An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.
Inosine 5'-Monophosphate. A purine nucleotide which has hypoxanthine as the base and one phosphate group esterified to the sugar moiety.
Oxidoreductases that are specific for KETONES.
An antibiotic substance derived from Penicillium stoloniferum, and related species. It blocks de novo biosynthesis of purine nucleotides by inhibition of the enzyme inosine monophosphate dehydrogenase. Mycophenolic acid is important because of its selective effects on the immune system. It prevents the proliferation of T-cells, lymphocytes, and the formation of antibodies from B-cells. It also may inhibit recruitment of leukocytes to inflammatory sites. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p1301)
Nucleosides in which the purine or pyrimidine base is combined with ribose. (Dorland, 28th ed)
Yoshida sarcoma is a rare and aggressive type of soft tissue cancer, specifically a malignant mesenchymal tumor, which was initially reported in Japan and typically occurs in children and young adults, often associated with a poor prognosis due to its rapid growth and high metastatic potential.
A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature.
A purine nucleoside that has guanine linked by its N9 nitrogen to the C1 carbon of ribose. It is a component of ribonucleic acid and its nucleotides play important roles in metabolism. (From Dorland, 28th ed)
Inosine nucleotides are purine nucleotides that contain inosine, a nucleoside with a hypoxanthine base, which can function as a weak agonist at adenosine receptors and play a role in the salvage pathways of nucleic acid metabolism.
Purines attached to a RIBOSE and a phosphate that can polymerize to form DNA and RNA.
An enzyme that catalyzes the reversible oxidation of inosine 5'-phosphate (IMP) to guanosine 5'-phosphate (GMP) in the presence of AMMONIA and NADP+. This enzyme was formerly classified as EC 1.6.6.8.
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
A nucleoside antimetabolite antiviral agent that blocks nucleic acid synthesis and is used against both RNA and DNA viruses.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
Guanine nucleotides are cyclic or linear molecules that consist of a guanine base, a pentose sugar (ribose in the cyclic form, deoxyribose in the linear form), and one or more phosphate groups, playing crucial roles in signal transduction, protein synthesis, and regulation of enzymatic activities.
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.
Nucleotides in which the purine or pyrimidine base is combined with ribose. (Dorland, 28th ed)
A purine nucleoside that has hypoxanthine linked by the N9 nitrogen to the C1 carbon of ribose. It is an intermediate in the degradation of purines and purine nucleosides to uric acid and in pathways of purine salvage. It also occurs in the anticodon of certain transfer RNA molecules. (Dorland, 28th ed)
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.
Guanine is a purine nucleobase, one of the four nucleobases in the nucleic acid of DNA and RNA, involved in forming hydrogen bonds between complementary base pairs in double-stranded DNA molecules.
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.
Glucose-6-Phosphate Dehydrogenase (G6PD) is an enzyme that plays a critical role in the pentose phosphate pathway, catalyzing the oxidation of glucose-6-phosphate to 6-phosphoglucono-δ-lactone while reducing nicotinamide adenine dinucleotide phosphate (NADP+) to nicotinamide adenine dinucleotide phosphate hydrogen (NADPH), thereby protecting cells from oxidative damage and maintaining redox balance.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
The rate dynamics in chemical or physical systems.
A series of heterocyclic compounds that are variously substituted in nature and are known also as purine bases. They include ADENINE and GUANINE, constituents of nucleic acids, as well as many alkaloids such as CAFFEINE and THEOPHYLLINE. Uric acid is the metabolic end product of purine metabolism.
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.
Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.
Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Glycerolphosphate Dehydrogenase is an enzyme (EC 1.1.1.8) that catalyzes the reversible conversion of dihydroxyacetone phosphate to glycerol 3-phosphate, using nicotinamide adenine dinucleotide (NAD+) as an electron acceptor in the process.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.
Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.
The Ketoglutarate Dehydrogenase Complex is a multi-enzyme complex involved in the citric acid cycle, catalyzing the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA and CO2, thereby connecting the catabolism of amino acids, carbohydrates, and fats to the generation of energy in the form of ATP.
Oxidoreductases that are specific for ALDEHYDES.
D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.
Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.
An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.
Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.
Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.
A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Alcohol oxidoreductases with substrate specificity for LACTIC ACID.

Mycophenolate mofetil inhibits rat and human mesangial cell proliferation by guanosine depletion. (1/295)

BACKGROUND: Mycophenolate mofetil (MMF) is used for immunosuppression after renal transplantation because it reduces lymphocyte proliferation by inhibiting inosine monophosphate dehydrogenase (IMPDH) in lymphocytes and GTP biosynthesis. In the present study we asked if therapeutic concentrations of MMF might interfere with mesangial cell (MC) proliferation which is involved in inflammatory proliferative glomerular diseases. METHODS: Rat and human MCs were growth-arrested by withdrawal of fetal calf serum (FCS) and stimulated by addition of FCS, platelet-derived growth factor (PDGF) or lysophosphatidic acid (LPA). Different concentrations of MMF (0.019-10 microM) were added concomitantly in the presence or absence of guanosine. MC proliferation was determined by [3H]thymidine incorporation. Cell viability was assessed by trypan blue exclusion. Apoptotic nuclei were stained using the Hoechst dye H33258. Cytosolic free Ca2+ concentrations were determined with the fluorescent calcium chelator fura-2-AM. RESULTS: MMF inhibited mitogen-induced rat MC proliferation with an IC50 of 0.45 +/- 0.13 microM. Human MCs proved to be even more sensitive (IC50 0.19 +/- 0.06 microM). Inhibition of MC proliferation was reversible and not accompanied by cellular necrosis or apoptosis. Addition of guanosine prevented the antiproliferative effect of MMF, indicating that inhibition of IMPDH is responsible for decreased MC proliferation. Early signalling events of GTP-binding-protein-coupled receptors, such as changes in intracellular Ca2+ levels were not affected by MMF. CONCLUSIONS: The results show that MMF has a concentration-dependent antiproliferative effect on cultured MCs in the therapeutic range, which might be a rationale for the use of this drug in the treatment of mesangial proliferative glomerulonephritis.  (+info)

Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design. (2/295)

Inosine monophosphate dehydrogenase (IMPDH) controls a key metabolic step in the regulation of cell growth and differentiation. This step is the NAD-dependent oxidation of inosine 5' monophosphate (IMP) to xanthosine 5' monophosphate, the rate-limiting step in the synthesis of the guanine nucleotides. Two isoforms of IMPDH have been identified, one of which (type II) is significantly up- regulated in neoplastic and differentiating cells. As such, it has been identified as a major target in antitumor and immunosuppressive drug design. We present here the 2.9-A structure of a ternary complex of the human type II isoform of IMPDH. The complex contains the substrate analogue 6-chloropurine riboside 5'-monophosphate (6-Cl-IMP) and the NAD analogue selenazole-4-carboxamide adenine dinucleotide, the selenium derivative of the active metabolite of the antitumor drug tiazofurin. The enzyme forms a homotetramer, with the dinucleotide binding at the monomer-monomer interface. The 6 chloro-substituted purine base is dehalogenated, forming a covalent adduct at C6 with Cys-331. The dinucleotide selenazole base is stacked against the 6-Cl-IMP purine ring in an orientation consistent with the B-side stereochemistry of hydride transfer seen with NAD. The adenosine end of the ligand interacts with residues not conserved between the type I and type II isoforms, suggesting strategies for the design of isoform-specific agents.  (+info)

Beneficial effect of the inosine monophosphate dehydrogenase inhibitor mycophenolate mofetil on survival and severity of glomerulonephritis in systemic lupus erythematosus (SLE)-prone MRLlpr/lpr mice. (3/295)

The aim of the present study was to evaluate the therapeutic effect of mycophenolate mofetil (MMF) on the course of disease in SLE-prone MRLlpr/lpr mice. Three-months-old mice displaying clinical symptoms of glomerulonephritis were given MMF (100 mg/kg per day) orally via the drinking water. Control mice received i.p. injections of cyclophosphamide (CYC) (1.8 mg/mouse per week) or saline. Survival, albuminuria and haematuria, immunoglobulin levels and anti-dsDNA antibodies in serum, frequencies of immunoglobulin-producing B lymphocytes and glomerular deposits of immunoglobulin and C3 were analysed. The results showed that MMF treatment significantly prolonged survival and reduced the occurrence of albuminuria and haematuria in MRLlpr/lpr mice. In addition, the number of immunoglobulin-producing B cells and serum levels of IgG and IgG anti-dsDNA antibodies were reduced after MMF and CYC treatment. MMF treatment significantly reduced the extent of deposition of C3 in glomeruli. We conclude that the reduced severity of glomerulonephritis following treatment of lupus-prone mice with MMF was as efficacious as that of CYC. These results warrant clinical trials of MMF in SLE patients with glomerulonephritis.  (+info)

The apparent inhibition of inosine monophosphate dehydrogenase by mycophenolic acid glucuronide is attributable to the presence of trace quantities of mycophenolic acid. (4/295)

BACKGROUND: Mycophenolic acid glucuronide, the primary metabolite of the immunosuppressive agent mycophenolic acid, affords weak inhibition of proliferating and resting lymphocytes and recombinant human inosine monophosphate dehydrogenase in comparison to the active drug. We evaluated the hypothesis that mycophenolic acid is a trace contaminant of the glucuronide metabolite preparation and that this accounts for the observed effects of mycophenolic acid glucuronide on human inosine monophosphate dehydrogenase catalytic activity both in lymphocytes and the pure enzyme. METHODS: We used negative ion electrospray HPLC-mass spectrometry (HPLC-MS) and HPLC-tandem MS (HPLC-MS-MS) to identify mycophenolic acid as a contaminant of mycophenolic acid glucuronide. Quantification of the mycophenolic acid contaminant was achieved using a negative ion electrospray HPLC-MS method in the selected-ion monitoring mode. RESULTS: Trace amounts of mycophenolic acid were detected and definitively identified in the mycophenolic acid glucuronide preparation by the HPLC-MS-MS analysis. In addition to having identical HPLC retention times, pure mycophenolic acid and the contaminant produced the following major fragments upon HPLC-MS-MS analysis: deprotonated molecular ion, m/z 319; and fragment ions, m/z 275, 243, 205, and 191 (the most abundant fragment ion). Using the negative ion electrospray HPLC-MS procedure in the selected-ion monitoring mode, the quantity of the contaminant mycophenolic acid was determined to be 0.312% +/- 0.0184% on a molar basis. CONCLUSION: These data provide strong support for the proposal that the apparent inhibition of the target enzyme inosine monophosphate dehydrogenase by mycophenolic acid glucuronide is attributable to the presence of trace amounts of contaminant mycophenolic acid.  (+info)

Benzamide riboside induces apoptosis independent of Cdc25A expression in human ovarian carcinoma N.1 cells. (5/295)

One of the mechanisms of action of a new oncolytic agent, benzamide riboside (BR) is by inhibiting inosine 5'-monophosphate dehydrogenase (IMPDH) which catalyzes the formation of xanthine 5'-monophosphate from inosine 5'-monophosphate and nicotinamide adenine dinucleotide, thereby restricting the biosynthesis of guanylates. In the present study BR (10 - 20 microM) induced apoptosis in a human ovarian carcinoma N.1 cell line (a monoclonal derivative of its heterogenous parent line HOC-7). This was ascertained by DNA fragmentation, TUNEL assay, [poly(ADP)ribose polymerase]-cleavage and alteration in cell morphology. Apoptosis was accompanied by sustained c-Myc expression, concurrent down-regulation of cdc25A mRNA and protein, and by inhibition of Cdk2 activity. Both Cdk2 and cdc25A are G1 phase specific genes and Cdk2 is the target of Cdc25A. These studies demonstrate that BR exhibits dual mechanisms of action, first by inhibiting IMPDH, and second by inducing apoptosis, which is associated with repression of components of the cell cycle that are downstream of constitutive c-Myc expression.  (+info)

The SHAPES strategy: an NMR-based approach for lead generation in drug discovery. (6/295)

BACKGROUND: Recently, it has been shown that nuclear magnetic resonance (NMR) may be used to identify ligands that bind to low molecular weight protein drug targets. Recognizing the utility of NMR as a very sensitive method for detecting binding, we have focused on developing alternative approaches that are applicable to larger molecular weight drug targets and do not require isotopic labeling. RESULTS: A new method for lead generation (SHAPES) is described that uses NMR to detect binding of a limited but diverse library of small molecules to a potential drug target. The compound scaffolds are derived from shapes most commonly found in known therapeutic agents. NMR detection of low (microM-mM) affinity binding is achieved using either differential line broadening or transferred NOE (nuclear Overhauser effect) NMR techniques. CONCLUSIONS: The SHAPES method for lead generation by NMR is useful for identifying potential lead classes of drugs early in a drug design program, and is easily integrated with other discovery tools such as virtual screening, high-throughput screening and combinatorial chemistry.  (+info)

Theoretical studies of the conformational properties of ribavirin. (7/295)

One of the factors required for the antiviral activity of the synthetic nucleoside, ribavirin (1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide), is the ability of the molecule to adopt the substrate conformation specified by the enzyme for which it is a competitive inhibitor, inosine 5'-phosphate dehydrogenase (IMP:NAD+ oxidoreductase, EC 1.2.1.14). The calculated glycosidic minimum for ribavirin is the high syn conformation, which is in agreement with experimental determinations of the molecule's solution conformation. The similarity in solution between the conformation of the active ribavirin molecule and the conformation of its inactive 5-methyl and 5-chloro derivatives indicate that some other substrate conformation is specified by the enzyme. The high anti conformation, found by these calculations to be close in energy to the high syn minimum, is postulated to be the active conformation required by the enzyme. The inactivity of the 5-methyl and 5-chloro derivatives is attributed to the much greater stability of these derivatives in the inactive high syn conformation.  (+info)

Broad-spectrum antiviral activity of the IMP dehydrogenase inhibitor VX-497: a comparison with ribavirin and demonstration of antiviral additivity with alpha interferon. (8/295)

The enzyme IMP dehydrogenase (IMPDH) catalyzes an essential step in the de novo biosynthesis of guanine nucleotides, namely, the conversion of IMP to XMP. The major event occurring in cells exposed to competitive IMPDH inhibitors such as ribavirin or uncompetitive inhibitors such as mycophenolic acid (MPA) is a depletion of the intracellular GTP and dGTP pools. Ribavirin is approved as an inhaled antiviral agent for treatment of respiratory syncytial virus (RSV) infection and orally, in combination with alpha interferon (IFN-alpha), for the treatment of chronic hepatitis C virus (HCV) infection. VX-497 is a potent, reversible uncompetitive IMPDH inhibitor which is structurally unrelated to other known IMPDH inhibitors. Studies were performed to compare VX-497 and ribavirin in terms of their cytotoxicities and their efficacies against a variety of viruses. They included DNA viruses (hepatitis B virus [HBV], human cytomegalovirus [HCMV], and herpes simplex virus type 1 [HSV-1]) and RNA viruses (respiratory syncytial virus [RSV], parainfluenza-3 virus, bovine viral diarrhea virus, Venezuelan equine encephalomyelitis virus [VEEV], dengue virus, yellow fever virus, coxsackie B3 virus, encephalomyocarditis virus [EMCV], and influenza A virus). VX-497 was 17- to 186-fold more potent than ribavirin against HBV, HCMV, RSV, HSV-1, parainfluenza-3 virus, EMCV, and VEEV infections in cultured cells. The therapeutic index of VX-497 was significantly better than that of ribavirin for HBV and HCMV (14- and 39-fold, respectively). Finally, the antiviral effect of VX-497 in combination with IFN-alpha was compared to that of ribavirin with IFN-alpha in the EMCV replication system. Both VX-497 and ribavirin demonstrated additivity when coapplied with IFN-alpha, with VX-497 again being the more potent in this combination. These data are supportive of the hypothesis that VX-497, like ribavirin, is a broad-spectrum antiviral agent.  (+info)

Inosine Monophosphate Dehydrogenase (IMDH or IMPDH) is an enzyme that is involved in the de novo biosynthesis of guanine nucleotides. It catalyzes the conversion of inosine monophosphate (IMP) to xanthosine monophosphate (XMP), which is the rate-limiting step in the synthesis of guanosine triphosphate (GTP).

There are two isoforms of IMPDH, type I and type II, which are encoded by separate genes. Type I IMPDH is expressed in most tissues, while type II IMPDH is primarily expressed in lymphocytes and other cells involved in the immune response. Inhibitors of IMPDH have been developed as immunosuppressive drugs to prevent rejection of transplanted organs. Defects in the gene encoding IMPDH type II have been associated with retinal degeneration and hearing loss.

Inosine monophosphate (IMP) is a nucleotide that plays a crucial role in the metabolic pathways of energy production and purine synthesis in cells. It is an ester of the nucleoside inosine and phosphoric acid. IMP is an important intermediate in the conversion of adenosine monophosphate (AMP) to guanosine monophosphate (GMP) in the purine nucleotide cycle, which is critical for maintaining the balance of purine nucleotides in the body. Additionally, IMP can be converted back to AMP through the action of the enzyme adenylosuccinate lyase. IMP has been studied for its potential therapeutic benefits in various medical conditions, including neurodegenerative disorders and ischemia-reperfusion injury.

Ketone oxidoreductases are a group of enzymes that catalyze the conversion of ketones to corresponding alcohols or vice versa, through the process of reduction or oxidation. These enzymes play an essential role in various metabolic pathways and biochemical reactions within living organisms.

In the context of medical research and diagnostics, ketone oxidoreductases have gained attention for their potential applications in the development of biosensors to detect and monitor blood ketone levels, particularly in patients with diabetes. Elevated levels of ketones in the blood (known as ketonemia) can indicate a serious complication called diabetic ketoacidosis, which requires prompt medical attention.

One example of a ketone oxidoreductase is the enzyme known as d-beta-hydroxybutyrate dehydrogenase (d-BDH), which catalyzes the conversion of d-beta-hydroxybutyrate to acetoacetate. This reaction is part of the metabolic pathway that breaks down fatty acids for energy production, and it becomes particularly important during periods of low carbohydrate availability or insulin deficiency, as seen in diabetes.

Understanding the function and regulation of ketone oxidoreductases can provide valuable insights into the pathophysiology of metabolic disorders like diabetes and contribute to the development of novel therapeutic strategies for their management.

Mycophenolic Acid (MPA) is an immunosuppressive drug that is primarily used to prevent rejection in organ transplantation. It works by inhibiting the enzyme inosine monophosphate dehydrogenase, which is a key enzyme for the de novo synthesis of guanosine nucleotides, an essential component for the proliferation of T and B lymphocytes. By doing this, MPA reduces the activity of the immune system, thereby preventing it from attacking the transplanted organ.

Mycophenolic Acid is available in two forms: as the sodium salt (Mycophenolate Sodium) and as the morpholinoethyl ester (Mycophenolate Mofetil), which is rapidly hydrolyzed to Mycophenolic Acid after oral administration. Common side effects of MPA include gastrointestinal symptoms such as diarrhea, nausea, and vomiting, as well as an increased risk of infections due to its immunosuppressive effects.

Ribonucleosides are organic compounds that consist of a nucleoside bound to a ribose sugar. Nucleosides are formed when a nitrogenous base (such as adenine, guanine, uracil, cytosine, or thymine) is attached to a sugar molecule (either ribose or deoxyribose) via a beta-glycosidic bond. In the case of ribonucleosides, the sugar component is D-ribose. Ribonucleosides play important roles in various biological processes, particularly in the storage, transfer, and expression of genetic information within cells. When ribonucleosides are phosphorylated, they become the building blocks of RNA (ribonucleic acid), a crucial biomolecule involved in protein synthesis and other cellular functions. Examples of ribonucleosides include adenosine, guanosine, uridine, cytidine, and inosine.

I'm sorry for the confusion, but "Sarcoma, Yoshida" is not a recognized medical term or a specific type of sarcoma in any major oncology reference or database. It appears that "Yoshida" might be referring to a person who described or studied a particular type of sarcoma. However, I cannot find any relevant information related to this exact term.

Sarcomas are cancers that develop from connective tissues such as bones, muscles, tendons, cartilages, nerves, and blood vessels. They can be categorized into two main groups: bone sarcomas and soft tissue sarcomas. There are many subtypes of sarcoma, each with its unique features, diagnostic criteria, and treatment approaches.

If you have more context or information about "Sarcoma, Yoshida," I would be happy to help you further research the topic. However, based on the available data, it is not possible to provide a medical definition for this term.

Guanosine monophosphate (GMP) is a nucleotide that is a fundamental unit of genetic material in DNA and RNA. It consists of a guanine base, a pentose sugar (ribose in the case of RNA, deoxyribose in DNA), and one phosphate group. GMP plays crucial roles in various biochemical reactions within cells, including energy transfer and signal transduction pathways. Additionally, it is involved in the synthesis of important molecules like nucleic acids, neurotransmitters, and hormones.

Guanosine is a nucleoside that consists of a guanine base linked to a ribose sugar molecule through a beta-N9-glycosidic bond. It plays a crucial role in various biological processes, such as serving as a building block for DNA and RNA during replication and transcription. Guanosine triphosphate (GTP) and guanosine diphosphate (GDP) are important energy carriers and signaling molecules involved in intracellular regulation. Additionally, guanosine has been studied for its potential role as a neuroprotective agent and possible contribution to cell-to-cell communication.

Inosine nucleotides are chemical compounds that play a role in the metabolism of nucleic acids, which are the building blocks of DNA and RNA. Inosine is a purine nucleoside that is formed when adenosine (a normal component of DNA and RNA) is deaminated, or has an amino group (-NH2) removed from its structure.

Inosine nucleotides are important in the salvage pathway of nucleotide synthesis, which allows cells to recycle existing nucleotides rather than synthesizing them entirely from scratch. Inosine nucleotides can be converted back into adenosine nucleotides through a process called reversal of deamination.

Inosine nucleotides also have important functions in the regulation of gene expression and in the response to cellular stress. For example, they can act as signaling molecules that activate various enzymes and pathways involved in DNA repair, apoptosis (programmed cell death), and other cellular processes.

Inosine nucleotides have been studied for their potential therapeutic uses in a variety of conditions, including neurological disorders, cancer, and viral infections. However, more research is needed to fully understand their mechanisms of action and potential benefits.

Purine nucleotides are fundamental units of life that play crucial roles in various biological processes. A purine nucleotide is a type of nucleotide, which is the basic building block of nucleic acids such as DNA and RNA. Nucleotides consist of a nitrogenous base, a pentose sugar, and at least one phosphate group.

In purine nucleotides, the nitrogenous bases are either adenine (A) or guanine (G). These bases are attached to a five-carbon sugar called ribose in the case of RNA or deoxyribose for DNA. The sugar and base together form the nucleoside, while the addition of one or more phosphate groups creates the nucleotide.

Purine nucleotides have several vital functions within cells:

1. Energy currency: Adenosine triphosphate (ATP) is a purine nucleotide that serves as the primary energy currency in cells, storing and transferring chemical energy for various cellular processes.
2. Genetic material: Both DNA and RNA contain purine nucleotides as essential components of their structures. Adenine pairs with thymine (in DNA) or uracil (in RNA), while guanine pairs with cytosine.
3. Signaling molecules: Purine nucleotides, such as adenosine monophosphate (AMP) and cyclic adenosine monophosphate (cAMP), act as intracellular signaling molecules that regulate various cellular functions, including metabolism, gene expression, and cell growth.
4. Coenzymes: Purine nucleotides can also function as coenzymes, assisting enzymes in catalyzing biochemical reactions. For example, nicotinamide adenine dinucleotide (NAD+) is a purine nucleotide that plays a critical role in redox reactions and energy metabolism.

In summary, purine nucleotides are essential biological molecules involved in various cellular functions, including energy transfer, genetic material formation, intracellular signaling, and enzyme cofactor activity.

GMP (guanosine monophosphate) reductase is an enzyme that plays a crucial role in the metabolism of nucleotides, specifically within the purine nucleotide pathway. This enzyme catalyzes the NADH-dependent reduction of GMP to IMP (inosine monophosphate), which is a key step in the de novo biosynthesis of purines and the salvage pathways for purine nucleotides.

GMP reductase is found in various organisms, including bacteria, fungi, and plants. In humans, two isoforms of GMP reductase exist: a cytosolic form (IRI1) and a mitochondrial form (IRI2). The enzyme's activity is tightly regulated, as it is involved in balancing the intracellular pools of purine nucleotides. Dysregulation of GMP reductase has been implicated in several diseases, such as cancer and neurological disorders.

Medical Definition:
GMP reductase (guanosine monophosphate reductase): An enzyme (EC 1.17.1.4) that catalyzes the NADH-dependent reduction of GMP to IMP, with the concomitant formation of hydrogen peroxide (H2O2). This enzyme is involved in the de novo biosynthesis and salvage pathways of purine nucleotides. In humans, two isoforms of GMP reductase exist: a cytosolic form (IRI1) and a mitochondrial form (IRI2).

L-Lactate Dehydrogenase (LDH) is an enzyme found in various tissues within the body, including the heart, liver, kidneys, muscles, and brain. It plays a crucial role in the process of energy production, particularly during anaerobic conditions when oxygen levels are low.

In the presence of the coenzyme NADH, LDH catalyzes the conversion of pyruvate to lactate, generating NAD+ as a byproduct. Conversely, in the presence of NAD+, LDH can convert lactate back to pyruvate using NADH. This reversible reaction is essential for maintaining the balance between lactate and pyruvate levels within cells.

Elevated blood levels of LDH may indicate tissue damage or injury, as this enzyme can be released into the circulation following cellular breakdown. As a result, LDH is often used as a nonspecific biomarker for various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and certain types of cancer. However, it's important to note that an isolated increase in LDH does not necessarily pinpoint the exact location or cause of tissue damage, and further diagnostic tests are usually required for confirmation.

Ribavirin is an antiviral medication used in the treatment of certain viral infections, including hepatitis C and respiratory syncytial virus (RSV) infection. It works by interfering with viral replication, preventing the virus from multiplying within infected cells. Ribavirin is often used in combination with other antiviral drugs for more effective treatment.

It's important to note that ribavirin can have serious side effects and should only be used under the supervision of a healthcare professional. Additionally, it is not effective against all types of viral infections and its use should be based on a confirmed diagnosis and appropriate medical evaluation.

Alcohol dehydrogenase (ADH) is a group of enzymes responsible for catalyzing the oxidation of alcohols to aldehydes or ketones, and reducing equivalents such as NAD+ to NADH. In humans, ADH plays a crucial role in the metabolism of ethanol, converting it into acetaldehyde, which is then further metabolized by aldehyde dehydrogenase (ALDH) into acetate. This process helps to detoxify and eliminate ethanol from the body. Additionally, ADH enzymes are also involved in the metabolism of other alcohols, such as methanol and ethylene glycol, which can be toxic if allowed to accumulate in the body.

Guanine nucleotides are molecules that play a crucial role in intracellular signaling, cellular regulation, and various biological processes within cells. They consist of a guanine base, a sugar (ribose or deoxyribose), and one or more phosphate groups. The most common guanine nucleotides are GDP (guanosine diphosphate) and GTP (guanosine triphosphate).

GTP is hydrolyzed to GDP and inorganic phosphate by certain enzymes called GTPases, releasing energy that drives various cellular functions such as protein synthesis, signal transduction, vesicle transport, and cell division. On the other hand, GDP can be rephosphorylated back to GTP by nucleotide diphosphate kinases, allowing for the recycling of these molecules within the cell.

In addition to their role in signaling and regulation, guanine nucleotides also serve as building blocks for RNA (ribonucleic acid) synthesis during transcription, where they pair with cytosine nucleotides via hydrogen bonds to form base pairs in the resulting RNA molecule.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme that plays a crucial role in the metabolic pathway of glycolysis. Its primary function is to convert glyceraldehyde-3-phosphate (a triose sugar phosphate) into D-glycerate 1,3-bisphosphate, while also converting nicotinamide adenine dinucleotide (NAD+) into its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has also been implicated in various non-metabolic processes, including DNA replication, repair, and transcription regulation, due to its ability to interact with different proteins and nucleic acids.

Ribonucleotides are organic compounds that consist of a ribose sugar, a phosphate group, and a nitrogenous base. They are the building blocks of RNA (ribonucleic acid), one of the essential molecules in all living organisms. The nitrogenous bases found in ribonucleotides include adenine, uracil, guanine, and cytosine. These molecules play crucial roles in various biological processes, such as protein synthesis, gene expression, and cellular energy production. Ribonucleotides can also be involved in cell signaling pathways and serve as important cofactors for enzymatic reactions.

Inosine is not a medical condition but a naturally occurring compound called a nucleoside, which is formed from the combination of hypoxanthine and ribose. It is an intermediate in the metabolic pathways of purine nucleotides, which are essential components of DNA and RNA. Inosine has been studied for its potential therapeutic benefits in various medical conditions, including neurodegenerative disorders, cardiovascular diseases, and cancer. However, more research is needed to fully understand its mechanisms and clinical applications.

Aldehyde dehydrogenase (ALDH) is a class of enzymes that play a crucial role in the metabolism of alcohol and other aldehydes in the body. These enzymes catalyze the oxidation of aldehydes to carboxylic acids, using nicotinamide adenine dinucleotide (NAD+) as a cofactor.

There are several isoforms of ALDH found in different tissues throughout the body, with varying substrate specificities and kinetic properties. The most well-known function of ALDH is its role in alcohol metabolism, where it converts the toxic aldehyde intermediate acetaldehyde to acetate, which can then be further metabolized or excreted.

Deficiencies in ALDH activity have been linked to a number of clinical conditions, including alcohol flush reaction, alcohol-induced liver disease, and certain types of cancer. Additionally, increased ALDH activity has been associated with chemotherapy resistance in some cancer cells.

Guanine is not a medical term per se, but it is a biological molecule that plays a crucial role in the body. Guanine is one of the four nucleobases found in the nucleic acids DNA and RNA, along with adenine, cytosine, and thymine (in DNA) or uracil (in RNA). Specifically, guanine pairs with cytosine via hydrogen bonds to form a base pair.

Guanine is a purine derivative, which means it has a double-ring structure. It is formed through the synthesis of simpler molecules in the body and is an essential component of genetic material. Guanine's chemical formula is C5H5N5O.

While guanine itself is not a medical term, abnormalities or mutations in genes that contain guanine nucleotides can lead to various medical conditions, including genetic disorders and cancer.

Glutamate Dehydrogenase (GLDH or GDH) is a mitochondrial enzyme that plays a crucial role in the metabolism of amino acids, particularly within liver and kidney tissues. It catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate, which links amino acid metabolism with the citric acid cycle and energy production. This enzyme is significant in clinical settings as its levels in blood serum can be used as a diagnostic marker for diseases that damage liver or kidney cells, since these cells release GLDH into the bloodstream upon damage.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also known as Glucosephosphate Dehydrogenase, is an enzyme that plays a crucial role in cellular metabolism, particularly in the glycolytic pathway. It catalyzes the conversion of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (1,3-BPG), while also converting nicotinamide adenine dinucleotide (NAD+) to its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has been widely used as a housekeeping gene in molecular biology research due to its consistent expression across various tissues and cells, although recent studies have shown that its expression can vary under certain conditions.

Malate Dehydrogenase (MDH) is an enzyme that plays a crucial role in the Krebs cycle, also known as the citric acid cycle or tricarboxylic acid (TCA) cycle. It catalyzes the reversible oxidation of malate to oxaloacetate, while simultaneously reducing NAD+ to NADH. This reaction is essential for energy production in the form of ATP and NADH within the cell.

There are two main types of Malate Dehydrogenase:

1. NAD-dependent Malate Dehydrogenase (MDH1): Found primarily in the cytoplasm, this isoform plays a role in the malate-aspartate shuttle, which helps transfer reducing equivalents between the cytoplasm and mitochondria.
2. FAD-dependent Malate Dehydrogenase (MDH2): Located within the mitochondrial matrix, this isoform is involved in the Krebs cycle for energy production.

Abnormal levels of Malate Dehydrogenase enzyme can be indicative of certain medical conditions or diseases, such as myocardial infarction (heart attack), muscle damage, or various types of cancer. Therefore, MDH enzyme activity is often assessed in diagnostic tests to help identify and monitor these health issues.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Purines are heterocyclic aromatic organic compounds that consist of a pyrimidine ring fused to an imidazole ring. They are fundamental components of nucleotides, which are the building blocks of DNA and RNA. In the body, purines can be synthesized endogenously or obtained through dietary sources such as meat, seafood, and certain vegetables.

Once purines are metabolized, they are broken down into uric acid, which is excreted by the kidneys. Elevated levels of uric acid in the body can lead to the formation of uric acid crystals, resulting in conditions such as gout or kidney stones. Therefore, maintaining a balanced intake of purine-rich foods and ensuring proper kidney function are essential for overall health.

Isocitrate Dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate to α-ketoglutarate in the presence of NAD+ or NADP+, producing NADH or NADPH respectively. This reaction occurs in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, which is a crucial metabolic pathway in the cell's energy production and biosynthesis of various molecules. There are three isoforms of IDH found in humans: IDH1 located in the cytosol, IDH2 in the mitochondrial matrix, and IDH3 within the mitochondria. Mutations in IDH1 and IDH2 have been associated with several types of cancer, such as gliomas and acute myeloid leukemia (AML), leading to abnormal accumulation of 2-hydroxyglutarate, which can contribute to tumorigenesis.

Guanosine triphosphate (GTP) is a nucleotide that plays a crucial role in various cellular processes, such as protein synthesis, signal transduction, and regulation of enzymatic activities. It serves as an energy currency, similar to adenosine triphosphate (ATP), and undergoes hydrolysis to guanosine diphosphate (GDP) or guanosine monophosphate (GMP) to release energy required for these processes. GTP is also a precursor for the synthesis of other essential molecules, including RNA and certain signaling proteins. Additionally, it acts as a molecular switch in many intracellular signaling pathways by binding and activating specific GTPase proteins.

Alcohol oxidoreductases are a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones, while reducing nicotinamide adenine dinucleotide (NAD+) to NADH. These enzymes play an important role in the metabolism of alcohols and other organic compounds in living organisms.

The most well-known example of an alcohol oxidoreductase is alcohol dehydrogenase (ADH), which is responsible for the oxidation of ethanol to acetaldehyde in the liver during the metabolism of alcoholic beverages. Other examples include aldehyde dehydrogenases (ALDH) and sorbitol dehydrogenase (SDH).

These enzymes are important targets for the development of drugs used to treat alcohol use disorder, as inhibiting their activity can help to reduce the rate of ethanol metabolism and the severity of its effects on the body.

Dihydrolipoamide dehydrogenase (DHLD) is an enzyme that plays a crucial role in several important metabolic pathways in the human body, including the citric acid cycle and the catabolism of certain amino acids. DHLD is a component of multi-enzyme complexes, such as the pyruvate dehydrogenase complex (PDC) and the alpha-ketoglutarate dehydrogenase complex (KGDC).

The primary function of DHLD is to catalyze the oxidation of dihydrolipoamide, a reduced form of lipoamide, back to its oxidized state (lipoamide) while simultaneously reducing NAD+ to NADH. This reaction is essential for the continued functioning of the PDC and KGDC, as dihydrolipoamide is a cofactor for these enzyme complexes.

Deficiencies in DHLD can lead to serious metabolic disorders, such as maple syrup urine disease (MSUD) and riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency (RR-MADD). These conditions can result in neurological symptoms, developmental delays, and metabolic acidosis, among other complications. Treatment typically involves dietary modifications, supplementation with specific nutrients, and, in some cases, enzyme replacement therapy.

Carbohydrate dehydrogenases are a group of enzymes that catalyze the oxidation of carbohydrates, including sugars and sugar alcohols. These enzymes play a crucial role in cellular metabolism by helping to convert these molecules into forms that can be used for energy or as building blocks for other biological compounds.

During the oxidation process, carbohydrate dehydrogenases remove hydrogen atoms from the carbohydrate substrate and transfer them to an electron acceptor, such as NAD+ or FAD. This results in the formation of a ketone or aldehyde group on the carbohydrate molecule and the reduction of the electron acceptor to NADH or FADH2.

Carbohydrate dehydrogenases are classified into several subgroups based on their substrate specificity, cofactor requirements, and other factors. Some examples include glucose dehydrogenase, galactose dehydrogenase, and sorbitol dehydrogenase.

These enzymes have important applications in various fields, including biotechnology, medicine, and industry. For example, they can be used to detect or quantify specific carbohydrates in biological samples, or to produce valuable chemical compounds through the oxidation of renewable resources such as plant-derived sugars.

Succinate dehydrogenase (SDH) is an enzyme complex that plays a crucial role in the process of cellular respiration, specifically in the citric acid cycle (also known as the Krebs cycle) and the electron transport chain. It is located in the inner mitochondrial membrane of eukaryotic cells.

SDH catalyzes the oxidation of succinate to fumarate, converting it into a molecule of fadaquate in the process. During this reaction, two electrons are transferred from succinate to the FAD cofactor within the SDH enzyme complex, reducing it to FADH2. These electrons are then passed on to ubiquinone (CoQ), which is a mobile electron carrier in the electron transport chain, leading to the generation of ATP, the main energy currency of the cell.

SDH is also known as mitochondrial complex II because it is the second complex in the electron transport chain. Mutations in the genes encoding SDH subunits or associated proteins have been linked to various human diseases, including hereditary paragangliomas, pheochromocytomas, gastrointestinal stromal tumors (GISTs), and some forms of neurodegenerative disorders.

L-Iditol 2-Dehydrogenase is an enzyme that catalyzes the chemical reaction between L-iditol and NAD+ to produce L-sorbose and NADH + H+. This enzyme plays a role in the metabolism of sugars, specifically in the conversion of L-iditol to L-sorbose in various organisms, including bacteria and fungi. The reaction catalyzed by this enzyme is part of the polyol pathway, which is involved in the regulation of osmotic pressure and other cellular processes.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Glycerol-3-phosphate dehydrogenase (GPD) is an enzyme that plays a crucial role in the metabolism of glucose and lipids. It catalyzes the conversion of dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate (G3P), which is a key intermediate in the synthesis of triglycerides, phospholipids, and other glycerophospholipids.

There are two main forms of GPD: a cytoplasmic form (GPD1) and a mitochondrial form (GPD2). The cytoplasmic form is involved in the production of NADH, which is used in various metabolic processes, while the mitochondrial form is involved in the production of ATP, the main energy currency of the cell.

Deficiencies or mutations in GPD can lead to a variety of metabolic disorders, including glycerol kinase deficiency and congenital muscular dystrophy. Elevated levels of GPD have been observed in certain types of cancer, suggesting that it may play a role in tumor growth and progression.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

Glucose 1-Dehydrogenase (G1DH) is an enzyme that catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone and reduces the cofactor NAD+ into NADH. This reaction plays a role in various biological processes, including glucose sensing and detoxification of reactive carbonyl species. G1DH is found in many organisms, including humans, and has several isoforms with different properties and functions.

Hydroxysteroid dehydrogenases (HSDs) are a group of enzymes that play a crucial role in steroid hormone metabolism. They catalyze the oxidation and reduction reactions of hydroxyl groups on the steroid molecule, which can lead to the activation or inactivation of steroid hormones. HSDs are involved in the conversion of various steroids, including sex steroids (e.g., androgens, estrogens) and corticosteroids (e.g., cortisol, cortisone). These enzymes can be found in different tissues throughout the body, and their activity is regulated by various factors, such as hormones, growth factors, and cytokines. Dysregulation of HSDs has been implicated in several diseases, including cancer, diabetes, and cardiovascular disease.

The Ketoglutarate Dehydrogenase Complex (KGDC or α-KGDH) is a multi-enzyme complex that plays a crucial role in the Krebs cycle, also known as the citric acid cycle. It is located within the mitochondrial matrix of eukaryotic cells and functions to catalyze the oxidative decarboxylation of α-ketoglutarate into succinyl-CoA, thereby connecting the Krebs cycle to the electron transport chain for energy production.

The KGDC is composed of three distinct enzymes:

1. α-Ketoglutarate dehydrogenase (E1): This enzyme catalyzes the decarboxylation and oxidation of α-ketoglutarate to form a thioester intermediate with lipoamide, which is bound to the E2 component.
2. Dihydrolipoyl succinyltransferase (E2): This enzyme facilitates the transfer of the acetyl group from the lipoamide cofactor to CoA, forming succinyl-CoA and regenerating oxidized lipoamide.
3. Dihydrolipoyl dehydrogenase (E3): The final enzyme in the complex catalyzes the reoxidation of reduced lipoamide back to its disulfide form, using FAD as a cofactor and transferring electrons to NAD+, forming NADH.

The KGDC is subject to regulation by several mechanisms, including phosphorylation-dephosphorylation reactions that can inhibit or activate the complex, respectively. Dysfunction of this enzyme complex has been implicated in various diseases, such as neurodegenerative disorders and cancer.

Aldehyde oxidoreductases are a class of enzymes that catalyze the oxidation of aldehydes to carboxylic acids using NAD+ or FAD as cofactors. They play a crucial role in the detoxification of aldehydes generated from various metabolic processes, such as lipid peroxidation and alcohol metabolism. These enzymes are widely distributed in nature and have been identified in bacteria, yeast, plants, and animals.

The oxidation reaction catalyzed by aldehyde oxidoreductases involves the transfer of electrons from the aldehyde substrate to the cofactor, resulting in the formation of a carboxylic acid and reduced NAD+ or FAD. The enzymes are classified into several families based on their sequence similarity and cofactor specificity.

One of the most well-known members of this family is alcohol dehydrogenase (ADH), which catalyzes the oxidation of alcohols to aldehydes or ketones as part of the alcohol metabolism pathway. Another important member is aldehyde dehydrogenase (ALDH), which further oxidizes the aldehydes generated by ADH to carboxylic acids, thereby preventing the accumulation of toxic aldehydes in the body.

Deficiencies in ALDH enzymes have been linked to several human diseases, including alcoholism and certain types of cancer. Therefore, understanding the structure and function of aldehyde oxidoreductases is essential for developing new therapeutic strategies to treat these conditions.

Glucose dehydrogenases (GDHs) are a group of enzymes that catalyze the oxidation of glucose to generate gluconic acid or glucuronic acid. This reaction involves the transfer of electrons from glucose to an electron acceptor, most commonly nicotinamide adenine dinucleotide (NAD+) or phenazine methosulfate (PMS).

GDHs are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They play important roles in different biological processes, such as glucose metabolism, energy production, and detoxification of harmful substances. Based on their cofactor specificity, GDHs can be classified into two main types: NAD(P)-dependent GDHs and PQQ-dependent GDHs.

NAD(P)-dependent GDHs use NAD+ or NADP+ as a cofactor to oxidize glucose to glucono-1,5-lactone, which is then hydrolyzed to gluconic acid by an accompanying enzyme. These GDHs are involved in various metabolic pathways, such as the Entner-Doudoroff pathway and the oxidative pentose phosphate pathway.

PQQ-dependent GDHs, on the other hand, use pyrroloquinoline quinone (PQQ) as a cofactor to catalyze the oxidation of glucose to gluconic acid directly. These GDHs are typically found in bacteria and play a role in energy production and detoxification.

Overall, glucose dehydrogenases are essential enzymes that contribute to the maintenance of glucose homeostasis and energy balance in living organisms.

3-Hydroxysteroid dehydrogenases (3-HSDs) are a group of enzymes that play a crucial role in steroid hormone biosynthesis. These enzymes catalyze the conversion of 3-beta-hydroxy steroids to 3-keto steroids, which is an essential step in the production of various steroid hormones, including progesterone, cortisol, aldosterone, and sex hormones such as testosterone and estradiol.

There are several isoforms of 3-HSDs that are expressed in different tissues and have distinct substrate specificities. For instance, 3-HSD type I is primarily found in the ovary and adrenal gland, where it catalyzes the conversion of pregnenolone to progesterone and 17-hydroxyprogesterone to 17-hydroxycortisol. On the other hand, 3-HSD type II is mainly expressed in the testes, adrenal gland, and placenta, where it catalyzes the conversion of dehydroepiandrosterone (DHEA) to androstenedione and androstenedione to testosterone.

Defects in 3-HSDs can lead to various genetic disorders that affect steroid hormone production and metabolism, resulting in a range of clinical manifestations such as adrenal insufficiency, ambiguous genitalia, and sexual development disorders.

Phosphogluconate dehydrogenase (PGD) is an enzyme that plays a crucial role in the pentose phosphate pathway, which is a metabolic pathway that supplies reducing energy to cells by converting glucose into ribose-5-phosphate and NADPH.

PGD catalyzes the third step of this pathway, in which 6-phosphogluconate is converted into ribulose-5-phosphate, with the concurrent reduction of NADP+ to NADPH. This reaction is essential for the generation of NADPH, which serves as a reducing agent in various cellular processes, including fatty acid synthesis and antioxidant defense.

Deficiencies in PGD can lead to several metabolic disorders, such as congenital nonspherocytic hemolytic anemia, which is characterized by the premature destruction of red blood cells due to a defect in the pentose phosphate pathway.

Sugar alcohol dehydrogenases (SADHs) are a group of enzymes that catalyze the interconversion between sugar alcohols and sugars, which involves the gain or loss of a pair of electrons, typically in the form of NAD(P)+/NAD(P)H. These enzymes play a crucial role in the metabolism of sugar alcohols, which are commonly found in various plants and some microorganisms.

Sugar alcohols, also known as polyols, are reduced forms of sugars that contain one or more hydroxyl groups instead of aldehyde or ketone groups. Examples of sugar alcohols include sorbitol, mannitol, xylitol, and erythritol. SADHs can interconvert these sugar alcohols to their corresponding sugars through a redox reaction that involves the transfer of hydrogen atoms.

The reaction catalyzed by SADHs is typically represented as follows:

R-CH(OH)-CH2OH + NAD(P)+ ↔ R-CO-CH2OH + NAD(P)H + H+

where R represents a carbon chain, and CH(OH)-CH2OH and CO-CH2OH represent the sugar alcohol and sugar forms, respectively.

SADHs are widely distributed in nature and have been found in various organisms, including bacteria, fungi, plants, and animals. These enzymes have attracted significant interest in biotechnology due to their potential applications in the production of sugar alcohols and other value-added products. Additionally, SADHs have been studied as targets for developing novel antimicrobial agents, as inhibiting these enzymes can disrupt the metabolism of certain pathogens that rely on sugar alcohols for growth and survival.

Acyl-CoA dehydrogenases are a group of enzymes that play a crucial role in the body's energy production process. They are responsible for catalyzing the oxidation of various fatty acids, which are broken down into smaller molecules called acyl-CoAs in the body.

More specifically, acyl-CoA dehydrogenases facilitate the removal of electrons from the acyl-CoA molecules, which are then transferred to coenzyme Q10 and eventually to the electron transport chain. This process generates energy in the form of ATP, which is used by cells throughout the body for various functions.

There are several different types of acyl-CoA dehydrogenases, each responsible for oxidizing a specific type of acyl-CoA molecule. These include:

* Very long-chain acyl-CoA dehydrogenase (VLCAD), which oxidizes acyl-CoAs with 12 to 20 carbon atoms
* Long-chain acyl-CoA dehydrogenase (LCAD), which oxidizes acyl-CoAs with 14 to 20 carbon atoms
* Medium-chain acyl-CoA dehydrogenase (MCAD), which oxidizes acyl-CoAs with 6 to 12 carbon atoms
* Short-chain acyl-CoA dehydrogenase (SCAD), which oxidizes acyl-CoAs with 4 to 8 carbon atoms
* Isovaleryl-CoA dehydrogenase, which oxidizes isovaleryl-CoA, a specific type of branched-chain acyl-CoA molecule

Deficiencies in these enzymes can lead to various metabolic disorders, such as medium-chain acyl-CoA dehydrogenase deficiency (MCADD) or long-chain acyl-CoA dehydrogenase deficiency (LCADD), which can cause symptoms such as hypoglycemia, muscle weakness, and developmental delays.

NADH dehydrogenase, also known as Complex I, is an enzyme complex in the electron transport chain located in the inner mitochondrial membrane. It catalyzes the oxidation of NADH to NAD+ and the reduction of coenzyme Q to ubiquinol, playing a crucial role in cellular respiration and energy production. The reaction involves the transfer of electrons from NADH to coenzyme Q, which contributes to the generation of a proton gradient across the membrane, ultimately leading to ATP synthesis. Defects in NADH dehydrogenase can result in various mitochondrial diseases and disorders.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Lactate dehydrogenases (LDH) are a group of intracellular enzymes found in nearly all human cells, particularly in the heart, liver, kidneys, muscles, and brain. They play a crucial role in energy production during anaerobic metabolism, converting pyruvate to lactate while regenerating NAD+ from NADH. LDH exists as multiple isoenzymes (LDH-1 to LDH-5) in the body, each with distinct distributions and functions.

An elevated level of LDH in the blood may indicate tissue damage or injury, as these enzymes are released into the circulation following cellular destruction. Therefore, measuring LDH levels is a common diagnostic tool to assess various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and some types of cancer. However, an isolated increase in LDH may not be specific enough for a definitive diagnosis, and additional tests are usually required for confirmation.

Mortimer SE, Xu D, McGrew D, Hamaguchi N, Lim HC, Bowne SJ, Daiger SP, Hedstrom L (December 2008). "IMP dehydrogenase type 1 ... Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K (March 1990). "Two distinct cDNAs for human IMP dehydrogenase". The ... Pimkin M, Pimkina J, Markham GD (March 2009). "A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate ... Senda M, Natsumeda Y (1994). "Tissue-differential expression of two distinct genes for human IMP dehydrogenase (E.C.1.1.1.205 ...
... also known as IMP dehydrogenase 2, is an enzyme that in humans is encoded by the IMPDH2 gene. IMP dehydrogenase 2 is the rate- ... "Entrez Gene: IMP (inosine monophosphate) dehydrogenase 2". Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K (March ... IMP dehydrogenase GRCh38: Ensembl release 89: ENSG00000178035 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... "Two distinct cDNAs for human IMP dehydrogenase". J. Biol. Chem. 265 (9): 5292-5. doi:10.1016/S0021-9258(19)34120-1. PMID ...
... also known as IMP dehydrogenase 1, is an enzyme that in humans is encoded by the IMPDH1 gene. IMP dehydrogenase 1 acts as a ... "Entrez Gene: IMP (inosine monophosphate) dehydrogenase 1". Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K (March ... 2008). "IMP dehydrogenase type 1 associates with polyribosomes translating rhodopsin mRNA". J. Biol. Chem. 283 (52): 36354-60. ... Defects in the IMPDH1 gene are a cause of retinitis pigmentosa type 10 (RP10). IMP dehydrogenase GRCh38: Ensembl release 89: ...
First, inosine monophosphate dehydrogenase (IMPDH) catalyzes the conversion of IMP to XMP; then GMP synthetase (GMPS) catalyzes ... through the IMP intermediate). Whereas the conversion of GMP to IMP involves a single enzyme, GMPR, the conversion of IMP to ... The GMPR gene encodes for the protein GMPR1 (GMP reductase enzyme) that catalyzes the reaction for converting GMP to IMP. IMP ... releasing IMP. Inosine monophosphate dehydrogenase (IMPDH) and GMPR have similar catalytic mechanisms but different structural ...
Franchetti P, Grifantini M (1999). "Nucleoside and non-nucleoside IMP dehydrogenase inhibitors as antitumor and antiviral ... inhibitors based on the compounds mycophenolic acid and tiazofurin inhibit IMP dehydrogenase at the NAD+ binding site. Because ... including glyceraldehyde 3-phosphate dehydrogenase and pyruvate dehydrogenase. In healthy mammalian tissues, estimates of the ... Lesk AM (1995). "NAD-binding domains of dehydrogenases". Curr. Opin. Struct. Biol. 5 (6): 775-83. doi:10.1016/0959-440X(95) ...
... is a drug which acts as an inhibitor of the enzyme IMP dehydrogenase. Tiazofurin and its analogues were under ...
Gilbert, Harry J. (1979). Studies on native and mutant forms of IMP dehydrogenase in Escherichia coli K12 (PhD thesis). ... a Bachelor of Science degree in 1975 followed by a PhD for research investigating mutant forms of the enzyme IMP dehydrogenase ...
IMP dehydrogenase (IMPDH) converts IMP into XMP GMP synthase converts XMP into GMP GMP reductase converts GMP back into IMP ... Different types of cancer by an increase in the activities of enzymes like IMP dehydrogenase. Modulation of purine metabolism ... So IMP, GMP and AMP are inhibitors while PRPP is an activator. Between the formation of 5'-phosphoribosyl, aminoimidazole and ... FAICAR → IMP + H2O In eukaryotes the second, third, and fifth step are catalyzed by trifunctional purine biosynthetic protein ...
IMP dehydrogenase catalyses the conversion of IMP to XMP and GMP synthetase catalyses the conversion of XMP to GMP. The operon ... IMP or inosinate). It consists of two structural genes guaB (encodes for IMP dehydrogenase or and guaA (encodes for GMP ... Mycophenolic acid, a drug which is an inhibitor of IMP dehydrogenase, is an inducer of IMD 2 gene (and hence IMD 2 probably has ... Two potential DnaA binding sites, one on the gua promoter and another 200 bp downstream of the IMP dehydrogenase initiation ...
EICAR was originally discovered as a potent inhibitor of the human enzyme IMP dehydrogenase, part of the guanylate biosynthesis ... August 2006). "Enhancement of the infectivity of SARS-CoV in BALB/c mice by IMP dehydrogenase inhibitors, including ribavirin ... Minakawa N, Matsuda A (July 1999). "Mechanism-based design of inosine 5-monophosphate dehydrogenase inhibitors: synthesis and ... A novel potent inhibitor of inosinate dehydrogenase activity and guanylate biosynthesis" (PDF). The Journal of Biological ...
2005). "Role of human nucleoside transporters in the cellular uptake of two inhibitors of IMP dehydrogenase, tiazofurin and ...
IMP. 5'-IMP is then catalyzed by Inosine-5'-monophosphate dehydrogenase (IMPDH) in guanine nucleotide biosynthesis. This is at ... This results in binding 5'-IMP is then catalyzed by Inosine-5'-monophosphate dehydrogenase (IMPDH), facilitating guanine ... IMP + NH3 Thus, the two substrates of this enzyme are 5'-AMP and H2O, whereas its two products are 5'-IMP and NH3. This enzyme ... Fotie J (2018-04-16). "Inosine 5'-Monophosphate Dehydrogenase (IMPDH) as a Potential Target for the Development of a New ...
It is formed from IMP via the action of IMP dehydrogenase, and it forms GMP via the action of GMP synthase. Also, XMP can be ...
... is the second step in the generation of GMP from IMP; the first step occurs when IMP dehydrogenase generates XMP, ... In the guanine nucleotide pathway, there are 2 enzymes involved in converting IMP to GMP, namely IMP dehydrogenase (IMPD1), ... IMP may also be generated into AMP by adenylosuccinate synthetase and then adenylosuccinate lyase. GMP synthase is also ... In the de novo synthesis of purine nucleotides, IMP is the branch point metabolite at which point the pathway diverges to the ...
IMP dehydrogenase), leading to DNA mutations. TGMP is converted by phosphorylation to thioguanosine diphosphate (TGDP) and ... accumulate intracellularly and hamper the synthesis of guanine nucleotides via the enzyme Inosine monophosphate dehydrogenase ( ...
IMP) dehydrogenase and xanthylate (XMP) aminase, converting TIMP to thioguanylic acid (TGMP). Animal tumors that are resistant ... IMP), including the conversion of IMP to xanthylic acid (XMP) and the conversion of IMP to adenylic acid (AMP) via ...
... imp dehydrogenase MeSH D08.811.682.047.497 - isocitrate dehydrogenase MeSH D08.811.682.047.500 - 3-isopropylmalate ... malate dehydrogenase MeSH D08.811.682.047.748 - malate dehydrogenase (nadp+) MeSH D08.811.682.047.892 - xanthine dehydrogenase ... acetoin dehydrogenase MeSH D08.811.682.047.070 - alcohol dehydrogenase MeSH D08.811.682.047.150 - carbohydrate dehydrogenases ... acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 - acyl-coa dehydrogenase, long-chain MeSH D08.811.682.660.150.200 - acyl- ...
... which either catalyzes the hydrolysis of IMP. or IMP and GMP Hypothetical proteins Human genes encoding proteins that contain ... The haloacid dehydrogenase superfamily (HAD superfamily) is a superfamily of enzymes that include phosphatases, phosphonatases ...
It works by blocking inosine monophosphate dehydrogenase (IMPDH), which is needed by lymphocytes to make guanosine. ... IMP). IMPDH inhibition particularly affects lymphocytes since they rely almost exclusively on de novo purine synthesis. In ... It reversibly inhibits inosine monophosphate dehydrogenase, the enzyme that controls the rate of synthesis of guanine ... Mycophenolic acid is a potent, reversible, non-competitive inhibitor of inosine-5′-monophosphate dehydrogenase (IMPDH), an ...
... monophosphate dehydrogenase Inosine pranobex Nucleobase Srinivasan S, Torres AG, Ribas de Pouplana L (April 2021). " ... Adenine is converted to adenosine or inosine monophosphate (IMP), either of which, in turn, is converted into inosine (I), ... Inosine monophosphate is oxidised by the enzyme inosine monophosphate dehydrogenase, yielding xanthosine monophosphate, a key ... anti-proliferative drug that acts as an inhibitor of inosine monophosphate dehydrogenase. It is used in the treatment of a ...
... closure of the second ring structure is carried out by IMP synthase to form IMP, where IMP fate would lead to the formation of ... Dihydroorotase and dihydroorotase dehydrogenase then converts N-Carbamoylaspartate to orotate. Orotate is covalently linked ... IMP). Essentially, IMP is converted into the purine nucleotides required for nucleic acid synthesis. The pathway begins with ...
... it can be converted back into DHT via 3α-hydroxysteroid dehydrogenase and 17β-hydroxysteroid dehydrogenase, bypassing ... They distilled over 17,000 liters (3,700 imp gal; 4,500 U.S. gal) of male urine, from which they got 50 milligrams (0.77 gr) of ... The enzyme 3α-hydroxysteroid dehydrogenase converts the reduced forms to 3α-androstanediol and 3β-androstanediol, which are ... are then converted to androsterone and etiocholanolone by 3α-hydroxysteroid dehydrogenase and 3β-hydroxysteroid dehydrogenase, ...
IMP dehydrogenase EC 1.2.1.15: malonate-semialdehyde dehydrogenase EC 1.2.1.16: succinate-semialdehyde dehydrogenase [NAD(P)+] ... EC 1.1.1.1: alcohol dehydrogenase EC 1.1.1.2: alcohol dehydrogenase (NADP+) EC 1.1.1.3: homoserine dehydrogenase EC 1.1.1.4: (R ... L-arabinitol 4-dehydrogenase EC 1.1.1.13: L-arabinitol 2-dehydrogenase EC 1.1.1.14: L-iditol 2-dehydrogenase EC 1.1.1.15: D- ... L-gulonate 3-dehydrogenase EC 1.1.1.46: L-arabinose 1-dehydrogenase EC 1.1.1.47: glucose 1-dehydrogenase [NAD(P)+)] EC 1.1.1.48 ...
IMP). Three-dimensional structures of the following integral monotopic proteins have been determined: prostaglandin H2 ... monoamine oxidases A and B fatty acid amide hydrolase mammalian cytochrome P450 oxidases corticosteroid 11-beta-dehydrogenases ...
Aspartate-semialdehyde dehydrogenase catalyzes the reduction reaction by dephosphorylation of aspartyl-β-phosphate to yield ... Further enzymatic modification of IMP produces the adenosine and guanosine bases of nucleotides. The first step in purine ... Aspartate semialdehyde dehydrogenase catalyzes the NADPH-dependent reduction of aspartyl phosphate to yield aspartate ... The other pathway for incorporating nitrogen onto the α-carbon of amino acids involves the enzyme glutamate dehydrogenase (GDH ...
In the purine nucleotide cycle, three nucleotides: AMP (adenosine monophosphate), IMP (inosine monophosphate), and S-AMP ( ... If rhabdomyolysis is suspected, serum myoglobin, creatine kinase, lactate dehydrogenase, electrolytes and renal function will ... IMP) and ammonia (NH3). Physicians may also check resting levels of creatine kinase, which are moderately increased in 90% of ... from the conversion of AMP into IMP), and uric acid (from excess AMP). Although the purine nucleotide cycle produces AMP along ...
Among these were: Peter G. Dowdeswell (born 1940) of Earls Barton, Northamptonshire, England, drank 2 litres (3.5 imp pt; 68 US ... a greater capacity for alcohol metabolization through the liver enzymes alcohol dehydrogenase and acetaldehyde dehydrogenase.[ ...
... is commonly used orally as a one-time dose of 30-150 millilitres (1.1-5.3 imp fl oz; 1.0-5.1 US fl oz) 70% solution. ... It is converted to fructose by sorbitol-6-phosphate 2-dehydrogenase. Sorbitol is an isomer of mannitol, another sugar alcohol; ...
AMP → IMP → Inosine → Hypoxanthine → Xanthine → Uric Acid Hyperuricemia experienced as gout is a common complication of solid ... and is a possible weak inhibitor of xanthine dehydrogenase. As a byproduct of its fermentation process, beer additionally ...
Production of IMP from PRPP requires glutamine, glycine, aspartate, and 6 ATP, among other things. IMP is then converted to AMP ... "Dihydropyrimidine dehydrogenase deficiency". Genetics Home Reference. Retrieved 31 October 2014. "Nucleotides: Their Synthesis ... While IMP can be directly converted to AMP, synthesis of GMP (guanosine monophosphate) requires an intermediate step, in which ... Deficiencies in enzymes involved in pyrimidine catabolism can lead to diseases such as Dihydropyrimidine dehydrogenase ...
Inhibitors of IMP dehydrogenase stimulate the phosphorylation of the anti-human immunodeficiency virus nucleosides 2,3- ... Inhibitors of IMP dehydrogenase stimulate the phosphorylation of the anti-human immunodeficiency virus nucleosides 2,3- ... Inhibitors of IMP dehydrogenase stimulate the phosphorylation of the anti-human immunodeficiency virus nucleosides 2,3- ... Inhibitors of IMP dehydrogenase stimulate the phosphorylation of the anti-human immunodeficiency virus nucleosides 2,3- ...
IMP dehydrogenase-2 drives aberrant nucleolar activity and promotes tumorigenesis in glioblastoma」の研究トピックを掘り下げます。これらがまとまってユニークな ... IMP dehydrogenase-2 drives aberrant nucleolar activity and promotes tumorigenesis in glioblastoma. Nature Cell Biology. 2019 8月 ... IMP dehydrogenase-2 drives aberrant nucleolar activity and promotes tumorigenesis in glioblastoma. In: Nature Cell Biology. ... IMP dehydrogenase-2 drives aberrant nucleolar activity and promotes tumorigenesis in
Mortimer SE, Xu D, McGrew D, Hamaguchi N, Lim HC, Bowne SJ, Daiger SP, Hedstrom L (December 2008). "IMP dehydrogenase type 1 ... Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K (March 1990). "Two distinct cDNAs for human IMP dehydrogenase". The ... Pimkin M, Pimkina J, Markham GD (March 2009). "A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate ... Senda M, Natsumeda Y (1994). "Tissue-differential expression of two distinct genes for human IMP dehydrogenase (E.C.1.1.1.205 ...
The functional basis of mycophenolic acid resistance in Candida albicans IMP dehydrogenase. / Köhler, Gerwald A.; Gong, Xin; ... The functional basis of mycophenolic acid resistance in Candida albicans IMP dehydrogenase. In: Journal of Biological Chemistry ... The functional basis of mycophenolic acid resistance in Candida albicans IMP dehydrogenase. Journal of Biological Chemistry. ... Dive into the research topics of The functional basis of mycophenolic acid resistance in Candida albicans IMP dehydrogenase. ...
IMP dehydrogenase-2 drives aberrant nucleolar activity and promotes tumorigenesis in glioblastoma. Kofuji S, Hirayama A, ...
IPR001093 IMP dehydrogenase/GMP reductase. Prediction based on longest six frame method >SGN-P246432 (350 Aa). ...
IPR001093 IMP dehydrogenase/GMP reductase. *IPR000626 Ubiquitin. Prediction based on longest six frame method >SGN-P242326 (481 ...
Inosine Monophosphate Dehydrogenase; Catalyzes The Rate-limiting Step In The De Novo Synthesis Of GTP; Member Of A Four-gene ... IMP dehydrogenase IMD4, YML056C. Inosine monophosphate dehydrogenase; catalyzes the rate-limiting step in the de novo synthesis ...
... not with inhibition of IMP dehydrogenase. Antimicrob. Agents Chemother. 2007, 51, 84-88. [Google Scholar] [CrossRef] [PubMed] ... IMP) and thereby inhibits the synthesis of IMP to xanthosine monophosphate (XMP) by IMPDH. Consequently, no guanosine ... Another indirect mode of action for RBV is the inhibition of the cellular inosine monophosphate dehydrogenase (IMPDH), which ... exerts its antiviral activity in vitro against flaviviruses and paramyxoviruses is mediated by inhibition of IMP dehydrogenase ...
... adenylosuccinate synthetase and IMP dehydrogenase[31]. According to the combined results of multiple studies, there is a well- ...
Inosine monophosphatase dehydrogenase (IMPDH) inhibitor. Cited in 1 publication. ... Senda et al (1995) Mycophenolic acid, an inhibitor of IMP dehydrogenase that is also an immunosuppressive agent, suppresses the ... Description: Inosine monophosphatase dehydrogenase (IMPDH) inhibitor Chemical Name: 6-(1,3-Dihydro-4-hydroxy-6-methoxy-7-methyl ... Potently inhibits inosine monophosphate dehydrogenase (IMPDH), thus inhibiting de novo GTP synthesis leading to decreased RNA ...
Enzyme: IMP dehydrogenase. *Second reaction step: XMP + ATP + glutamine → guanosine-5-monophosphate (GMP) + AMP + PPi + ... AMP synthesis: oxygen atom at C6 atom of IMP exchanged by an amino group (NH2 group) *First reaction step: IMP + aspartate + ... GTP is involved in the synthesis of IMP to AMP, while ATP is involved in the synthesis of IMP to GMP! ... Xanthine oxidase (xanthine dehydrogenase): catalyzes the conversion of hypoxanthine to xanthine and xanthine to uric acid ...
Pyruvate Dehydrogenase - Clear. Gall Bladder Mucocele Formation - Clear. Ophthalmologist Eye CEA tested 7wks (UNAFFECTED). ... Aust Ch Mackland Wings Ov Change (IMP South Africa). Breed :. Shetland Sheepdog. Sex :. Bitch (Female). Call Name :. Miley. ... Dam : CH LEIGH-HIS COME FLY WITH ME TO MACKLAND IMP usA). S: GOLDENHYLITEST HE X FACTOR. S: HIGHLEDGEIR ISHC REAM. ... S: Can Ch/Aust SUP CH Grandgables Home Town Hero ( IMP USA- Gen CEA Clear. S: Am Ch Tara Hill Home Base ( USA). ...
Enzymes: 1, AMP deaminase; 2, IMP dehydrogenase; 3, adenosine deaminase; 4, guanase; 5, xanthine dehydrogenase or oxidase. ... IMP dehydrogenase (2), 5′-nucleotidase (3), purine nucleoside phosphorylase (4), and xanthine dehydrogenase/oxidase (5). ... alcohol dehydrogenase and then aldehyde dehydrogenase produces NADH, which shifts the equilibrium of the lactate dehydrogenase ... The common precursor IMP inhibits the formation of PRPP itself, as do ADP and GDP (not shown). These effects adjust the flow ...
ID: GO:0004463 Type: http://bio2vec.net/ontology/gene_function Label: leukotriene-A4 hydrolase activity Synonyms: leukotriene-A4 hydrolase activity Alternative IDs: als API: GO SPARQL: GO ...
inosine-5-monophosphate dehydrogenase. F:IMP dehydrogenase activity, catalytic activity;P:GMP biosynthetic process, metabolic ... G6PD3 (GLUCOSE-6-PHOSPHATE DEHYDROGENASE 3). Encodes a plastidic glucose-6-phosphate dehydrogenase that is sensitive to ... ADH1 (ALCOHOL DEHYDROGENASE 1). Catalyzes the reduction of acetaldehyde using NADH as reductant. Requires zinc for activity. ... 6-phosphogluconate dehydrogenase family protein. F:in 6 functions;P:response to fructose stimulus, response to cadmium ion, ...
inosine monophosphate dehydrogenase 2. Synonyms. IMP dehydrogenase type II. MMRRC Submission. 041645-MU ...
... guaB encodes IMP dehydrogenase ... carbon flux into the guanosine synthesis branch at the IMP node ...
IMP dehydrogenase/GMP reductase. KOG2550. Eten_1102_orf1. F. CTP synthase (UTP-ammonia lyase). KOG2387. ...
IMP dehydrogenase / GMP reductase domain. 9.2E-07. 264. 310. PF01645. Glu_synthase. Conserved region in glutamate synthase. 2.3 ... FMN-dependent dehydrogenase. 6.5E-126. 23. 355. PF00478. IMPDH. ...
IMP dehydrogenase [1] (data from MRSA252). SACOL_RS02335. GMP synthase (glutamine-hydrolyzing) [1] (data from MRSA252). ... pyruvate dehydrogenase E1 component subunit alpha [1] (data from MRSA252). SACOL_RS06135. cell division protein FtsA [1] (data ... L-lactate dehydrogenase [1] (data from MRSA252). SACOL_RS01530. 5-nucleotidase, lipoprotein e(P4) family [1] (data from ...
IMP Dehydrogenase Medicine & Life Sciences 15% * Cell Proliferation Medicine & Life Sciences 12% ... Mechanistically, p38α signaling increases expression of inosine-5′-monophosphate dehydrogenase 2 in HSPCs, leading to altered ... Mechanistically, p38α signaling increases expression of inosine-5′-monophosphate dehydrogenase 2 in HSPCs, leading to altered ... Mechanistically, p38α signaling increases expression of inosine-5′-monophosphate dehydrogenase 2 in HSPCs, leading to altered ...
IMP dehydrogenase [1] (data from MRSA252). NWMN_RS02920. 50S ribosomal protein L10 [1] (data from MRSA252). ... L-lactate dehydrogenase [1] (data from MRSA252). NWMN_RS02105. alkyl hydroperoxide reductase subunit C [1] (data from MRSA252) ... NAD-specific glutamate dehydrogenase [1] (data from MRSA252). NWMN_RS04700. glucose-6-phosphate isomerase [1] (data from ... phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating) [1] (data from MRSA252). NWMN_RS08275. glycine--tRNA ligase ...
","inosine-5-monophosphate dehydrogenase, putative [Ensembl]. IMP dehydrogenase/GMP reductase, CBS domain [Interproscan]."," ... "iron-dependent alcohol dehydrogenase of the multifunctional alcohol dehydrogenase AdhE [Ensembl]. Aldehyde dehydrogenase family ... ","Sorbitol dehydrogenase [Ensembl]. Zinc-binding dehydrogenase, Alcohol dehydrogenase GroES-like domain [Interproscan]."," ... imp cyclohydrolase) (inosinicase) (imp synthetase) (ATIC) [Ensembl]. MGS-like domain, AICARFT/IMPCHase bienzyme [Interproscan ...
Host inosine-5- monophosphate dehydrogenase (IMPDH) involved in the synthesis of guanine nucleotides, is known to be a ... Hedstrom L. IMP Dehydrogenase: Structure, Mechanism and Inhibition. Chem Rev. 2009;109(7):2903-28. ... Inhibitory action of polyunsaturated fatty acids on IMP dehydrogenase. Biochimie. 2007;89(5):581-90. ... IMPDH controls the conversion of IMP to XMP, which is the rate-limiting step in de novo synthesis of guanine nucleotides [25]. ...
The antibiotic potential of prokaryotic IMP dehydrogenase inhibitors. abstract::Inosine 5-monophosphate dehydrogenase (IMPDH) ...
IMP dehydrogenase from Pneumocystis carinii as a potential drug target. OGara, M J; Lee, C H; Weinberg, G A; Nott, J M; ... Mycophenolic acid, a specific inhibitor of IMP dehydrogenase (IMPDH; EC 1.1.1.205), is a potent inhibitor of Pneumocystis ... Extracts of these E. coli cells contained IMPDH activity that had an apparent Km for IMP of 21.7 +/- 0.3 microM and an apparent ... IMP Desidrogenase/genética , Pneumocystis/genética , Sequência de Aminoácidos , Antifúngicos/farmacologia , Clonagem Molecular ...
Hedstrom L: IMP dehydrogenase: mechanism of action and inhibition. Curr Med Chem. 1999 Jul;6(7):545-60. Pubmed: 10390600 ... Markland W, McQuaid TJ, Jain J, Kwong AD: Broad-spectrum antiviral activity of the IMP dehydrogenase inhibitor VX-497: a ... Jayaram HN, Cooney DA, Grusch M, Krupitza G: Consequences of IMP dehydrogenase inhibition, and its relationship to cancer and ... Digits JA, Hedstrom L: Drug selectivity is determined by coupling across the NAD+ site of IMP dehydrogenase. Biochemistry. 2000 ...
  • Inosine-5′-monophosphate dehydrogenase (IMPDH) is a purine biosynthetic enzyme that catalyzes the nicotinamide adenine dinucleotide (NAD+)-dependent oxidation of inosine monophosphate (IMP) to xanthosine monophosphate (XMP), the first committed and rate-limiting step towards the de novo biosynthesis of guanine nucleotides from IMP. (wikipedia.org)
  • Most IMPDH monomers contain two domains: a catalytic (β/α)8 barrel domain with an active site located in the loops at the C-terminal end of the barrel, and a subdomain consisting of two, repeated cystathionine beta synthetase (CBS) domains that are inserted within the dehydrogenase sequence. (wikipedia.org)
  • In cell culture, C. albicans is sensitive to mycophenolic acid (MPA) and mizoribine, both natural product inhibitors of IMP dehydrogenase (IMPDH). (okstate.edu)
  • Potently inhibits inosine monophosphate dehydrogenase (IMPDH), thus inhibiting de novo GTP synthesis leading to decreased RNA and DNA synthesis. (tocris.com)
  • Host inosine-5'- monophosphate dehydrogenase (IMPDH) involved in the synthesis of guanine nucleotides, is known to be a potential target to inhibit the replication of viruses. (biomedcentral.com)
  • While in the de novo synthesis of GTP, IMPDH catalyzes the oxidation of inosine monophosphate (IMP) to xanthosine monophosphate (XMP) which is the rate-limiting step. (biomedcentral.com)
  • Mechanistically, p38α signaling increases expression of inosine-5′-monophosphate dehydrogenase 2 in HSPCs, leading to altered levels of amino acids and purine-related metabolites and changes in cell-cycle progression in vitro and in vivo. (elsevierpure.com)
  • Xanthylic acid is an important metabolic intermediate in the purine metabolism, and is a product or substrate of the enzymes inosine monophosphate dehydrogenase (EC 1.1.1.205), hypoxanthine phosphoribosyltransferase (EC 2.4.2.8), xanthine phosphoribosyltransferase (EC 2.4.2.22), 5'-ribonucleotide phosphohydrolase (EC 3.1.3.5), Ap4A hydrolase (EC 3.6.1.17), nucleoside-triphosphate diphosphatase (EC 3.6.1.19), phosphoribosylamine-glycine ligase (EC 6.3.4.1), and glutamine amidotransferase (EC 6.3.5.2). (ecmdb.ca)
  • Inhibitors of IMP dehydrogenase stimulate the phosphorylation of the anti-human immunodeficiency virus nucleosides 2',3'-dideoxyadenosine and 2',3'-dideoxyinosine. (aspetjournals.org)
  • It became apparent from early studies that 6-MP was catalyzed by hypoxanthine guanine phosphoribosyltransferase (HGPRTase) to 6-thioinosine 5'-phosphate(6-TIMP) which inhibited the enzymes, PRPP amidotransferase, IMP dehydrogenase, adenylosuccinate synthetase and adenylosuccinate lyase. (go.jp)
  • Aldehyde dehydrogenase family, Iron-containing alcohol dehydrogenase [Interproscan]. (ntu.edu.sg)
  • GTP is involved in the synthesis of IMP to AMP , while ATP is involved in the synthesis of IMP to GMP ! (amboss.com)
  • protein_coding" "AAC74323","adhE","Escherichia coli","fused acetaldehyde-CoA dehydrogenase/iron-dependent alcohol dehydrogenase/pyruvate-formate lyase deactivase [Ensembl]. (ntu.edu.sg)
  • short chain dehydrogenase [Interproscan]. (ntu.edu.sg)
  • Glyceraldehyde 3-phosphate dehydrogenase [Interproscan]. (ntu.edu.sg)
  • Here we show that IMP dehydrogenase-2 (IMPDH2), the rate-limiting enzyme for de novo guanine nucleotide biosynthesis, is overexpressed in the highly lethal brain cancer glioblastoma. (elsevierpure.com)
  • Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). (umbc.edu)
  • 13. Hyle J.W., Shaw R.J., Reines D. Functional distinctions bet ween IMP dehydrogenase genes in providing mycophenolate resistance and guanine prototrophy to yeast. (org.ua)
  • IMP binds to the active site and a conserved cysteine residue attacks the 2-position of the purine ring. (wikipedia.org)
  • Wright DG, Boosalis MS, Waraska K, Oshry LJ, Weintraub LR, Vosburgh E. Tiazofurin effects on IMP-dehydrogenase activity and expression in the leukemia cells of patients with CML blast crisis. (bu.edu)
  • There are at least two isozymes of the corticosteroid 11-beta-dehydrogenase, a microsomal enzyme complex responsible for the interconversion of cortisol and cortisone. (nih.gov)
  • These substances include two aromatic moieties: one which interacts using the hypoxanthine bottom of IMP and one which interacts with Tyr358 in the adjacent subunit (Schu S4 (this enzyme is here now denoted ought to be susceptible to Schu S4. (cancer8.info)
  • 13666 IMP dehydrogenase guaB BBZA01000001 CDS ARMA_0013 13762. (go.jp)
  • 16. Ribavirin induces widespread accumulation of IMP dehydrogenase into rods/rings structures in multiple major mouse organs. (nih.gov)
  • 2010. Mycophenolate and Ribavirin inhibit IMP dehydrogenase, hence GMP is not formed. (marquardtadvogados.com.br)
  • The conversion of PRPP to IMP can be inhibited by the drug 6-MP (6-mercaptopurine) as well as by its prodrug azathioprine.Finally, IMP can be converted to either AMP (adenosine monophosphate) or GMP (guanine monophosphate). (marquardtadvogados.com.br)
  • The type II isozyme, encoded by this gene, has only 11-beta-dehydrogenase activity. (nih.gov)
  • Single nucleotide variants of succinate dehydrogenase A gene in renal cell carcinoma. (nih.gov)
  • IMP binds to the active site and a conserved cysteine residue attacks the 2-position of the purine ring. (wikipedia.org)
  • In individual and various other eukaryotic IMPDHs, the cofactor binds in the normal extended conformation noticed for some dehydrogenases, as well as the cofactor binding site is basically contained inside the same monomer as IMP (31). (cancer8.info)
  • 2. Immune Response-Dependent Assembly of IMP Dehydrogenase Filaments. (nih.gov)
  • The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex. (yeastrc.org)
  • As the IMP and nicotinamide binding servings of the energetic site are extremely conserved, the rest from the cofactor binding site is quite 58558-08-0 IC50 different in individual and bacterial IMPDHs. (cancer8.info)
  • In prokaryotic IMPDHs, the cofactor is normally bound within an uncommon compressed conformation, as well as the adenosine subsite is situated in the monomer next to the IMP and nicotinamide binding sites (32). (cancer8.info)
  • The first-order rate constants for the reaction of the sesquiterpene lactones with IMP dehydrogenase (k1) and the second-order rate constants for the reaction of the sesquiterpene lactones with glutathione (k2) were also determined. (nih.gov)
  • Binding of the drugs by IMP dehydrogenase increased as the size of the drug increased. (nih.gov)
  • Genetic expression differences of 11 beta-hydroxysteroid dehydrogenase in the bone microvascular endothelial cells derived from different regions of the human femoral head]. (nih.gov)
  • The first step is the conversion of ribose-6-phosphate to PRPP(PRPP stands for phosphoribosyl pyrophosphate), In the next step, PRPP is converted into IMP. (marquardtadvogados.com.br)