipase (HSL), and acyl dehydrogenases was analyzed in virus-infected hepatocytes. (academic-accelerator.com)
  • Alanine dehydrogenase (EC 1.4.1.1) is an enzyme that catalyzes the chemical reaction L-alanine + H2O + NAD+ ⇌ {\displaystyle \rightleftharpoons } pyruvate + NH3 + NADH + H+ The 2 substrates of this enzyme are L-alanine, water, and nicotinamide adenine dinucleotide+ because water is 55M and does not change, whereas its 4 products are pyruvate, ammonia, NADH, and hydrogen ion. (wikipedia.org)
  • reaction catalyzed by pyruvate carboxylase. (rahulgladwin.com)
  • reaction catalyzed by PEP carboxykinase (PEPCK). (rahulgladwin.com)
  • Recently, it was shown that Pediococcus acidilactici FAM18098 catabolized serine and threonine and formed α-aminobutyrate (AABA) and alanine in vitro and in cheese (Irmler et al. (springeropen.com)
  • Likewise, serine could be converted via pyruvate to alanine. (springeropen.com)
  • In pancreatic cancer cells a cytosolic metabolic enzyme, wild-type isocitrate dehydrogenase 1 (wtIDH1), enables adaptation to these conditions. (nature.com)
  • Other names in common use include AlaDH, L-alanine dehydrogenase, NAD+-linked alanine dehydrogenase, alpha-alanine dehydrogenase, NAD+-dependent alanine dehydrogenase, alanine oxidoreductase, and NADH-dependent alanine dehydrogenase. (wikipedia.org)
  • Many recent data revealed that kidney alcohol dehydrogenase activity increased significantly after ethanol administration what affected the capacity of the kidney to prevent NADH accumulation in the cytosol. (precisionfda.org)
  • Complejo enzimático que cataliza la DESCARBOXILACIÓN oxidativa y la DESAMINACIÓN de la GLICINA en DIÓXIDO DE CARBONO, AMONÍACO, NADH y N5N10-metilenotetrahidrofolato. (bvsalud.org)
  • We also found that renal cell cancer patients have significantly higher total activity of alcohol dehydrogenase and its class I isoenzyme in the serum. (precisionfda.org)
  • For example, alcohol dehydrogenase converts primary alcohols to aldehydes. (cliffsnotes.com)
  • A thermostable alcohol dehydrogenase from Thermoanaerobacter brockii (TbSADH) has been repurposed to perform asymmetric reduction of a series of prochiral ketones with the formation of enantio-pure secondary alcohols, which are crucial chiral synthons needed in the preparation of various pharmaceuticals. (springeropen.com)
  • 2008 ). As a complementary strategy to the traditional approach, it has been demonstrated that alcohol dehydrogenases (ADHs) can reduce such prochiral ketones with very high chemo-, regio-, and stereoselectivity, thereby enabling a sustainable synthetic route to chiral alcohols, which includes biodegradability of the biocatalyst (Garcia-Urdiales et al. (springeropen.com)
  • In blood ammonia transport, glutamine synthetase catalyzes the combination of glutamic acid and ammonia to generate glutamine. (mgm-biochem.com)
  • 1. Olson, J.A. and Anfinsen, C.B. The crystallization and characterization of L -glutamic acid dehydrogenase. (qmul.ac.uk)
  • Pyruvate cannot produce oxaloacetate and is shunted to alternative pathways that produce lactic acid and alanine. (medscape.com)
  • The precursor of oxaloacetate, pyruvate, is shunted toward alternate metabolic pathways, leading to an increase in lactic acid, alanine, and acetylcoenzyme A (acetyl-CoA). (medscape.com)
  • Complex II of the chain is the succinate dehydrogenase enzyme complex. (histocutup.co.uk)
  • The systematic name of this enzyme class is L-alanine:NAD+ oxidoreductase (deaminating). (wikipedia.org)
  • Pyruvate, orthophosphate dikinase (PPDK) and phosphoenolpyruvate synthetase (PEPS) catalyze the conversion of pyruvate to phosphoenolpyruvate (PEP). (scirp.org)
  • EC 2.7.9.1) catalyzes the reversible conversion of pyruvate to phosphoenolpyruvate (PEP) and is important in C 4 plants as it is generally recognized as catalyzing the rate-limiting step of C 4 photosynthesis [1]. (scirp.org)
  • PC catalyzes the conversion of pyruvate to oxaloacetate with biotin as a cofactor. (medscape.com)
  • It catalyzed the transfer of the amino group from leucine, methionine, AABA, alanine, cysteine, and phenylalanine to the amino group acceptor α-ketoglutarate. (springeropen.com)
  • Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. (rhea-db.org)
  • In this study, choline dehydrogenase ( betA ) gene encoding for glycine betaine biosynthesis in Escherichia coli isolated from salted shark ( Scoliodon sp. (scialert.net)
  • Mechanistically, BH4 is a potent radical-trapping antioxidant that protects lipid membranes from autoxidation, alone and in synergy with vitamin E. Dihydrofolate reductase catalyzes the regeneration of BH4, and its inhibition by methotrexate synergizes with GPX4 inhibition. (biomed.news)
  • In plant, the first and the third steps of the synthesis of methionine and threonine are catalyzed by a bifunctional enzyme, aspartate kinase-homoserine dehydrogenase (AK-HSDH). (rhea-db.org)
  • Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana. (rhea-db.org)
  • Only nominal studies in characterization of choline dehydrogenase from E . coli have been reported to date. (scialert.net)
  • In this study, we report the characterization and structural analysis of choline dehydrogenase in E . coli . (scialert.net)
  • Some sulfur- Here we report the discovery and characterization of a pre- oxidizing bacteria (SOB) known to play an important role in viously undescribed copper center that forms the active site of global geochemical cycles can utilize thiocyanate as the sole a copper-containing enzyme thiocyanate dehydrogenase (sug- source of energy and nitrogen . (docslib.org)
  • the encoded PFL1 protein catalyzes a major fermentative pathway in wild-type Chlamydomonas cells. (montana.edu)
  • The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. (rhea-db.org)
  • Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II. (rhea-db.org)
  • Four semi-conserved histidine residues were individually mutated to alanine. (tamu.edu)
  • IDH1 is a cytosolic enzyme that catalyzes the reversible conversion of isocitrate and αKG. (nature.com)
  • In skeletal muscle, pyruvate is transaminated to alanine, thus affording an additional route of nitrogen transport from muscle to liver. (medmuv.com)
  • that is, maize leaf PDRP only catalyzes the regulation of PPDK and E. coli PSRP only catalyzes the regulation of PEPS. (scirp.org)
  • The inhibition of pyrimidine biosynthesis by blocking the dihydroorotate dehydrogenase (DHODH) activity, the prime target of leflunomide (LEF), has been proven to be an effective strategy for rheumatoid arthritis (RA) treatment. (biomedcentral.com)
  • Β-Alanine and β-aminoisobutyrate pyrimidines are the nitrogen bases present on the information we have and it may not be so! (euroasfalti.net)
  • Crystallization and mutational studies of carbon monoxide dehydrogenase from moorella thermoacetica. (tamu.edu)
  • In our previous study we found that the total activity of aldehyde dehydrogenase in cancer ON123300 of RCC is at the same level as in normal renal tissue [10]. (precisionfda.org)
  • haloalkaliphilic SOB of the genus Thioalkalivibrio can catalyze molecular mechanism this process. (docslib.org)