Dihydroorotase
Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)
Aspartate Carbamoyltransferase
Dihydroorotate Oxidase
Orotic Acid
Amidohydrolases
Pyrimidine Nucleotides
Orotate Phosphoribosyltransferase
Multienzyme Complexes
Orotidine-5'-Phosphate Decarboxylase
Carbamoyl-Phosphate Synthase (Ammonia)
Cobalt
Pyrimidines
Phosphonoacetic Acid
Mesocricetus
Carcinoma, Ehrlich Tumor
Zinc
Escherichia coli
Micronuclei formation with chromosome breaks and gene amplification caused by Vpr, an accessory gene of human immunodeficiency virus. (1/157)
Vpr, an accessory gene of human immunodeficiency virus, induces cell cycle abnormality by accumulating cells at the G2-M phase. We reported recently that Vpr caused both micronuclei formation and aneuploidy. Here, we show that Vpr also induced chromosome breaks and gene amplification. Expression of Vpr induced more than 10-fold increase of colonies resistant to N-(phosphonacetyl)-L-aspartate, an inhibitor of pyrimidine de novo synthesis. Fluorescence in situ hybridization analysis detected that 4 of 10 N-(phosphonacetyl)-L-aspartate resistant clones studied had intrachromosomal amplification of carbamyl-phosphate synthetase/aspartate transcarbamoylase/dihydroorotase gene. Another single clone had dicentrics. Data suggested that the Vpr-induced chromosome breaks leading to gene amplification, followed by bridge-breakage-fusion cycle, were one of the possible mechanisms of Vpr-induced genomic instability. (+info)Functional linkage between the glutaminase and synthetase domains of carbamoyl-phosphate synthetase. Role of serine 44 in carbamoyl-phosphate synthetase-aspartate carbamoyltransferase-dihydroorotase (cad). (2/157)
Mammalian carbamoyl-phosphate synthetase is part of carbamoyl-phosphate synthetase-aspartate carbamoyltransferase-dihydroorotase (CAD), a multifunctional protein that also catalyzes the second and third steps of pyrimidine biosynthesis. Carbamoyl phosphate synthesis requires the concerted action of the glutaminase (GLN) and carbamoyl-phosphate synthetase domains of CAD. There is a functional linkage between these domains such that glutamine hydrolysis on the GLN domain does not occur at a significant rate unless ATP and HCO(3)(-), the other substrates needed for carbamoyl phosphate synthesis, bind to the synthetase domain. The GLN domain consists of catalytic and attenuation subdomains. In the separately cloned GLN domain, the catalytic subdomain is down-regulated by interactions with the attenuation domain, a process thought to be part of the functional linkage. Replacement of Ser(44) in the GLN attenuation domain with alanine increases the k(cat)/K(m) for glutamine hydrolysis 680-fold. The formation of a functional hybrid between the mammalian Ser(44) GLN domain and the Escherichia coli carbamoyl-phosphate synthetase large subunit had little effect on glutamine hydrolysis. In contrast, ATP and HCO(3)(-) did not stimulate the glutaminase activity, indicating that the interdomain linkage had been disrupted. In accord with this interpretation, the rate of glutamine hydrolysis and carbamoyl phosphate synthesis were no longer coordinated. Approximately 3 times more glutamine was hydrolyzed by the Ser(44) --> Ala mutant than that needed for carbamoyl phosphate synthesis. Ser(44), the only attenuation subdomain residue that extends into the GLN active site, appears to be an integral component of the regulatory circuit that phases glutamine hydrolysis and carbamoyl phosphate synthesis. (+info)Substitutions in the aspartate transcarbamoylase domain of hamster CAD disrupt oligomeric structure. (3/157)
Aspartate transcarbamoylase (ATCase; EC 2.1.3.2) is one of three enzymatic domains of CAD, a protein whose native structure is usually a hexamer of identical subunits. Alanine substitutions for the ATCase residues Asp-90 and Arg-269 were generated in a bicistronic vector that encodes a 6-histidine-tagged hamster CAD. Stably transfected mammalian cells expressing high levels of CAD were easily isolated and CAD purification was simplified over previous procedures. The substitutions reduce the ATCase V(max) of the altered CADs by 11-fold and 46-fold, respectively, as well as affect the enzyme's affinity for aspartate. At 25 mM Mg(2+), these substitutions cause the oligomeric CAD to dissociate into monomers. Under the same dissociating conditions, incubating the altered CAD with the ATCase substrate carbamoyl phosphate or the bisubstrate analogue N-phosphonacetyl-L-aspartate unexpectedly leads to the reformation of hexamers. Incubation with the other ATCase substrate, aspartate, has no effect. These results demonstrate that the ATCase domain is central to hexamer formation in CAD and suggest that the ATCase reaction mechanism is ordered in the same manner as the Escherichia coli ATCase. Finally, the data indicate that the binding of carbamoyl phosphate induces conformational changes that enhance the interaction of CAD subunits. (+info)Direct examination of histone acetylation on Myc target genes using chromatin immunoprecipitation. (4/157)
Overexpression of c-Myc can lead to altered transcriptional regulation of cellular genes and to neoplastic transformation. Although DNA binding is clearly required, the mechanism by which recruitment of c-Myc to target promoters results in transcriptional activation is highly debated. Much of this controversy comes from the difficulty in clearly defining a true Myc target gene. We have previously determined that cad is a bona fide Myc target gene and thus now use the cad promoter as a model to study Myc function. Others have shown that Myc can interact indirectly with histone acetylases and have suggested that Myc mediates transcriptional activation by causing an increase in the levels of acetylated histones on target promoters. To directly test this model, we employed a chromatin immunoprecipitation assay to examine the levels of acetylated histones on the cad promoter. Although Myc was bound to the cad promoter in S phase but not in G(0) phase, we found high levels of acetylated histones on the promoter in both stages. We also examined acetylated histones on the cad promoter before and after differentiation of U937 cells. Although the levels of c-Myc bound to the cad promoter were greatly reduced after differentiation, we saw high levels of acetylated histones on the cad promoter both before and after differentiation. Finally, we found that a 30-fold change in binding of N-Myc to the telomerase promoter did not result in a concomitant change in histone acetylation. Thus, recruitment of a Myc family member to a target promoter does not necessarily influence the amount of acetylated histones at that promoter. Further investigations are in progress to define the role of Myc in transcriptional activation. (+info)Fluoroorotic acid-selected Nicotiana plumbaginifolia cell lines with a stable thymine starvation phenotype have lost the thymine-regulated transcriptional program. (5/157)
We have selected 143 independent Nicotiana plumbaginifolia cell lines that survive in the presence of 5-fluoroorotic acid. These lines show several diverse phenotypes. The majority of these cell lines showed reduced levels of UMP synthase. However, one particular phenotype, which represents 14% of the total independent lines (20 cell lines), showed an unexpected, high level of UMP synthase and was therefore analyzed in detail. The selected cell lines showed no differences with wild-type cells with respect to uptake of orotic acid, affinity of UMP synthase for its substrates, or UMP synthase gene-copy number. Alternative detoxification mechanisms were also excluded. The elevated enzyme activity was correlated with elevated UMP synthase protein levels as well as elevated UMP synthase mRNA levels. In contrast to wild-type cell lines, the fluoroorotic acid-selected cell lines did not respond to thymine or to other biochemicals that affect thymine levels. In addition, there was also a concomitant up-regulation of aspartate transcarbamoylase, however, dihydroorotase and dihydroorotate dehydrogenase are not up-regulated in these cell lines. (+info)Gene amplification in fibroblasts from ataxia telangiectasia (AT) patients and in X-ray hypersensitive AT-like Chinese hamster mutants. (6/157)
In search of functions involved in the regulation of gene amplification, and given the relevance of chromosome breakage in initiating the process, we analyzed the gene amplification ability of cells hypersensitive to inducers of DNA double-strand breaks and defective in cell cycle control: two human fibroblast strains derived from patients affected by ataxia telangiectasia (AT) and two hamster mutant cell lines belonging to complementation group XRCC8 of the rodent X-ray-sensitive mutants. These mutants are considered hamster models of AT cells. To measure gene amplification, the frequency and the rate of occurrence of N-(phosphonacetyl)-L-aspartate resistant cells were determined. In both hamster mutants, these two parameters were increased by about an order of magnitude compared with parental cells, suggesting that amplification ability was increased by the genetic defect. In primary AT fibroblasts, as in normal human fibroblasts, gene amplification was undetectable and a block in the G(1) phase of the cell cycle was induced upon PALA treatment. These results suggest that in AT fibroblasts, where only the ATM gene is mutated, ATM-independent mechanisms prevent gene amplification, while, in the immortalized hamster cell lines, which are already permissive for gene amplification, the AT-like defect increases the probability of gene amplification. (+info)Contribution of the bacterial endosymbiont to the biosynthesis of pyrimidine nucleotides in the deep-sea tube worm Riftia pachyptila. (7/157)
The deep-sea tube worm Riftia pachyptila (Vestimentifera) from hydrothermal vents lives in an intimate symbiosis with a sulfur-oxidizing bacterium. That involves specific interactions and obligatory metabolic exchanges between the two organisms. In this work, we analyzed the contribution of the two partners to the biosynthesis of pyrimidine nucleotides through both the "de novo" and "salvage" pathways. The first three enzymes of the de novo pathway, carbamyl-phosphate synthetase, aspartate transcarbamylase, and dihydroorotase, were present only in the trophosome, the symbiont-containing tissue. The study of these enzymes in terms of their catalytic and regulatory properties in both the trophosome and the isolated symbiotic bacteria provided a clear indication of the microbial origin of these enzymes. In contrast, the succeeding enzymes of this de novo pathway, dihydroorotate dehydrogenase and orotate phosphoribosyltransferase, were present in all body parts of the worm. This finding indicates that the animal is fully dependent on the symbiont for the de novo biosynthesis of pyrimidines. In addition, it suggests that the synthesis of pyrimidines in other tissues is possible from the intermediary metabolites provided by the trophosomal tissue and from nucleic acid degradation products since the enzymes of the salvage pathway appear to be present in all tissues of the worm. Analysis of these salvage pathway enzymes in the trophosome strongly suggested that these enzymes belong to the worm. In accordance with this conclusion, none of these enzyme activities was found in the isolated bacteria. The enzymes involved in the production of the precursors of carbamyl phosphate and nitrogen assimilation, glutamine synthetase and nitrate reductase, were also investigated, and it appears that these two enzymes are present in the bacteria. (+info)Increased gene amplification in immortal rodent cells deficient for the DNA-dependent protein kinase catalytic subunit. (8/157)
Gene amplification is one of the most frequent genome anomalies observed in tumor cells, whereas it has never been detected in cells of normal origin. A large body of evidence indicates that DNA double-strand breaks (DSBs) play a key role in initiating gene amplification. In mammals, DSBs are mainly repaired through the nonhomologous end-joining pathway (NHEJ) that requires a functional DNA-dependent protein kinase catalytic subunit (DNA-PKcs). In rodent cell lines, N-(phosphonacetyl)-L-aspartate (PALA) resistance is considered a measure of gene amplification because it is mainly attributable to amplification of the carbamyl-P-synthetase aspartate transcarbamylase dihydro-orotase (CAD) gene. In this paper we show that the radiosensitive hamster cell line V3, which is defective in DSB repair because of a mutation in the DNA-PKcs gene, displays also an increased frequency of gene amplification. In these cells, we found that the amplification of the CAD gene occurs with a frequency and a rate more than one order of magnitude higher than in control cell lines, although it relies on the same mechanisms. When the same analysis was performed in mouse embryo fibroblasts (MEFs) obtained from animals in which the DNA-PKcs gene was ablated by homologous recombination, a higher frequency of amplification compared with the controls was found only after cellular immortalization. In primary DNA-PKcs(-/-) MEFs, PALA treatment induced a block in the cell cycle, and no PALA-resistant clones were found. Our results indicate that the lack of DNA-PKcs increases the probability that gene amplification occurs in a genetic background already permissive, like that of immortalized cells, although it is not sufficient to make normal cells able to amplify. (+info)Dihydroorotase is an enzyme that plays a crucial role in the synthesis of pyrimidines, which are essential components of nucleic acids such as DNA and RNA. Specifically, dihydroorotase catalyzes the conversion of N-carbamoyl-L-aspartate into L-dihydroorotate and L-carbamoyl aspartate in the third step of de novo pyrimidine biosynthesis.
The reaction catalyzed by dihydroorotase is:
N-carbamoyl-L-aspartate + H2O → L-dihydroorotate + L-carbamoyl aspartate
Dihydroorotase is a member of the amidohydrolase superfamily and functions as a homodimer or homotetramer. In humans, dihydroorotase is encoded by the DHODH gene and is found in the cytoplasm of cells. Defects in this enzyme can lead to a rare genetic disorder called dihydropyrimidine dehydrogenase deficiency, which is characterized by an accumulation of pyrimidines and their precursors in the body.
Aspartate carbamoyltransferase (ACT) is a crucial enzyme in the urea cycle, which is the biochemical pathway responsible for the elimination of excess nitrogen waste from the body. This enzyme catalyzes the second step of the urea cycle, where it facilitates the transfer of a carbamoyl group from carbamoyl phosphate to aspartic acid, forming N-acetylglutamic semialdehyde and releasing phosphate in the process.
The reaction catalyzed by aspartate carbamoyltransferase is as follows:
Carbamoyl phosphate + L-aspartate → N-acetylglutamic semialdehyde + P\_i + CO\_2
This enzyme plays a critical role in maintaining nitrogen balance and preventing the accumulation of toxic levels of ammonia in the body. Deficiencies or mutations in aspartate carbamoyltransferase can lead to serious metabolic disorders, such as citrullinemia and hyperammonemia, which can have severe neurological consequences if left untreated.
Dihydroorotate oxidase is a mitochondrial enzyme that plays a crucial role in the de novo biosynthesis of pyrimidines, which are essential nucleotides required for the synthesis of DNA, RNA, and other vital molecules in the body.
The enzyme catalyzes the oxidation of dihydroorotate to orotate, using molecular oxygen as an electron acceptor. This reaction is the third step in the pyrimidine biosynthesis pathway, following the condensation of carbamoyl phosphate and aspartate to form carbamoylaspartate, and the decarboxylation of carbamoylaspartate to form dihydroorotate.
Dihydroorotate oxidase is a flavoprotein that contains a FAD cofactor, which accepts electrons from dihydroorotate and transfers them to molecular oxygen, generating hydrogen peroxide as a byproduct. The enzyme is inhibited by the drug leflunomide, which is used in the treatment of rheumatoid arthritis and other autoimmune diseases.
In humans, dihydroorotate oxidase is encoded by two genes, DHODH and SUOX, which are located on different chromosomes. Mutations in these genes can lead to deficiencies in pyrimidine biosynthesis and result in various genetic disorders, such as Miller syndrome, a rare autosomal recessive disorder characterized by craniofacial abnormalities, limb defects, and hearing loss.
Orotic acid, also known as pyrmidine carboxylic acid, is a organic compound that plays a role in the metabolic pathway for the biosynthesis of pyrimidines, which are nitrogenous bases found in nucleotides and nucleic acids such as DNA and RNA. Orotic acid is not considered to be a vitamin, but it is sometimes referred to as vitamin B13 or B15, although these designations are not widely recognized by the scientific community.
In the body, orotic acid is converted into orotidine monophosphate (OMP) by the enzyme orotate phosphoribosyltransferase. OMP is then further metabolized to form uridine monophosphate (UMP), a pyrimidine nucleotide that is an important precursor for the synthesis of RNA and other molecules.
Elevated levels of orotic acid in the urine, known as orotic aciduria, can be a sign of certain genetic disorders that affect the metabolism of pyrimidines. These conditions can lead to an accumulation of orotic acid and other pyrimidine precursors in the body, which can cause a range of symptoms including developmental delays, neurological problems, and kidney stones. Treatment for these disorders typically involves dietary restrictions and supplementation with nucleotides or nucleosides to help support normal pyrimidine metabolism.
Amidohydrolases are a class of enzymes that catalyze the hydrolysis of amides and related compounds, resulting in the formation of an acid and an alcohol. This reaction is also known as amide hydrolysis or amide bond cleavage. Amidohydrolases play important roles in various biological processes, including the metabolism of xenobiotics (foreign substances) and endogenous compounds (those naturally produced within an organism).
The term "amidohydrolase" is a broad one that encompasses several specific types of enzymes, such as proteases, esterases, lipases, and nitrilases. These enzymes have different substrate specificities and catalytic mechanisms but share the common ability to hydrolyze amide bonds.
Proteases, for example, are a major group of amidohydrolases that specifically cleave peptide bonds in proteins. They are involved in various physiological processes, such as protein degradation, digestion, and regulation of biological pathways. Esterases and lipases hydrolyze ester bonds in various substrates, including lipids and other organic compounds. Nitrilases convert nitriles into carboxylic acids and ammonia by cleaving the nitrile bond (C≡N) through hydrolysis.
Amidohydrolases are found in various organisms, from bacteria to humans, and have diverse applications in industry, agriculture, and medicine. For instance, they can be used for the production of pharmaceuticals, biofuels, detergents, and other chemicals. Additionally, inhibitors of amidohydrolases can serve as therapeutic agents for treating various diseases, such as cancer, viral infections, and neurodegenerative disorders.
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.
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.
Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.
I'm sorry for any confusion, but "Razoxane" is not a medical term that has a widely accepted or specific definition in the field of medicine. It is possible that you may be referring to "razoxane," which is a medication used in the treatment of certain types of cancer. Razoxane is an antineoplastic agent, which means it is a drug that is used to treat cancer. It works by interfering with the formation of blood vessels that supply tumors, which can help to slow or stop the growth of the tumor.
It is important to note that the use of razoxane is not widely accepted and it is not a commonly used cancer treatment. It is typically used only in certain specific circumstances and when other treatments have not been effective. As with any medication, razoxane should be used under the close supervision of a healthcare professional, and it is important to be aware of the potential risks and benefits.
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.
Cobalt is a chemical element with the symbol Co and atomic number 27. It is a hard, silver-white, lustrous, and brittle metal that is found naturally only in chemically combined form, except for small amounts found in meteorites. Cobalt is used primarily in the production of magnetic, wear-resistant, and high-strength alloys, as well as in the manufacture of batteries, magnets, and pigments.
In a medical context, cobalt is sometimes used in the form of cobalt-60, a radioactive isotope, for cancer treatment through radiation therapy. Cobalt-60 emits gamma rays that can be directed at tumors to destroy cancer cells. Additionally, small amounts of cobalt are present in some vitamin B12 supplements and fortified foods, as cobalt is an essential component of vitamin B12. However, exposure to high levels of cobalt can be harmful and may cause health effects such as allergic reactions, lung damage, heart problems, and neurological issues.
Pyrimidines are heterocyclic aromatic organic compounds similar to benzene and pyridine, containing two nitrogen atoms at positions 1 and 3 of the six-member ring. They are one of the two types of nucleobases found in nucleic acids, the other being purines. The pyrimidine bases include cytosine (C) and thymine (T) in DNA, and uracil (U) in RNA, which pair with guanine (G) and adenine (A), respectively, through hydrogen bonding to form the double helix structure of nucleic acids. Pyrimidines are also found in many other biomolecules and have various roles in cellular metabolism and genetic regulation.
Phosphonoacetic acid (PAA) is not a naturally occurring substance, but rather a synthetic compound that is used in medical and scientific research. It is a colorless, crystalline solid that is soluble in water.
In a medical context, PAA is an inhibitor of certain enzymes that are involved in the replication of viruses, including HIV. It works by binding to the active site of these enzymes and preventing them from carrying out their normal functions. As a result, PAA has been studied as a potential antiviral agent, although it is not currently used as a medication.
It's important to note that while PAA has shown promise in laboratory studies, its safety and efficacy have not been established in clinical trials, and it is not approved for use as a drug by regulatory agencies such as the U.S. Food and Drug Administration (FDA).
"Mesocricetus" is a genus of rodents, more commonly known as hamsters. It includes several species of hamsters that are native to various parts of Europe and Asia. The best-known member of this genus is the Syrian hamster, also known as the golden hamster or Mesocricetus auratus, which is a popular pet due to its small size and relatively easy care. These hamsters are burrowing animals and are typically solitary in the wild.
I'm sorry for any confusion, but "Carcinoma, Ehrlich Tumor" is not a recognized medical term or a valid medical definition. The term "Ehrlich tumor" is sometimes used to refer to a type of transplantable tumor that was first developed by the German physician Paul Ehrlich in the early 20th century for cancer research purposes. However, it's important to note that this type of tumor is not a naturally occurring cancer and is typically used only in laboratory experiments.
Carcinoma, on the other hand, is a medical term that refers to a type of cancer that starts in cells that line the inner or outer surfaces of organs. Carcinomas can develop in various parts of the body, including the lungs, breasts, colon, and skin.
If you have any specific questions about cancer or a particular medical condition, I would be happy to try to help answer them for you.
Zinc is an essential mineral that is vital for the functioning of over 300 enzymes and involved in various biological processes in the human body, including protein synthesis, DNA synthesis, immune function, wound healing, and cell division. It is a component of many proteins and participates in the maintenance of structural integrity and functionality of proteins. Zinc also plays a crucial role in maintaining the sense of taste and smell.
The recommended daily intake of zinc varies depending on age, sex, and life stage. Good dietary sources of zinc include red meat, poultry, seafood, beans, nuts, dairy products, and fortified cereals. Zinc deficiency can lead to various health problems, including impaired immune function, growth retardation, and developmental delays in children. On the other hand, excessive intake of zinc can also have adverse effects on health, such as nausea, vomiting, and impaired immune function.
'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.
Dihydroorotase
Ribonucleotide
Formylmethanofuran dehydrogenase
PyrC leader
Pyrimidine metabolism
Biosynthesis
CAD protein
Aspartate carbamoyltransferase
Nucleotide
Amorphea
RHEB
Multilocus sequence typing
List of MeSH codes (D08)
Opisthokont
List of EC numbers (EC 3)
Dihydroorotase - Wikipedia
Dihydroorotase (Acinetobacter baumannii AB307-0294) | Protein Target - PubChem
Zinc in PDB 2z28: THR109VAL Dihydroorotase From E. Coli
SCOP 1.73: Superfamily c.1.9: Metallo-dependent hydrolases
MMRRC:040182-MU
metabolic pathway pertinent to the brain - Ontology Report - Rat Genome Database
Buying Vesicare Cost Without Insurance, Purchase vesicare buy germany usa Centre for Research on the Epidemiology of Disasters...
Brian Shoichet, PhD · School of Pharmacy · UCSF
Aspartate transcarbamoylase (ATCase) and Feedback Inhibition | Molecular Biology | JoVE
WikiGenes - Carbamoyl - aminomethanone
Vol. 122 No. 2 (2022) | The Ohio Journal of Science
Nucleotide transport and metabolism
Purines and pyrimidines
Propagation of PurR regulog to Shigella flexneri 2a str. 301
SSGCID: Pathways: PWY-7211: Brugia
AT4G22930 details
Pre GI: CDS description
Regulon of PyrR in Lactobacillus acidophilus NCFM
Network Portal - Gene RSP 2316
CAD | PlatCOVID
NEDD4 and CAD Interaction - Wiki-Pi
Bioorganic Chemistry - Texas A&M University (TAMU) Scholar
txid1655611[Organism:noexp] - Protein - NCBI
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Dr Ian Ross - Institute for Molecular Bioscience - University of Queensland
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HADHB - wikidoc
Aspartate transcarbamoylase1
- This gene encodes a trifunctional protein which is associated with the enzymatic activities of the first 3 enzymes in the 6-step pathway of pyrimidine biosynthesis: carbamoylphosphate synthetase (CPS II), aspartate transcarbamoylase, and dihydroorotase. (platcovid.com)
Carbamoyl3
- Dihydroorotase (EC 3.5.2.3, carbamoylaspartic dehydrase, dihydroorotate hydrolase) is an enzyme which converts carbamoyl aspartic acid into 4,5-dihydroorotic acid in the biosynthesis of pyrimidines. (wikipedia.org)
- ATCase is part of the CAD multi-enzyme complex, part of the pyrimidine biosynthesis pathway, along with carbamoyl phosphate synthetase II and dihydroorotase. (jove.com)
- Then, the ring closes through intramolecular condensation , converting carbamoyl phosphate into dihydroorotate by the enzyme dihydroorotase . (biologyonline.com)
Zinc2
- Dihydroorotase is a zinc metalloenzyme. (wikipedia.org)
- The binding sites of Zinc atom in the THR109VAL Dihydroorotase From E. Coli (pdb code 2z28 ). (atomistry.com)
Aspartate4
- Dihydroorotase (EC 3.5.2.3 ) (DHOase) catalyzes the third step in the de novo biosynthesis of pyrimidine, the conversion of ureidosuccinic acid (N-carbamoyl-L-aspartate) into dihydroorotate. (expasy.org)
- Organization of the yeast URA2 gene: identification of a defective dihydroorotase-like domain in the multifunctional carbamoylphosphate synthetase-aspartate transcarbamylase complex. (expasy.org)
- Our efforts have allowed us to characterize the structures of the dihydroorotase and aspartate transcarbamoylase domains of CAD, to define their catalytic and regulatory mechanisms, and to understand how these domains nucleate the organization of CAD into a very large hexameric particle. (csic.es)
- This gene encodes a trifunctional protein which is associated with the enzymatic activities of the first 3 enzymes in the 6-step pathway of pyrimidine biosynthesis: carbamoylphosphate synthetase (CPS II), aspartate transcarbamoylase, and dihydroorotase. (nih.gov)
Dihydroorotate2
- Dihydroorotase (EC 3.5.2.3, carbamoylaspartic dehydrase, dihydroorotate hydrolase) is an enzyme which converts carbamoyl aspartic acid into 4,5-dihydroorotic acid in the biosynthesis of pyrimidines. (wikipedia.org)
- Orotate inhibition of dihydroorotase and dihydroorotate dehydrogenase. (nih.gov)
Binds1
- Dihydroorotase binds a zinc ion which is required for its catalytic activity [ 1 ]. (expasy.org)
Protein3
- Dihydroorotase expressed by the pyrC plasmid in E. coli constituted 6.3% of the soluble protein in frozen cell paste. (nih.gov)
- Two splice variants of the third gene (dihydroorotase) were identified, one of them encoding a premature stop codon generating a non-functional truncated protein. (unboundmedicine.com)
- Dihydroorotase was chosen for further analysis and docked with natural product libraries (Ayurvedic and Streptomycin compounds), while the control was orotic acid or vitamin B13 (which is a natural binder of this protein). (bvsalud.org)
Gene2
- We conclude that the entire pyrC gene is present on the hybrid plasmid and that the dihydroorotase produced from this plasmid is identical to the wild type. (nih.gov)
- Structure of the Saccharomyces cerevisiae URA4 gene encoding dihydroorotase. (expasy.org)
PyrC1
- Pure dihydroorotase derived from this frozen cell paste was compared with pure enzyme derived from an E. coli strain lacking the pyrC plasmid: tryptic peptide maps from the two dihydroorotase preparations, produced using reverse-phase high performance liquid chromatography, were indistinguishable. (nih.gov)
Current1
- The current study proposed dihydroorotase as a significant drug target in S. flexneri and 4-tritriacontanone & patupilone compounds as potent drugs against shigellosis. (bvsalud.org)