Uridine Monophosphate
Orotate Phosphoribosyltransferase
Orotidine-5'-Phosphate Decarboxylase
Uridine Kinase
Purine-Pyrimidine Metabolism, Inborn Errors
Nucleoside-Phosphate Kinase
Uridine Phosphorylase
Uridine Triphosphate
Uridine Diphosphate Sugars
Uracil Nucleotides
Uridine Diphosphate
Cyclic AMP
Cyclic GMP
Inosine Monophosphate
Adenosine Monophosphate
Uridine Diphosphate Glucose
Cytidine
8-Bromo Cyclic Adenosine Monophosphate
Cytidine Monophosphate
Guanosine Monophosphate
Pyrimidine Nucleotides
Nucleosides
Uridine Diphosphate N-Acetylglucosamine
IMP Dehydrogenase
Thiamine Monophosphate
Uracil
Hexosephosphates
Uridine Diphosphate Galactose
Bucladesine
His ... Asp catalytic dyad of ribonuclease A: histidine pKa values in the wild-type, D121N, and D121A enzymes. (1/255)
Bovine pancreatic ribonuclease A (RNase A) has a conserved His ... Asp catalytic dyad in its active site. Structural analyses had indicated that Asp121 forms a hydrogen bond with His119, which serves as an acid during catalysis of RNA cleavage. The enzyme contains three other histidine residues including His12, which is also in the active site. Here, 1H-NMR spectra of wild-type RNase A and the D121N and D121A variants were analyzed thoroughly as a function of pH. The effect of replacing Asp121 on the microscopic pKa values of the histidine residues is modest: none change by more than 0.2 units. There is no evidence for the formation of a low-barrier hydrogen bond between His119 and either an aspartate or an asparagine residue at position 121. In the presence of the reaction product, uridine 3'-phosphate (3'-UMP), protonation of one active-site histidine residue favors protonation of the other. This finding is consistent with the phosphoryl group of 3'-UMP interacting more strongly with the two active-site histidine residues when both are protonated. Comparison of the titration curves of the unliganded enzyme with that obtained in the presence of different concentrations of 3'-UMP shows that a second molecule of 3'-UMP can bind to the enzyme. Together, the data indicate that the aspartate residue in the His ... Asp catalytic dyad of RNase A has a measurable but modest effect on the ionization of the adjacent histidine residue. (+info)Rickettsia prowazekii transports UMP and GMP, but not CMP, as building blocks for RNA synthesis. (2/255)
Rickettsia prowazekii, the etiological agent of epidemic typhus, is an obligate intracellular bacterium and is apparently unable to synthesize ribonucleotides de novo. Here, we show that as an alternative, isolated, purified R. prowazekii organisms transported exogenous uridyl- and guanylribonucleotides and incorporated these labeled precursors into their RNA in a rifampin-sensitive manner. Transport systems for nucleotides, which we have shown previously and show here are present in rickettsiae, have never been reported in free-living bacteria, and the usual nucleobase and nucleoside transport systems are absent in rickettsiae. There was a clear preference for the monophosphate form of ribonucleotides as the transported substrate. In contrast, rickettsiae did not transport cytidylribonucleotides. The source of rickettsial CTP appears to be the transport of UMP followed by its phosphorylation and the amination of intrarickettsial UTP to CTP by CTP synthetase. A complete schema of nucleotide metabolism in rickettsiae is presented that is based on a combination of biochemical, physiological, and genetic information. (+info)Hypersensitive substrate for ribonucleases. (3/255)
A substrate for a hypersensitive assay of ribonucleolytic activity was developed in a systematic manner. This substrate is based on the fluorescence quenching of fluorescein held in proximity to rhodamine by a single ribonucleotide embedded within a series of deoxynucleotides. When the substrate is cleaved, the fluorescence of fluorescein is manifested. The optimal substrate is a tetranucleotide with a 5',6-carboxyfluorescein label (6-FAM) and a 3',6-carboxy-tetramethylrhodamine (6-TAMRA) label: 6-FAM-dArUdAdA-6-TAMRA. The fluorescence of this substrate increases 180-fold upon cleavage. Bovine pancreatic ribonuclease A (RNase A) cleaves this substrate with a k (cat)/ K (m)of 3.6 x 10(7)M(-1)s(-1). Human angiogenin, which is a homolog of RNase A that promotes neovascularization, cleaves this substrate with a k (cat)/ K (m)of 3. 3 x 10(2)M(-1)s(-1). This value is >10-fold larger than that for other known substrates of angio-genin. With these attributes, 6-FAM-dArUdAdA-6-TAMRA is the most sensitive known substrate for detecting ribo-nucleolytic activity. This high sensitivity enables a simple protocol for the rapid determination of the inhibition constant ( K (i)) for competitive inhibitors such as uridine 3'-phosphate and adenosine 5'-diphos-phate. (+info)Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of rRNA. (4/255)
In budding yeast (Saccharomyces cerevisiae), the majority of box H/ACA small nucleolar RNPs (snoRNPs) have been shown to direct site-specific pseudouridylation of rRNA. Among the known protein components of H/ACA snoRNPs, the essential nucleolar protein Cbf5p is the most likely pseudouridine (Psi) synthase. Cbf5p has considerable sequence similarity to Escherichia coli TruBp, a known Psi synthase, and shares the "KP" and "XLD" conserved sequence motifs found in the catalytic domains of three distinct families of known and putative Psi synthases. To gain additional evidence on the role of Cbf5p in rRNA biosynthesis, we have used in vitro mutagenesis techniques to introduce various alanine substitutions into the putative Psi synthase domain of Cbf5p. Yeast strains expressing these mutated cbf5 genes in a cbf5Delta null background are viable at 25 degrees C but display pronounced cold- and heat-sensitive growth phenotypes. Most of the mutants contain reduced levels of Psi in rRNA at extreme temperatures. Substitution of alanine for an aspartic acid residue in the conserved XLD motif of Cbf5p (mutant cbf5D95A) abolishes in vivo pseudouridylation of rRNA. Some of the mutants are temperature sensitive both for growth and for formation of Psi in the rRNA. In most cases, the impaired growth phenotypes are not relieved by transcription of the rRNA from a polymerase II-driven promoter, indicating the absence of polymerase I-related transcriptional defects. There is little or no abnormal accumulation of pre-rRNAs in these mutants, although preferential inhibition of 18S rRNA synthesis is seen in mutant cbf5D95A, which lacks Psi in rRNA. A subset of mutations in the Psi synthase domain impairs association of the altered Cbf5p proteins with selected box H/ACA snoRNAs, suggesting that the functional catalytic domain is essential for that interaction. Our results provide additional evidence that Cbf5p is the Psi synthase component of box H/ACA snoRNPs and suggest that the pseudouridylation of rRNA, although not absolutely required for cell survival, is essential for the formation of fully functional ribosomes. (+info)Alterations in ribonuclease activities in the plasma, spleen, and thymus of tumor-bearing mice. (5/255)
Six transplantable murine tumor models were evaluated for changes in RNase activity. This study was conducted with spleen and thymus homogenates, as well as with plasma collected from tumor-bearing mice. Nuclease activity directed against the synthetic substrates, polyadenylic acid, polyuridylic acid, and polycytidylic acid, was measured and the data obtained for tumor-bearing animals were compared to their normal counterparts. Elevated activity against polyuridylic acid was observed in the plasma of all tumor-bearing mice. Although not as all inclusive, RNase levels in both the spleen and thymus were generally altered as well. The observance of unilateral changes in nuclease activity directed against the synthetic substrates demonstrated that, in most cases, two or more enzymes were being detected. The assay may have some eventual value in the monitoring of cancer (+info)Regulation of the biosynthesis of N-acetylglucosaminylpyrophosphoryldolichol, feedback and product inhibition. (6/255)
The assembly of the core oligosaccharide region of asparagine-linked glycoproteins proceeds by means of the dolichol pathway. The first step of this pathway, the reaction of dolichol phosphate with UDP-GlcNAc to form N-acetylglucosaminylpyrophosphoryldolichol (GlcNAc-P-P-dolichol), is under investigation as a possible site of metabolic regulation. This report describes feedback inhibition of this reaction by the second intermediate of the pathway, N-acetylglucosaminyl-N-acetylglucosaminylpyrophosphoryldolichol (GlcNAc-GlcNAc-P-P-dolichol), and product inhibition by GlcNAc-P-P-dolichol itself. These influences were revealed when the reactions were carried out in the presence of showdomycin, a nucleoside antibiotic, present at concentrations that block the de novo formation of GlcNAc-GlcNAc-P-P-dolichol but not that of GlcNAc-P-P-dolichol. The apparent K(i) values for GlcNAc-P-P-dolichol and GlcNAc-GlcNAc-P-P-dolichol under basal conditions were 4.4 and 2.8 microM, respectively. Inhibition was also observed under conditions where mannosyl-P-dolichol (Man-P-dol) stimulated the biosynthesis of GlcNAc-P-P-dolichol; the apparent K(i) values for GlcNAc-P-P-dolichol and GlcNAc-GlcNAc-P-P-dolichol were 2.2 and 11 microM, respectively. Kinetic analysis of the types of inhibition indicated competitive inhibition by GlcNAc-P-P-dolichol toward the substrate UDP-GlcNAc and non-competitive inhibition toward dolichol phosphate. Inhibition by GlcNAc-GlcNAc-P-P-dolichol was uncompetitive toward UDP-GlcNAc and competitive toward dolichol phosphate. A model is presented for the kinetic mechanism of the synthesis of GlcNAc-P-P-dolichol. GlcNAc-P-P-dolichol also exerts a stimulatory effect on the biosynthesis of Man-P-dol, i.e. a reciprocal relationship to that previously observed between these two intermediates of the dolichol pathway. This network of inhibitory and stimulatory influences may be aspects of metabolic control of the pathway and thus of glycoprotein biosynthesis in general. (+info)A novel principle for conferring selectivity to poly(A)-binding proteins: interdependence of two ATP synthase beta-subunit mRNA-binding proteins. (7/255)
Based on electrophoretic mobility-shift assays and UV cross-linking experiments, we present evidence in the present work for the existence of two mammalian cytosolic proteins that selectively interact with the 3'-untranslated region of the mRNA coding for the catalytic beta-subunit of mitochondrial ATP synthase (beta-mtATPase). One of the proteins, beta-mtATPase mRNA-binding protein (BARB)1, is a novel poly(A)-binding protein that specifically binds the poly(A) tail of the beta-mtATPase transcript. BARB1 achieves this mRNA selectivity through its interaction with a second protein, BARB2, that binds the beta-mtATPase mRNA through a 22-bp element with a uridylate core, located 75 bp upstream of the poly(A) tail. Conversely, in the absence of BARB1, BARB2 is still able to bind the beta-mtATPase mRNA, but does so with lower affinity. Thus the interaction between BARB1 and BARB2 and beta-mtATPase mRNA involves the formation of a complex between the two BARB proteins. We conclude that BARB1 and BARB2 selectively bind the 3'-untranslated region of beta-mtATPase mRNA in a novel and interdependent manner. The complex between these two proteins may be involved in post-transcriptional regulation of gene expression. (+info)Poliovirus RNA-dependent RNA polymerase (3D(pol)). Assembly of stable, elongation-competent complexes by using a symmetrical primer-template substrate (sym/sub). (8/255)
Detailed studies of the kinetics and mechanism of nucleotide incorporation catalyzed by the RNA-dependent RNA polymerase from poliovirus, 3D(pol), have been limited by the inability to assemble elongation complexes that permit activity to be monitored by extension of end-labeled primers. We have solved this problem by employing a short, symmetrical, heteropolymeric RNA primer-template that we refer to as "sym/sub." Formation of 3D(pol)-sym/sub complexes is slow owing to a slow rate of association (0.1 microM(-1) s(-1)) of 3D(pol) and sym/sub and a slow isomerization (0. 076 s(-1)) of the 3D(pol)-sym/sub complex that is a prerequisite for catalytic competence of this complex. Complex assembly is stoichiometric under conditions in which competing reactions, such as enzyme inactivation, are eliminated. Inactivation of 3D(pol) occurs at a maximal rate of 0.051 s(-1) at 22 degrees C in reaction buffer lacking nucleotide. At this temperature, ATP protects 3D(pol) against inactivation with a K(0.5) of 37 microM. Once formed, 3D(pol)-sym/sub elongation complexes are stable (t((1)/(2)) = 2 h at 22 degrees C) and appear to contain only a single polymerase monomer. In the presence of Mg(2+), AMP, 2'-dAMP, and 3'-dAMP are incorporated into sym/sub by 3D(pol) at rates of 72, 0.6, and 1 s(-1), respectively. After incorporation of AMP, 3D(pol)-sym/sub product complexes have a half-life of 8 h at 22 degrees C. The stability of 3D(pol)-sym/sub complexes is temperature-dependent. At 30 degrees C, there is a 2-8-fold decrease in complex stability. Complex dissociation is the rate-limiting step for primer utilization. 3D(pol) dissociates from the end of template at a rate 10-fold faster than from internal positions. The sym/sub system will facilitate mechanistic analysis of 3D(pol) and permit a direct kinetic and thermodynamic comparison of the RNA-dependent RNA polymerase to the other classes of nucleic acid polymerases. (+info)Uridine Monophosphate (UMP) is a nucleotide that is a constituent of RNA (Ribonucleic Acid). It consists of a nitrogenous base called Uridine, linked to a sugar molecule (ribose) and a phosphate group. UMP plays a crucial role in various biochemical reactions within the body, including energy transfer and cellular metabolism. It is also involved in the synthesis of other nucleotides and serves as an important precursor in the production of genetic material during cell division.
Orotate phosphoribosyltransferase (OPRT) is an enzyme that catalyzes the conversion of orotate to oximine monophosphate (OMP), which is a key step in the biosynthesis of pyrimidines, a type of nucleotide. This enzyme plays a crucial role in the metabolism of nucleic acids, which are the building blocks of DNA and RNA.
The reaction catalyzed by OPRT is as follows:
orotate + phosphoribosyl pyrophosphate (PRPP) -> oximine monophosphate (OMP) + pyrophosphate
Defects in the gene that encodes for OPRT can lead to orotic aciduria, a rare genetic disorder characterized by an accumulation of orotic acid and other pyrimidines in the urine and other body fluids. Symptoms of this condition may include developmental delay, mental retardation, seizures, and megaloblastic anemia.
Orotidine-5’-phosphate decarboxylase (ODC) is an enzyme that is involved in the synthesis of pyrimidines, which are essential nucleotides required for the production of DNA and RNA. The gene that encodes this enzyme is called UMPS.
ODC catalyzes the decarboxylation of orotidine-5’-phosphate (OMP) to form uridine monophosphate (UMP), which is a precursor to other pyrimidines such as cytidine triphosphate (CTP) and thymidine triphosphate (TTP). This reaction is the fifth step in the de novo synthesis of pyrimidines.
Defects in the ODC enzyme can lead to a rare genetic disorder called orotic aciduria, which is characterized by an accumulation of orotic acid and orotidine in the urine, as well as neurological symptoms such as developmental delay, seizures, and ataxia. Treatment for this condition typically involves supplementation with uridine and a low-protein diet to reduce the production of excess orotic acid.
Uridine kinase is an enzyme that phosphorylates the pyrimidine nucleoside uridine to produce uridine monophosphate (UMP). This reaction plays a crucial role in the salvage pathway of pyrimidine nucleotide synthesis, which recycles nucleosides generated from the degradation of RNA.
The human genome encodes two isoforms of uridine kinase, UCK1 and UCK2, which share a high degree of sequence similarity but have distinct tissue expression patterns and subcellular localization. UCK1 is primarily expressed in the liver and kidney, while UCK2 is more widely expressed in various tissues.
Uridine kinase activity has been implicated in several physiological processes, including the regulation of intracellular nucleotide pools, the biosynthesis of glycosaminoglycans and proteoglycans, and the modulation of antiviral responses. Dysregulation of uridine kinase activity has been associated with various pathological conditions, such as cancer, viral infections, and neurological disorders.
Inborn errors of purine-pyrimidine metabolism refer to genetic disorders that result in dysfunctional enzymes involved in the metabolic pathways of purines and pyrimidines. These are essential components of nucleotides, which in turn are building blocks of DNA and RNA.
Inherited as autosomal recessive or X-linked recessive traits, these disorders can lead to an accumulation of toxic metabolites, a deficiency of necessary compounds, or both. Clinical features vary widely depending on the specific enzyme defect but may include neurologic symptoms, kidney problems, gout, and/or immunodeficiency.
Examples of such disorders include Lesch-Nyhan syndrome (deficiency of hypoxanthine-guanine phosphoribosyltransferase), adenosine deaminase deficiency (leading to severe combined immunodeficiency), and orotic aciduria (due to defects in pyrimidine metabolism). Early diagnosis and management are crucial to improve outcomes.
Nucleoside-phosphate kinase (NPK) is an enzyme that plays a crucial role in the synthesis and metabolism of nucleotides, which are the building blocks of DNA and RNA. NPK catalyzes the transfer of a phosphate group from a donor molecule, typically ATP, to a nucleoside or deoxynucleoside, forming a nucleoside monophosphate (NMP) or deoxynucleoside monophosphate (dNMP).
There are several isoforms of NPK found in different cellular compartments and tissues, each with distinct substrate specificities. These enzymes play essential roles in maintaining the balance of nucleotides required for various cellular processes, including DNA replication, repair, and transcription, as well as RNA synthesis and metabolism.
Abnormalities in NPK activity or expression have been implicated in several human diseases, such as cancer, viral infections, and neurological disorders. Therefore, understanding the function and regulation of NPK is crucial for developing novel therapeutic strategies to target these conditions.
Uridine phosphorylase is an enzyme that plays a role in the metabolism of nucleosides, specifically uridine. The medical definition of 'uridine phosphorylase' is:
An enzyme (EC 2.4.2.3) involved in the reversible phosphorolysis of uridine to uracil and ribose-1-phosphate. This enzyme also catalyzes the phosphorolytic cleavage of other pyrimidine nucleosides, such as cytidine and thymidine, into their respective bases and ribose-1-phosphate. Uridine phosphorylase has a role in the salvage pathway of pyrimidine nucleotide biosynthesis and is found in various tissues, including the liver, intestines, and blood cells. Deficiency or dysfunction of uridine phosphorylase can lead to impaired nucleotide metabolism and may be associated with certain medical conditions, such as hereditary orotic aciduria.
Uridine Triphosphate (UTP) is a nucleotide that plays a crucial role in the synthesis and repair of DNA and RNA. It consists of a nitrogenous base called uracil, a pentose sugar (ribose), and three phosphate groups. UTP is one of the four triphosphates used in the biosynthesis of RNA during transcription, where it donates its uracil base to the growing RNA chain. Additionally, UTP serves as an energy source and a substrate in various biochemical reactions within the cell, including phosphorylation processes and the synthesis of glycogen and other molecules.
Uridine diphosphate sugars (UDP-sugars) are nucleotide sugars that play a crucial role in the biosynthesis of glycans, which are complex carbohydrates found on the surface of many cell types. UDP-sugars consist of a uridine diphosphate molecule linked to a sugar moiety, such as glucose, galactose, or xylose. These molecules serve as activated donor substrates for glycosyltransferases, enzymes that catalyze the transfer of sugar residues to acceptor molecules, including proteins and other carbohydrates. UDP-sugars are essential for various biological processes, such as cell recognition, signaling, and protein folding. Dysregulation of UDP-sugar metabolism has been implicated in several diseases, including cancer and congenital disorders of glycosylation.
Uracil nucleotides are chemical compounds that play a crucial role in the synthesis, repair, and replication of DNA and RNA. Specifically, uracil nucleotides refer to the group of molecules that contain the nitrogenous base uracil, which is linked to a ribose sugar through a beta-glycosidic bond. This forms the nucleoside uridine, which can then be phosphorylated to create the uracil nucleotide.
Uracil nucleotides are important in the formation of RNA, where uracil base pairs with adenine through two hydrogen bonds during transcription. However, uracil is not typically found in DNA, and its presence in DNA can indicate damage or mutation. When uracil is found in DNA, it is usually the result of a process called deamination, where the nitrogenous base cytosine is spontaneously converted to uracil. This can lead to errors during replication, as uracil will pair with adenine instead of guanine, leading to a C-to-T or G-to-A mutation.
To prevent this type of mutation, cells have enzymes called uracil DNA glycosylases that recognize and remove uracil from DNA. This initiates the base excision repair pathway, which removes the damaged nucleotide and replaces it with a correct one. Overall, uracil nucleotides are essential for proper cellular function, but their misincorporation into DNA can have serious consequences for genome stability.
Uridine diphosphate (UDP) is a nucleotide diphosphate that consists of a pyrophosphate group, a ribose sugar, and the nucleobase uracil. It plays a crucial role as a coenzyme in various biosynthetic reactions, including the synthesis of glycogen, proteoglycans, and other polysaccharides. UDP is also involved in the detoxification of bilirubin, an end product of hemoglobin breakdown, by converting it to a water-soluble form that can be excreted through the bile. Additionally, UDP serves as a precursor for the synthesis of other nucleotides and their derivatives.
Cyclic adenosine monophosphate (cAMP) is a key secondary messenger in many biological processes, including the regulation of metabolism, gene expression, and cellular excitability. It is synthesized from adenosine triphosphate (ATP) by the enzyme adenylyl cyclase and is degraded by the enzyme phosphodiesterase.
In the body, cAMP plays a crucial role in mediating the effects of hormones and neurotransmitters on target cells. For example, when a hormone binds to its receptor on the surface of a cell, it can activate a G protein, which in turn activates adenylyl cyclase to produce cAMP. The increased levels of cAMP then activate various effector proteins, such as protein kinases, which go on to regulate various cellular processes.
Overall, the regulation of cAMP levels is critical for maintaining proper cellular function and homeostasis, and abnormalities in cAMP signaling have been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.
Cyclic guanosine monophosphate (cGMP) is a important second messenger molecule that plays a crucial role in various biological processes within the human body. It is synthesized from guanosine triphosphate (GTP) by the enzyme guanylyl cyclase.
Cyclic GMP is involved in regulating diverse physiological functions, such as smooth muscle relaxation, cardiovascular function, and neurotransmission. It also plays a role in modulating immune responses and cellular growth and differentiation.
In the medical field, changes in cGMP levels or dysregulation of cGMP-dependent pathways have been implicated in various disease states, including pulmonary hypertension, heart failure, erectile dysfunction, and glaucoma. Therefore, pharmacological agents that target cGMP signaling are being developed as potential therapeutic options for these conditions.
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.
Adenosine monophosphate (AMP) is a nucleotide that is the monophosphate ester of adenosine, consisting of the nitrogenous base adenine attached to the 1' carbon atom of ribose via a β-N9-glycosidic bond, which in turn is esterified to a phosphate group. It is an important molecule in biological systems as it plays a key role in cellular energy transfer and storage, serving as a precursor to other nucleotides such as ADP and ATP. AMP is also involved in various signaling pathways and can act as a neurotransmitter in the central nervous system.
Uridine Diphosphate Glucose (UDP-glucose) is a nucleotide sugar that plays a crucial role in the synthesis and metabolism of carbohydrates in the body. It is formed from uridine triphosphate (UTP) and glucose-1-phosphate through the action of the enzyme UDP-glucose pyrophosphorylase.
UDP-glucose serves as a key intermediate in various biochemical pathways, including glycogen synthesis, where it donates glucose molecules to form glycogen, a large polymeric storage form of glucose found primarily in the liver and muscles. It is also involved in the biosynthesis of other carbohydrate-containing compounds such as proteoglycans and glycolipids.
Moreover, UDP-glucose is an essential substrate for the enzyme glucosyltransferase, which is responsible for adding glucose molecules to various acceptor molecules during the process of glycosylation. This post-translational modification is critical for the proper folding and functioning of many proteins.
Overall, UDP-glucose is a vital metabolic intermediate that plays a central role in carbohydrate metabolism and protein function.
Cytidine is a nucleoside, which consists of the sugar ribose and the nitrogenous base cytosine. It is an important component of RNA (ribonucleic acid), where it pairs with guanosine via hydrogen bonding to form a base pair. Cytidine can also be found in some DNA (deoxyribonucleic acid) sequences, particularly in viral DNA and in mitochondrial DNA.
Cytidine can be phosphorylated to form cytidine monophosphate (CMP), which is a nucleotide that plays a role in various biochemical reactions in the body. CMP can be further phosphorylated to form cytidine diphosphate (CDP) and cytidine triphosphate (CTP), which are involved in the synthesis of lipids, glycogen, and other molecules.
Cytidine is also available as a dietary supplement and has been studied for its potential benefits in treating various health conditions, such as liver disease and cancer. However, more research is needed to confirm these potential benefits and establish safe and effective dosages.
8-Bromo Cyclic Adenosine Monophosphate (8-Br-cAMP) is a synthetic, cell-permeable analog of cyclic adenosine monophosphate (cAMP). Cyclic AMP is an important second messenger in many signal transduction pathways, and 8-Br-cAMP is often used in research to mimic or study the effects of increased cAMP levels. The bromine atom at the 8-position makes 8-Br-cAMP more resistant to degradation by phosphodiesterases, allowing it to have a longer duration of action compared to cAMP. It is used in various biochemical and cellular studies as a tool compound to investigate the role of cAMP in different signaling pathways.
Cytidine monophosphate (CMP) is a nucleotide that consists of a cytosine molecule attached to a ribose sugar molecule, which in turn is linked to a phosphate group. It is one of the four basic building blocks of RNA (ribonucleic acid) along with adenosine monophosphate (AMP), guanosine monophosphate (GMP), and uridine monophosphate (UMP). CMP plays a critical role in various biochemical reactions within the body, including protein synthesis and energy metabolism.
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.
Pyrimidine nucleotides are organic compounds that play crucial roles in various biological processes, particularly in the field of genetics and molecular biology. They are the building blocks of nucleic acids, which include DNA and RNA, and are essential for the storage, transmission, and expression of genetic information within cells.
Pyrimidine is a heterocyclic aromatic organic compound similar to benzene and pyridine, containing two nitrogen atoms at positions 1 and 3 of the six-member ring. Pyrimidine nucleotides are derivatives of pyrimidine, which contain a phosphate group, a pentose sugar (ribose or deoxyribose), and one of three pyrimidine bases: cytosine (C), thymine (T), or uracil (U).
* Cytosine is present in both DNA and RNA. It pairs with guanine via hydrogen bonding during DNA replication and transcription.
* Thymine is exclusively found in DNA, where it pairs with adenine through two hydrogen bonds.
* Uracil is a pyrimidine base that replaces thymine in RNA molecules and pairs with adenine via two hydrogen bonds during RNA transcription.
Pyrimidine nucleotides, along with purine nucleotides (adenine, guanine, and their derivatives), form the fundamental units of nucleic acids, contributing to the structure, function, and regulation of genetic material in living organisms.
A nucleoside is a biochemical molecule that consists of a pentose sugar (a type of simple sugar with five carbon atoms) covalently linked to a nitrogenous base. The nitrogenous base can be one of several types, including adenine, guanine, cytosine, thymine, or uracil. Nucleosides are important components of nucleic acids, such as DNA and RNA, which are the genetic materials found in cells. They play a crucial role in various biological processes, including cell division, protein synthesis, and gene expression.
Uridine Diphosphate N-Acetylglucosamine (UDP-GlcNAc) is not a medical term per se, but rather a biochemical term. It is a form of nucleotide sugar that plays a crucial role in several biochemical processes in the human body.
To provide a more detailed definition: UDP-GlcNAc is a nucleotide sugar that serves as a donor substrate for various glycosyltransferases involved in the biosynthesis of glycoproteins, proteoglycans, and glycolipids. It is a key component in the process of N-linked and O-linked glycosylation, which are important post-translational modifications of proteins that occur within the endoplasmic reticulum and Golgi apparatus. UDP-GlcNAc also plays a role in the biosynthesis of hyaluronic acid, a major component of the extracellular matrix.
Abnormal levels or functioning of UDP-GlcNAc have been implicated in various disease states, including cancer and diabetes. However, it is not typically used as a diagnostic marker or therapeutic target in clinical medicine.
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.
Thiamine monophosphate (TMP) is a biochemical compound that is a derivative of thiamine (vitamin B1). It is a cofactor for several enzymes involved in key metabolic processes, particularly in the conversion of carbohydrates into energy. TMP plays an essential role in the metabolism of carbohydrates, amino acids, and neurotransmitters.
Thiamine monophosphate is formed when thiamine undergoes phosphorylation by the enzyme thiamine pyrophosphokinase. This reaction adds a phosphate group to the thiamine molecule, resulting in the formation of TMP. Thiamine monophosphate can then be further phosphorylated to form thiamine triphosphate (TTP) or dephosphorylated back to thiamine.
Deficiency in thiamine and its derivatives, including TMP, can lead to several medical conditions, such as beriberi, Wernicke-Korsakoff syndrome, and other neurological disorders. These conditions are often associated with impaired energy metabolism, nerve damage, and cognitive decline. Proper intake of thiamine through diet or supplementation is crucial for maintaining normal physiological functions and preventing these health issues.
Uracil is not a medical term, but it is a biological molecule. Medically or biologically, uracil can be defined as one of the four nucleobases in the nucleic acid of RNA (ribonucleic acid) that is linked to a ribose sugar by an N-glycosidic bond. It forms base pairs with adenine in double-stranded RNA and DNA. Uracil is a pyrimidine derivative, similar to thymine found in DNA, but it lacks the methyl group (-CH3) that thymine has at the 5 position of its ring.
Hexose phosphates are organic compounds that consist of a hexose sugar molecule (a monosaccharide containing six carbon atoms, such as glucose or fructose) that has been phosphorylated, meaning that a phosphate group has been added to it. This process is typically facilitated by enzymes called kinases, which transfer a phosphate group from a donor molecule (usually ATP) to the sugar molecule.
Hexose phosphates play important roles in various metabolic pathways, including glycolysis, gluconeogenesis, and the pentose phosphate pathway. For example, glucose-6-phosphate is a key intermediate in both glycolysis and gluconeogenesis, while fructose-6-phosphate and fructose-1,6-bisphosphate are important intermediates in glycolysis. The pentose phosphate pathway, which is involved in the production of NADPH and ribose-5-phosphate, begins with the conversion of glucose-6-phosphate to 6-phosphogluconolactone by the enzyme glucose-6-phosphate dehydrogenase.
Overall, hexose phosphates are important metabolic intermediates that help regulate energy production and utilization in cells.
Uridine Diphosphate Galactose (UDP-galactose) is a nucleotide sugar that plays a crucial role in the biosynthesis of glycans, proteoglycans, and glycolipids. It is formed from uridine diphosphate glucose (UDP-glucose) through the action of the enzyme UDP-glucose 4'-epimerase.
In the body, UDP-galactose serves as a galactosyl donor in various metabolic pathways, including lactose synthesis in the mammary gland and the addition of galactose residues to proteoglycans and glycoproteins in the Golgi apparatus. Defects in the metabolism of UDP-galactose have been linked to several genetic disorders, such as galactosemia, which can result in serious health complications if left untreated.
I apologize for the confusion, but "Bucladesine" is not a recognized medical term or a medication in current use in medicine. It's possible that there may be some mistake or typo in the spelling. If you have any more context about where you encountered this term, I might be able to provide a more accurate and helpful response.
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.
Uridine monophosphate - Wikipedia
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Synthase15
- The enzyme Uridine monophosphate synthase (EC 4.1.1.23, UMPS) (orotate phosphoribosyl transferase and orotidine-5'-decarboxylase) catalyses the formation of uridine monophosphate (UMP), an energy-carrying molecule in many important biosynthetic pathways. (wikipedia.org)
- In microorganisms, these two domains are separate proteins, but, in multicellular eukaryotes, the two catalytic sites are expressed on a single protein, uridine monophosphate synthase. (wikipedia.org)
- Uridine monophosphate synthase (UMPS) is a fundamental enzyme in pyrimidine synthesis. (nih.gov)
- Diagnosis of uridine monophosphate synthase deficiency is by DNA analysis and/or enzyme assay in a variety of tissues. (msdmanuals.com)
- Treatment of uridine monophosphate synthase deficiency is with oral uridine supplementation. (msdmanuals.com)
- 11. Orotic aciduria and uridine monophosphate synthase: a reappraisal. (nih.gov)
- 12. Expression of catalytic domains of human UMP synthase in uridine auxotrophic bacteria. (nih.gov)
- Ghanem ME, Nakao T, Nishibori M (2006): Deficiency of uridine monophosphate synthase (DUMPS) and X- chromosome deletion in fetal mummification in cattle. (ankara.edu.tr)
- Poli MA, Dewey R, Semorile L, Lozano ME, Albarino CG, Romanowski V, Grau O (1996): PCR screening for carriers of bovine leukocyte adhesion deficiency (BLAD) and uridine monophosphate synthase (DUMPS) in Argentine Holstein cattle. (ankara.edu.tr)
- Schoeber S, Simon D, Schwenger B (1993): Sequence of the cDNA encoding bovine uridine monophosphate synthase. (ankara.edu.tr)
- Schwenger B, Schöber S and Simon D (1993): DUMPS cattle carry a point mutation in the uridine monophosphate synthase gene. (ankara.edu.tr)
- Schwenger B, Tammen I, Aurich C (1994): Detection of the homozygous recessive genotype for deficiency of uridine monophosphate synthase by DNA typing among bovine embryos produced in vitro. (ankara.edu.tr)
- Shanks RD, Bragg DS, Robinson JL (1987): Incidence and inheritance of deficiency for uridine monophosphate synthase in Holstein bulls. (ankara.edu.tr)
- Shanks RD (1990): Reproductive consequences of deficiency of uridine monophosphate synthase in Holstein cattle. (ankara.edu.tr)
- Shanks RD, Popp RG, Mccoy GC, Nelson DR, Robinson JL (1992): Identification of the homozygous recessive genotype for the deficiency of uridine monophosphate synthase in 35-day bovine embryos. (ankara.edu.tr)
Disodium6
- Uridine Monophosphate Disodium, a prominent compound in nucleic acid metabolism, emerges as a focal point in neurological research. (bc9.org)
- Uridine Monophosphate Disodium is a nucleotide derivative crucial for RNA synthesis and the formation of cell membranes. (bc9.org)
- Researchers are actively exploring the diverse applications of Uridine Monophosphate Disodium in neuroscience. (bc9.org)
- Uridine Monophosphate Disodium, a vital player in cellular processes, holds promise in various research applications. (bc9.org)
- With potential benefits spanning cognitive function, sleep modulation, and metabolic regulation, Uridine Monophosphate Disodium presents a compelling avenue for further investigation in the realm of neuroscience. (bc9.org)
- Uridine (5′-monophosphate disodium) 50g. (bionootropics.com)
Cytidine3
- Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. (nih.gov)
- This gene encodes a uridine-cytidine kinase that catalyzes the phosphorylation of uridine and cytidine to uridine monophosphate (UMP) and cytidine monophosphate (CMP) but not the phosphorylation of deoxyribonucleosides or purine ribonucleosides. (nih.gov)
- This enzyme can also phosphorylate uridine and cytidine analogs and uses both ATP and GTP as a phosphate donor. (nih.gov)
Orotate phosphoribosyltransferase3
- Uridine monophosphate is the enzyme that catalyzes orotate phosphoribosyltransferase and orotidine-5 ′ -monophosphate decarboxylase reactions. (msdmanuals.com)
- 15. Orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase exist as multienzyme complex in human malaria parasite Plasmodium falciparum. (nih.gov)
- The last two enzymes of the pathway, orotate phosphoribosyltransferase and orotidine-5-monophosphate decarboxylase, are fused in a multi-domain enzyme and are duplicated in some P. infestans strains. (unboundmedicine.com)
Docosahexaenoic acid1
- In a study, gerbils fed a combination of uridine monophosphate, choline, and docosahexaenoic acid (DHA) were found to have significantly improved performance in running mazes over those not fed the supplements, implying an increase in cognitive function. (wikipedia.org)
Supplementation2
- Uridine supplementation in the treatment of HIV lipoatrophy: results of ACTG 5229. (bc9.org)
- There is a lot of evidence supporting the use of uridine as a nootropic, with several clinical trials showing good improvements in focus, memory and mood with daily uridine monophosphate supplementation. (gel-e.co)
Orotidine2
- Uridine monophosphate is formed from Orotidine 5'-monophosphate (orotidylic acid) in a decarboxylation reaction catalyzed by the enzyme orotidylate decarboxylase. (wikipedia.org)
- After addition of ribose-P to orotate by OPRTase to form orotidine-5'-monophosphate (OMP), OMP is decarboxylated to form uridine monophosphate by ODCase. (wikipedia.org)
Choline1
- Since Uridine Monophosphate Supplement isn't directly cholinergic, in that it doesn't directly affect acetylcholine production, it serves as a fantastic catalyst when combined with the likes of Alpha GPC choline. (mindnutrition.com)
Enzyme1
- A third enzyme then splits the CO2 off the orotic ribose P, leaving uracil ribose P, also known as uridine monophosphate, which is a complete nucleotide. (nih.gov)
Orotic acid1
- 18. Uracil metabolism--UMP synthesis from orotic acid or uridine and conversion of uracil to beta-alanine: enzymes and cDNAs. (nih.gov)
Synthesis2
Nucleoside1
- It is an ester of phosphoric acid with the nucleoside uridine. (wikipedia.org)
Protein1
- The most horrifying revelation was the sinister presence of "three bladder cancer markers - BTA serine/threonine protein, NMP uridine monophosphate and RCAS1, a receptor-binding cancer antigen. (nationalenquirer.com)
Nootropic3
- Uridine is often described as a great nootropic for helping with mood , as well as a general cognitive enhancer. (gel-e.co)
- Besides being a potent nootropic, uridine can also be a neuroprotectant. (gel-e.co)
- Often abbreviated as UMP or UDP, Uridine Monophosphate is a lesser-known nootropic that is potentially more effective than the most popular options. (smartdrugsforcollege.com)
Nucleotide1
- Uridine monophosphate (UMP), also known as 5′-uridylic acid (conjugate base uridylate), is a nucleotide that is used as a monomer in RNA. (wikipedia.org)
Deficiency1
- The aim of this study was to investigate whether the deficiency uridine monophosphate syntase (DUMPS) allele exists in Holsteins cattle breed including native cattle breeds in Turkey. (ankara.edu.tr)
Neurotransmitter2
Sodium1
- Uridine Monophosphate Sodium (UMP) is a naturally occurring component of RNA which is found in various foodstuffs. (mindnutrition.com)
Metabolism1
- Non-phosphorylated uridine is not bioavailable beyond first-pass metabolism, as it is almost entirely catabolised in the liver and gastrointestinal tract. (wikipedia.org)
Pyrimidine1
- XURIDEN is a pyrimidine analog for uridine replacement indicated in adult and pediatric patients for the treatment of hereditary orotic aciduria. (nih.gov)
Enhances1
- When taken in supplemental form, uridine enhances the growth of neural projections, known as neurites. (gel-e.co)
Liver2
Synaptic1
- The first, by Richard Wurtman and colleagues, validated that uridine increases phospholipids and synaptic proteins, which are necessary for neuron growth and function. (gel-e.co)
Nutrients1
- Life Extension supplements and vitamins can help you on the path to general health and well-being that include nutrients and compounds like uridine-5'-monophosphate for healthy brain tissue, pomegranate extract for its antioxidant properties, and coenzyme Q10 to promote the conversion of fat to energy. (pureformulas.com)
Compound2
- In brain research studies, uridine monophosphate is used as a convenient delivery compound for uridine. (wikipedia.org)
- Uridine is the active component of this compound. (wikipedia.org)
Naturally1
- Uridine Monophosphate - An Overview Uridine (Uridine Monophosphate, UMP) is a naturally occurring amino acid. (holisticnootropics.com)
Neurons1
- One study showed that uridine has positive effects on the dendric spines of neurons, which are considered memory storage neurons. (gel-e.co)
Supplements1
- For this reason, uridine supplements may be an excellent solution. (gel-e.co)
Substance1
- Uridine is an important substance found in the brain. (gel-e.co)
Brain4
- For example, your brain needs uridine-5'-monophosphate (and that certainly isn't a household name). (pureformulas.com)
- What does uridine do to the brain? (gel-e.co)
- In addition to being the primary component of RNA, Uridine Monophosphate also has potential benefits in the brain. (gel-e.co)
- Uridine-5'-monophosphate (UMP) is a phosphatide building block of RNA-DNA that is critical to optimal brain function and the health of neuronal cell membranes. (lifeextension.com)
Research2
Exists1
- It exists as uridine monophosphate and is secreted into the bloodstream where it is delivered to the various organs in the body. (gel-e.co)
Form1
- Uridine is present in many foods, mainly in the form of RNA. (wikipedia.org)
Addition1
- In addition, the second study by Sara Holiguin and colleagues revealed that uridine also stimulates the release of dopamine, a mood enhancer. (gel-e.co)
Positive effects1
- Studies suggest that Uridine Monophosphate may have positive effects on learning and memory processes. (bc9.org)
Memory1
- Ocalan B, Cakir A, Koc C, Suyen GG, Kahveci N. Uridine treatment prevents REM sleep deprivation-induced learning and memory impairment. (bc9.org)
Studies1
- Preliminary studies suggest a connection between Uridine Monophosphate and fat mass regulation. (bc9.org)
Benefits2
Found1
- From there, Kornberg and his colleagues quickly found additional enzymes that could make three other nucleotides (those of cytosine, adenine, and guanine) using uridine or PRPP as starting points. (nih.gov)
Study1
- In a study commissioned by the National Institute of Mental Health, uridine reduced the symptoms of depressive patients, improving the production of dopamine. (gel-e.co)