• On the other hand, the alternative test is called a specific toxin test, which can be done either with a cell cytotoxicity assay, which has become obsolete because it's too slow and no labs know how to do it any longer, and it has been replaced by an enzyme immunoassay for toxin. (hcplive.com)
  • It can be done with PCR first and then followed by a toxin test, or it can be done with a GDH test followed by an enzyme immunoassay for toxin, and then arbitrating those tests that don't agree with a PCR test. (hcplive.com)
  • A toxin enzyme immunoassay should not be used as a stand-alone test. (oklahoma.gov)
  • They assimilated ammonium via the glutamate cycle enzymes glutamine synthetase and glutamate synthase. (microbiologyresearch.org)
  • The action of antidiabetic plants of the Canadian James Bay Cree traditional pharmacopeia on key enzymes of hepatic glucose homeostasis ") report the antidiabetic action of seven Canadian plants as evidenced by glucose-6-phosphatase and glycogen synthase, two key enzymes, respectively, involved in gluconeogenesis and glycogenesis in hepatocytes. (hindawi.com)
  • Part of glutamate synthase (GltAB, orange and magenta) blocks the active site of glutamate dehydrogenase (green). (acs.org)
  • Researchers led by James S. Fraser of the University of California San Francisco and Dan S. Tawfik and Vijay Jayaraman of the Weizmann Institute of Science solved cryo-electron microscopy structures of a complex of the enzymes glutamate synthase (GltAB) and glutamate dehydrogenase (GudB) in Bacillus subtilis . (acs.org)
  • Results from sucrose density gradient centrifugation of a cell-free particulate fraction and comparison with marker enzymes suggested that α-isopropylmalate synthase was located in the mitochondria. (ku.edu)
  • It thus appears that, in yeast, the first specific enzyme in the leucine biosynthetic pathway (α-isopropylmalate synthase) is particulate, whereas the next two enzymes in the pathway (isopropylmalate isomerase and β-isopropylmalate dehydrogenase) are "soluble," with glutamate-α-ketoisocaproate transaminase activity being located in both the cytosol and particulate cell fractions. (ku.edu)
  • Multiple isozymes of 2,3-butanediol dehydrogenase, ATP synthase and [FeFe]-hydrogenase were differentiated and assigned roles according to their structural properties and genomic contexts. (umass.edu)
  • An NADP + dependent enzyme that catalyzes the oxidation of L-glutamate 5-semialdehyde to L-glutamyl 5-phosphate. (online-medical-dictionary.org)
  • Structure of NADP(+)-dependent glutamate dehydrogenase from Escherichia coli--reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases. (anl.gov)
  • EC 1.4.1.2-4) catalyse the oxidative deamination of L-glutamate to α-ketoglutarate, using NAD(+) and/or NADP(+) as a cofactor. (anl.gov)
  • Hyperprolinemia type II is caused by variants in the ALDH4A1 gene, which provides instructions for producing the enzyme pyrroline-5-carboxylate dehydrogenase. (medlineplus.gov)
  • Variants in either the PRODH or ALDH4A1 gene can cause a reduction in proline dehydrogenase or pyrroline-5-carboxylate dehydrogenase function and a decrease in the breakdown of proline. (medlineplus.gov)
  • How is alanine formed from pyruvate and glutamate? (flashcardmachine.com)
  • animals were sacrificed at 30, 60, or 90 days for chemical analyses (serum glutamate-oxalacetate-transaminase, lactic-dehydrogenase, blood urea nitrogen, serum glutamate-pyruvate-transaminase, and serum triglycerides). (cdc.gov)
  • The E3 component is associated with 2 additional alpha-ketoacid dehydrogenase complexes, namely pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase. (medscape.com)
  • Mutations in E3 cause additional deficiencies of pyruvate and alpha-ketoglutarate dehydrogenases. (medscape.com)
  • 1. Olson, J.A. and Anfinsen, C.B. The crystallization and characterization of L -glutamic acid dehydrogenase. (qmul.ac.uk)
  • Rapid and progressive reductions in oxidative enzyme activities bring about a reduced mitochondrial ATP production. (lww.com)
  • Glutamate dehydrogenase 1 (GLUD1) is a mitochondrial enzyme expressed in all tissues, including brain. (uky.edu)
  • The BCKD enzyme complex, which is associated with the inner mitochondrial membrane, has 3 different catalytic components (ie, E1, E2, E3) and 2 associated regulatory enzymes (ie, BCKD phosphatase, BCKD kinase). (medscape.com)
  • Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+. (lookformedical.com)
  • dehydrogenase gene and their antigen levels in peripheral blood samples of malaria patients. (thehindubusinessline.com)
  • Sirtuins or "silent information regulators" of gene transcription, are a family of enzymes which are expressed throughout all phyla of life. (frontiersin.org)
  • Gene silencing by this family of enzymes has been correlated directly with longer lifespan in yeast and worms ( Yang and Sauve, 2005 ). (frontiersin.org)
  • We also analyzed the glutamate dehydrogenase gene for the exons encoding an allosteric regulatory domain of the enzyme. (diabetesjournals.org)
  • Hyperprolinemia type I is caused by variants in the PRODH gene, which provides instructions for producing an enzyme called proline dehydrogenase. (medlineplus.gov)
  • Quental et al identified a homozygous 1-bp deletion (117delC) in the BCKDHA gene (this gene codes for the alpha subunit of the BCKD enzyme complex, specifically E1) in Portuguese Gypsies and estimated the carrier frequency for this deletion to be as high as 1.4% (about 1 case per 71 live births). (medscape.com)
  • This enzyme catalyzes the irreversible oxidation of glutamate-gamma- semialdehyde to glutamate as part of the proline degradation pathway. (expasy.org)
  • What enzyme catalyzes the conversion of phenylalanine to tyrosine? (flashcardmachine.com)
  • What enzyme catalyzes glutamate → glutamine? (flashcardmachine.com)
  • EC 1.4.1.3) catalyzes reversible oxidative deamination of l -glutamate to α-ketoglutarate. (diabetesjournals.org)
  • GltAB catalyzes glutamate formation, but when there's too much glutamate present, the cell shuts down GltAB but not GudB production. (acs.org)
  • A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. (lookformedical.com)
  • A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the reversible transamination of branched-chain AMINO ACIDS to 2-oxoglutarate. (lookformedical.com)
  • An enzyme that catalyzes the first step in the biosynthetic pathway to LEUCINE , forming isopropyl malate from acetyl-CoA and alpha-ketoisovaleric acid. (lookformedical.com)
  • This finding suggests that constitutively activated GDH enhances oxidation of glutamate, which is intracellularly converted from glutamine to α-ketoglutarate, a tricarboxylic acid cycle substrate, which thereby stimulates insulin secretion. (diabetesjournals.org)
  • GDH is ubiquitously expressed, and its oxidative deamination reaction feeds the tricarboxylic acid (TCA) cycle by converting l -glutamate to α-ketoglutarate, whereas the reductive amination reaction supplies nitrogen for several biosynthetic pathways. (diabetesjournals.org)
  • Catabolic glutamate dehydrogenases were discovered, implying that the tricarboxylic acid (TCA) cycle can function catabolically. (umass.edu)
  • This enzyme catalyses the following chemical reaction L-glutamate + H2O + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } 2-oxoglutarate + NH4+ + NAD(P)H + H+ Olson JA, Anfinsen CB (May 1952). (wikipedia.org)
  • What enzyme does the reverse reaction? (flashcardmachine.com)
  • Each enzyme is allocated a four-digit EC number, the first three digits of which define the reaction catalysed and the fourth of which is a unique identifier (serial number). (cam.ac.uk)
  • Each enzyme is also assigned a systematic name that uniquely defines the reaction catalysed. (cam.ac.uk)
  • Enzymes act on molecules, called substrates , whereas the molecule formed in the chemical reaction is known as the product . (biologyonline.com)
  • This enzyme begins the process of breaking down proline by starting the reaction that converts proline to pyrroline-5-carboxylate. (medlineplus.gov)
  • This enzyme helps to break down the pyrroline-5-carboxylate produced in the previous reaction, converting it to the amino acid glutamate. (medlineplus.gov)
  • Leucine is rapidly transported across the blood-brain barrier and is metabolized to presumably yield glutamate and glutamine. (medscape.com)
  • Glutamate dehydrogenase (NAD(P)+) (EC 1.4.1.3, glutamic dehydrogenase, glutamate dehydrogenase [NAD(P)+]) is an enzyme with systematic name L-glutamate:NAD(P)+ oxidoreductase (deaminating). (wikipedia.org)
  • Our study provides scientific evidence for the conserved nature of glutamate dehydrogenase sequences in Indian isolates which can be used as a potential biomarker for diagnosis of malaria," said Dr. Praveen Kumar Bharti, leader of the research team. (thehindubusinessline.com)
  • Usually enzyme complexes make multistep processes easier by catalyzing sequential reactions in which the product of one enzyme becomes the substrate for the next. (acs.org)
  • The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide. (lookformedical.com)
  • Subunits of homo-hexameric bacterial enzymes comprise a substrate-binding domain I followed by a nucleotide-binding domain II. (anl.gov)
  • Most enzymes bind to a specific substrate. (biologyonline.com)
  • Maple syrup urine disease (MSUD), also known as branched-chain ketoaciduria, is an aminoacidopathy due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. (medscape.com)
  • S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2 ) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. (expasy.org)
  • I also describe the activation of the inactive recombinant enzyme produced in mesophilic Escherichia coli from the viewpoint of the relationship between structure and activity. (go.jp)
  • The structures reveal that the two enzymes form a complex in which one of GltAB's subunits blocks the active site of GudB. (acs.org)
  • Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs180) contain long N- and C-terminal segments flanking the catalytic core. (diamond.ac.uk)
  • Maple syrup urine disease is caused by a deficiency of the branched-chain alpha-keto acid dehydrogenase (BCKD) enzyme complex, which catalyses the decarboxylation of the alpha-keto acids of leucine, isoleucine, and valine to their respective branched-chain acyl-CoAs. (medscape.com)
  • Among the three genes, nucleotide composition of glutamate dehydrogenase was almost the same across the samples. (thehindubusinessline.com)
  • What are the affected genes/enzymes in PKU? (flashcardmachine.com)
  • At the transcriptional level in the hippocampus, cells respond by increasing the expression of genes related to neurite growth and synapse formation, indications of adaptive or compensatory responses to the effects of increases in the release and action of glutamate at synapses. (uky.edu)
  • These genes provide instructions for enzymes that break down proline. (medlineplus.gov)
  • In many bacterial species, both activities are carried out by a single bifunctional enzyme. (expasy.org)
  • In this way, the complex has the effect of regulating the amount of the glutamate inside the bacterial cell. (acs.org)
  • Amine oxidoreductases that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-LYSINE or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-GLUTAMATE. (bvsalud.org)
  • The conversion of proline to glutamate (and the conversion of glutamate to proline, which is controlled by different enzymes) is important for maintaining a supply of amino acids needed for protein production, and for energy transfer within the cell. (medlineplus.gov)
  • Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. (cathdb.info)
  • Instead, the effect is specific to LIV and is accompanied by a major reduction in transcription and activity of LIV biosynthetic enzymes. (nih.gov)
  • The enzymes from hyperthermophiles are generally extremely thermostable and lose little or no activity during long periods under a variety conditions. (go.jp)
  • The accumulation of both peptides in the endothelial cells suggested in vivo inhibitory activity of the angiotensin I-converting enzyme. (go.jp)
  • The activity of the enzyme is regulated positively and negatively by several allosteric effectors, such as leucine, ADP, and GTP. (diabetesjournals.org)
  • When bound to each other, one of the enzymes inhibits the activity of the other. (acs.org)
  • Of the total glutamate-α-ketoisocaproate transaminase activity, approximately 20% was in the initial soluble fraction, whereas solubilization of the remainder again required homogenization of the spheroplast lysate. (ku.edu)
  • Plasma glutamate dehydrogenase activity initially increased but rapidly declined thereafter and was attributed to acute focal hepatocellular injury. (bioone.org)
  • Plasma sorbitol dehydrogenase activity was the most specific indicator of liver injury in both groups. (bioone.org)
  • The Tg mice have increased activity of GLUD, as well as elevated levels and increased synaptic and depolarization-induced release of glutamate. (uky.edu)
  • This panel may be modified as appropriate for other species, eg, glutamate dehydrogenase (GDH) and/or gamma-glutamyl transferase (GGT) are more appropriate "liver enzymes" for horses and farm animals, or it may be more appropriate to concentrate primarily on muscle enzymes (CK and AST) in athletic animals. (merckvetmanual.com)
  • Clinical biochemistry refers to the analysis of the blood plasma (or serum) for a wide variety of substances-substrates, enzymes, hormones, etc-and their use in diagnosis and monitoring of disease. (merckvetmanual.com)
  • Clostridium difficile ( Clostridium difficile testing should include a glutamate dehydrogenase screen and if positive followed by a confirmatory test OR nucleic acid amplification test in patients with documented diarrhea. (oklahoma.gov)
  • This review summarizes evidence for the role of proteolytic enzymes that degrade and inactivate insulin-like growth factor binding proteins (IGFBP) during follicular development in mammals. (bioone.org)
  • Results indicated a decrease in the level of enzymes classically found in serum following acute liver injury. (cdc.gov)
  • Although conserved residues in the nucleotide-binding domains of various dehydrogenases have been linked to cofactor preferences, the structural basis for specificity in the GDH family remains poorly understood. (anl.gov)
  • For an enzyme that's both found in both toxigenic and nontoxigenic strains of C diff , originally developed as a toxin A-test, but unfortunately it was identifying the wrong antigen. (hcplive.com)
  • Histologic changes correlated poorly with biochemical results, possibly because the small area of hepatic parenchyma that was damaged did not affect enzyme values substantially. (bioone.org)
  • Each step of these sequential reactions occurs under the action of a specific enzyme . (biologyonline.com)
  • The structure and mechanism of methanol dehydrogenase. (microbiologyresearch.org)
  • In this review, I describe the molecular mechanism underlying the extreme stability of unboiled NAD-dependent glutamate dehydrogenase from the hyperthermophile Pyrobaculum islandicum . (go.jp)
  • The absence of asparagine synthetase and the presence of a mutant tRNA for asparagine encoded among RNA-active enzymes suggest that P. carbinolicus may make asparaginyl-tRNA in a novel way. (umass.edu)
  • Although this enzyme is expressed in glutamatergic pathways, its function as a regulator of glutamate neurotransmitter levels is still not well defined. (uky.edu)