Cytidine Deaminase
RNA Editing
Adenosine Deaminase
Cytosine Deaminase
Nucleotides
Aminohydrolases
Molecular Sequence Data
vif Gene Products, Human Immunodeficiency Virus
Inosine
Amino Acid Sequence
Base Sequence
Gene Products, vif
Polymorphism, Single Nucleotide
Adenine Nucleotides
Cytidine
Mutation
Guanine Nucleotides
RNA, Double-Stranded
Cloning, Molecular
L-Serine Dehydratase
Purine Nucleotides
Nucleic Acid Conformation
Sequence Homology, Amino Acid
Sequence Alignment
Escherichia coli
RNA, Messenger
Adenosine
HIV-1
Substrate Specificity
DNA
Binding Sites
Alu Elements
Models, Molecular
RNA
Regulation of AMP deaminase from chicken erythrocytes. A kinetic study of the allosteric interactions. (1/137)
The allosteric properties of AMP deaminase [EC 3.5.4.6] from chicken erythrocytes have been qualitatively and quantitatively accounted for by the concerted transition theory of Monod et al., on the assumption that this enzyme has different numbers of binding sites for each ligand. Theoretical curves yield a satisfactory fit for all experimental saturation functions with respect to activation by alkali metals and inhibition by Pi, assuming that the numbers of binding sites for AMP, alkali metals, and Pi are 4, 2, and 4, respectively. The enzyme was inhibited by concentrations of ATP and GTP below 0.1 and 0.25 mM, respectively, whereas activation of the enzyme was observed at ATP and GTP concentrations above 0.4 and 1.5 mM, respectively. These unusual kinetics with respect to ATP and GTP could be also accounted for by assuming 2 inhibitory and 4 activating sites for each ligand. (+info)Regulation of chicken erythrocyte AMP deaminase by phytic acid. (2/137)
AMP deaminase [EC 3.5.6.4] purified from chicken erythrocytes was inhibited by phytic acid (inositol hexaphosphate), which is the principal organic phosphate in chicken red cells. Kinetic analysis has indicated that this inhibition is of an allosteric type. The estimated Ki value was within the normal range of phytic acid concentration, suggesting that this compound acts as a physiological effector. Divalent cations such as Ca2+ and Mg2+ were shown to affect AMP deaminase by potentiating inhibition by lower concentrations of phytic acid, and by relieving the inhibition at higher concentrations of phytic acid. These results suggests that Ca2+ and Mg2+ can modify the inhibition of AMP deaminase by phytic acid in chicken red cells. (+info)ATIC-ALK: A novel variant ALK gene fusion in anaplastic large cell lymphoma resulting from the recurrent cryptic chromosomal inversion, inv(2)(p23q35). (3/137)
The subset of CD30-positive anaplastic large cell lymphomas (ALCL) with the NPM-ALK gene fusion arising from the t(2;5)(p23;q35) forms a distinct clinical and prognostic entity. Recently, various cytogenetic, molecular, and protein studies have provided evidence for the existence of several types of variant ALK fusions in up to 20% of ALK+ ALCL, of which only one, a TPM3-ALK fusion resulting from a t(1;2)(q25;p23), has so far been cloned. A cryptic inv(2)(p23q35) has been described as another recurrent cytogenetic alteration involving ALK and an unidentified fusion partner in some ALCL. In a screen for variant ALK gene fusions, we identified two ALCL that were negative for NPM-ALK by reverse transcriptase-polymerase chain reaction, but were positive for cytoplasmic ALK with both polyclonal and monoclonal antibodies to the ALK tyrosine kinase domain, consistent with ALK deregulation by an alteration other than the t(2;5) Case 1 was a T-lineage nodal and cutaneous ALCL in a 52-year-old woman, and Case 2 was a T-lineage nodal ALCL in a 12-year-old girl. FISH analysis confirmed ALK rearrangement in both cases. An inverse polymerase chain reaction approach was then used to identify the ALK translocation partner in Case 1. We found an in-frame fusion of ALK to ATIC, a gene previously mapped to 2q34-q35. We then confirmed by DNA polymerase chain reaction the localization of ATIC to yeast artificial chromosome (YAC) 914E7 previously reported to span the 2q35 break in the inv(2)(p23q35). FISH analysis in Case 1 confirmed rearrangement of YAC 914E7 and fusion to ALK. The ATIC-ALK fusion was confirmed in Case 1 and also identified in Case 2 by conventional reverse transcriptase-polymerase chain reaction using ATIC forward and ALK reverse primers. ATIC encodes an enzyme involved in purine biosynthesis which, like other fusion partners of ALK, is constitutively expressed and appears to contain a dimerization domain. ATIC-ALK fusion resulting from the inv(2)(p23q35) thus provides a third mechanism of ALK activation in ALK+ ALCL. (+info)A new variant anaplastic lymphoma kinase (ALK)-fusion protein (ATIC-ALK) in a case of ALK-positive anaplastic large cell lymphoma. (4/137)
Anaplastic lymphoma kinase (ALK)-positive lymphomas ("ALKomas") constitute a distinct molecular and clinicopathological entity within the heterogeneous group of CD30-positive large cell lymphomas. In 80-85% of cases tumor cells express a Mr 80,000 hybrid protein comprising the nucleolar phosphoprotein nucleophosmin (NPM) and the ALK. We report here the cloning and expression of a novel ALK-fusion protein from an ALK-positive lymphoma. This case was selected for molecular investigation because of (a) the absence of NPM-ALK transcripts; (b) the atypical staining patterns for ALK (cytoplasm-restricted) and for NPM (nucleus-restricted); and (c) the presence of a Mr 96,000 ALK-protein differing in size from NPM-ALK. Nucleotide sequence analysis of ALK transcripts isolated by 5'-rapid amplification of cDNA ends revealed a chimeric mRNA corresponding to an ATIC-ALK in-frame fusion. ATIC is a bifunctional enzyme (5-aminoimidazole-4-carboxamide ribonucleotide transformylase and IMP cyclohydrolase enzymatic activities) that catalyzes the penultimate and final enzymatic activities of the purine nucleotide synthesis pathway. Expression of full-length ATIC-ALK cDNA in mouse fibroblasts revealed that the fusion protein (a) possesses constitutive tyrosine kinase activity; (b) forms stable complexes with the signaling proteins Grb2 and Shc; (c) induces tyrosine-phosphorylation of Shc; and (d) provokes oncogenic transformation. These findings point to fusion with ATIC as an alternative mechanism of ALK activation. (+info)Inv(2)(p23q35) in anaplastic large-cell lymphoma induces constitutive anaplastic lymphoma kinase (ALK) tyrosine kinase activation by fusion to ATIC, an enzyme involved in purine nucleotide biosynthesis. (5/137)
The non-Hodgkin lymphoma (NHL) subtype anaplastic large-cell lymphoma (ALCL) is frequently associated with a t(2;5)(p23;q35) that results in the fusion of the ubiquitously expressed nucleophosmin (NPM) gene at 5q35 to the anaplastic lymphoma kinase (ALK) gene at 2p23, which is not normally expressed in hematopoietic tissues. Approximately 20% of ALCLs that express ALK do not contain the t(2;5), suggesting that other genetic abnormalities can result in aberrant ALK expression. Here we report the molecular characterization of an alternative genetic means of ALK activation, the inv(2)(p23q35). This recurrent abnormality produces a fusion of the amino-terminus of 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC), a bifunctional homodimeric enzyme that catalyzes the penultimate and final steps of de novo purine nucleotide biosynthesis, with the intracellular portion of the ALK receptor tyrosine kinase. RT-PCR analysis of 5 ALCL tumors that contained the inv(2) revealed identical ATIC-ALK fusion cDNA junctions in all of the cases. Transient expression studies show that the ATIC-ALK fusion transcript directs the synthesis of an approximately 87-kd chimeric protein that is localized to the cytoplasm, in contrast to NPM-ALK, which typically exhibits a cytoplasmic and nuclear subcellular distribution. ATIC-ALK was constitutively tyrosine phosphorylated and could convert the IL-3-dependent murine hematopoietic cell line BaF3 to cytokine-independent growth. Our studies demonstrate an alternative mechanism for ALK involvement in the genesis of NHL and suggest that ATIC-ALK activation results from ATIC-mediated homodimerization. In addition, expected decreases in ATIC enzymatic function in ATIC-ALK-containing lymphomas may render these tumors more sensitive to antifolate drugs such as methotrexate. (Blood. 2000;95:2144-2149) (+info)Binding of PurH to a muscle-specific splicing enhancer functionally correlates with exon inclusion in vivo. (6/137)
Regulated alternative splicing of avian cardiac troponin T (cTNT) pre-mRNA requires multiple intronic elements called muscle-specific splicing enhancers (MSEs) that flank the alternative exon 5 and promote muscle-specific exon inclusion. To understand the function of the MSEs in muscle-specific splicing, we sought to identify trans-acting factors that bind to these elements. MSE3, which is located 66-81 nucleotides downstream of exon 5, assembles a complex that is both sequence- and muscle-specific. Purification and characterization of the MSE3 complex identified one component as 5-aminoimidazole-4-carboxamide ribonucleotideformyltransferase/IMP cyclohydrolase (PurH), an enzyme involved in de novo purine synthesis. Recombinant human PurH protein directly binds MSE3 RNA and PurH is the primary determinant of sequence-specific binding in the native complex. Furthermore, we show a direct correlation between the in vitro binding affinity of both the MSE3 complex and recombinant PurH with functional activation of exon inclusion in vivo. Together, these results strongly suggest that PurH performs a second function as a component of a complex that regulates MSE3-dependent exon inclusion. (+info)Characterization of two 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase isozymes from Saccharomyces cerevisiae. (7/137)
The Saccharomyces cerevisiae ADE16 and ADE17 genes encode 5-aminoimidazole-4-carboxamide ribonucleotide transformylase isozymes that catalyze the penultimate step of the de novo purine biosynthesis pathway. Disruption of these two chromosomal genes results in adenine auxotrophy, whereas expression of either gene alone is sufficient to support growth without adenine. In this work, we show that an ade16 ade17 double disruption also leads to histidine auxotrophy, similar to the adenine/histidine auxotrophy of ade3 mutant yeast strains. We also report the purification and characterization of the ADE16 and ADE17 gene products (Ade16p and Ade17p). Like their counterparts in other organisms, the yeast isozymes are bifunctional, containing both 5-aminoimidazole-4-carboxamide ribonucleotide transformylase and inosine monophosphate cyclohydrolase activities, and exist as homodimers based on cross-linking studies. Both isozymes are localized to the cytosol, as shown by subcellular fractionation experiments and immunofluorescent staining. Epitope-tagged constructs were used to study expression of the two isozymes. The expression of Ade17p is repressed by the addition of adenine to the media, whereas Ade16p expression is not affected by adenine. Ade16p was observed to be more abundant in cells grown on nonfermentable carbon sources than in glucose-grown cells, suggesting a role for this isozyme in respiration or sporulation. (+info)Human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase. A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity. (8/137)
The bifunctional enzyme aminoimidazole carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase (ATIC) is responsible for catalysis of the last two steps in the de novo purine pathway. Gel filtration studies performed on human enzyme suggested that this enzyme is monomeric in solution. However, cross-linking studies performed on both yeast and avian ATIC indicated that this enzyme might be dimeric. To determine the oligomeric state of this protein in solution, we carried out sedimentation equilibrium analysis of ATIC over a broad concentration range. We find that ATIC participates in a monomer/dimer equilibrium with a dissociation constant of 240 +/- 50 nM at 4 degrees C. To determine whether the presence of substrates affects the monomer/dimer equilibrium, further ultracentrifugation studies were performed. These showed that the equilibrium is only significantly shifted in the presence of both AICAR and a folate analog, resulting in a 10-fold reduction in the dissociation constant. The enzyme concentration dependence on each of the catalytic activities was studied in steady state kinetic experiments. These indicated that the transformylase activity requires dimerization whereas the cyclohydrolase activity only slightly prefers the dimeric form over the monomeric form. (+info)Nucleotide deaminases are a group of enzymes that catalyze the removal of an amino group (-NH2) from nucleotides, which are the building blocks of DNA and RNA. Specifically, these enzymes convert cytidine or adenosine to uridine or inosine, respectively, by removing an amino group from the corresponding nitrogenous base (cytosine or adenine).
There are several types of nucleotide deaminases that differ in their substrate specificity and cellular localization. For example, some enzymes deaminate DNA or RNA directly, while others act on free nucleotides or nucleosides. Nucleotide deaminases play important roles in various biological processes, including the regulation of gene expression, immune response, and DNA repair.
Abnormal activity or mutations in nucleotide deaminases have been associated with several human diseases, such as cancer, autoimmune disorders, and viral infections. Therefore, understanding the function and regulation of these enzymes is crucial for developing new therapeutic strategies to treat these conditions.
Nucleoside deaminases are a group of enzymes that catalyze the removal of an amino group (-NH2) from nucleosides, converting them to nucleosides with a modified base. This modification process is called deamination. Specifically, these enzymes convert cytidine and adenosine to uridine and inosine, respectively. Nucleoside deaminases play crucial roles in various biological processes, including the regulation of gene expression, immune response, and nucleic acid metabolism. Some nucleoside deaminases are also involved in the development of certain diseases and are considered as targets for drug design and discovery.
Cytidine deaminase is an enzyme that catalyzes the removal of an amino group from cytidine, converting it to uridine. This reaction is part of the process of RNA degradation and also plays a role in the immune response to viral infections.
Cytidine deaminase can be found in various organisms, including bacteria, humans, and other mammals. In humans, cytidine deaminase is encoded by the APOBEC3 gene family, which consists of several different enzymes that have distinct functions and expression patterns. Some members of this gene family are involved in the restriction of retroviruses, such as HIV-1, while others play a role in the regulation of endogenous retroelements and the modification of cellular RNA.
Mutations in cytidine deaminase genes have been associated with various diseases, including cancer and autoimmune disorders. For example, mutations in the APOBEC3B gene have been linked to an increased risk of breast cancer, while mutations in other members of the APOBEC3 family have been implicated in the development of lymphoma and other malignancies. Additionally, aberrant expression of cytidine deaminase enzymes has been observed in some autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus, suggesting a potential role for these enzymes in the pathogenesis of these conditions.
RNA editing is a process that alters the sequence of a transcribed RNA molecule after it has been synthesized from DNA, but before it is translated into protein. This can result in changes to the amino acid sequence of the resulting protein or to the regulation of gene expression. The most common type of RNA editing in mammals is the hydrolytic deamination of adenosine (A) to inosine (I), catalyzed by a family of enzymes called adenosine deaminases acting on RNA (ADARs). Inosine is recognized as guanosine (G) by the translation machinery, leading to A-to-G changes in the RNA sequence. Other types of RNA editing include cytidine (C) to uridine (U) deamination and insertion/deletion of nucleotides. RNA editing is a crucial mechanism for generating diversity in gene expression and has been implicated in various biological processes, including development, differentiation, and disease.
Adenosine Deaminase (ADA) is an enzyme that plays a crucial role in the immune system by helping to regulate the levels of certain chemicals called purines within cells. Specifically, ADA helps to break down adenosine, a type of purine, into another compound called inosine. This enzyme is found in all tissues of the body, but it is especially active in the immune system's white blood cells, where it helps to support their growth, development, and function.
ADA deficiency is a rare genetic disorder that can lead to severe combined immunodeficiency (SCID), a condition in which babies are born with little or no functional immune system. This makes them extremely vulnerable to infections, which can be life-threatening. ADA deficiency can be treated with enzyme replacement therapy, bone marrow transplantation, or gene therapy.
Cytosine deaminase is an enzyme that catalyzes the hydrolytic deamination of cytosine residues in DNA or deoxycytidine residues in RNA, converting them to uracil or uridine, respectively. This enzyme plays a role in the regulation of gene expression and is also involved in the defense against viral infections in some organisms. In humans, cytosine deamination in DNA can lead to mutations and has been implicated in the development of certain diseases, including cancer.
Nucleotides are the basic structural units of nucleic acids, such as DNA and RNA. They consist of a nitrogenous base (adenine, guanine, cytosine, thymine or uracil), a pentose sugar (ribose in RNA and deoxyribose in DNA) and one to three phosphate groups. Nucleotides are linked together by phosphodiester bonds between the sugar of one nucleotide and the phosphate group of another, forming long chains known as polynucleotides. The sequence of these nucleotides determines the genetic information carried in DNA and RNA, which is essential for the functioning, reproduction and survival of all living organisms.
Deamination is a biochemical process that refers to the removal of an amino group (-NH2) from a molecule, especially from an amino acid. This process typically results in the formation of a new functional group and the release of ammonia (NH3). Deamination plays a crucial role in the metabolism of amino acids, as it helps to convert them into forms that can be excreted or used for energy production. In some cases, deamination can also lead to the formation of toxic byproducts, which must be efficiently eliminated from the body to prevent harm.
Aminohydrolases are a class of enzymes that catalyze the hydrolysis of amide bonds and the breakdown of urea, converting it into ammonia and carbon dioxide. They are also known as amidases or urease. These enzymes play an essential role in various biological processes, including nitrogen metabolism and the detoxification of xenobiotics.
Aminohydrolases can be further classified into several subclasses based on their specificity for different types of amide bonds. For example, peptidases are a type of aminohydrolase that specifically hydrolyze peptide bonds in proteins and peptides. Other examples include ureases, which hydrolyze urea, and acylamidases, which hydrolyze acylamides.
Aminohydrolases are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They have important applications in biotechnology and medicine, such as in the production of pharmaceuticals, the treatment of wastewater, and the diagnosis of genetic disorders.
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.
The "vif" gene in the Human Immunodeficiency Virus (HIV) encodes for the Vif (Viral Infectivity Factor) protein. This protein is essential for the virus to infect and replicate within certain types of immune cells, particularly the CD4+ T-cells and cells of the macrophage lineage.
The Vif protein plays a crucial role in counteracting the host's antiviral defense mechanisms. Specifically, it targets and degrades a cellular protein called APOBEC3G (Apolipoprotein B mRNA Editing Enzyme Catalytic Polypeptide-like 3G), which would otherwise be incorporated into viral particles during the budding process. APOBEC3G has the ability to mutate the HIV genome, leading to the production of nonfunctional viral particles. By degrading APOBEC3G, Vif ensures the production of functional progeny virions and allows for efficient infection of new cells.
In summary, the Vif protein, encoded by the vif gene in HIV, is a critical factor that enables the virus to evade host immune defenses and maintain its replicative potential within susceptible cells.
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.
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.
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.
Vif ( Viral Infectivity Factor) is a gene product of certain retroviruses, including HIV-1 and HIV-2. It is an accessory protein that plays a crucial role in the viral replication cycle by counteracting the host cell's antiviral defense mechanisms.
The primary function of Vif is to neutralize the host restriction factor APOBEC3G (Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G), which would otherwise be incorporated into viral particles during budding and deaminate cytidine residues in the single-stranded DNA during reverse transcription. This results in hypermutation of the viral genome, leading to the production of nonfunctional viral proteins and ultimately inhibiting viral replication.
Vif binds to APOBEC3G and targets it for ubiquitination and subsequent degradation by the proteasome, thereby preventing its incorporation into virions and allowing efficient viral replication. Vif also interacts with other host factors involved in the ubiquitination pathway, such as CUL5 (Cullin 5) and ELOBC3 (Elongin B3), to form an E3 ubiquitin ligase complex that mediates APOBEC3G degradation.
In summary, Vif is a gene product of certain retroviruses that counteracts the host's antiviral defense mechanisms by neutralizing the restriction factor APOBEC3G and allowing efficient viral replication.
Single Nucleotide Polymorphism (SNP) is a type of genetic variation that occurs when a single nucleotide (A, T, C, or G) in the DNA sequence is altered. This alteration must occur in at least 1% of the population to be considered a SNP. These variations can help explain why some people are more susceptible to certain diseases than others and can also influence how an individual responds to certain medications. SNPs can serve as biological markers, helping scientists locate genes that are associated with disease. They can also provide information about an individual's ancestry and ethnic background.
Guanine Deaminase is an enzyme that catalyzes the chemical reaction in which guanine, one of the four nucleotides that make up DNA and RNA, is deaminated to form xanthine. This reaction is part of the purine catabolism pathway, which is the breakdown of purines to produce energy and eliminate nitrogenous waste. The gene that encodes this enzyme in humans is located on chromosome 2 and is called GDA. Deficiency in guanine deaminase has been associated with Lesch-Nyhan syndrome, a rare genetic disorder characterized by mental retardation, self-mutilation, spasticity, and uric acid overproduction.
Adenine nucleotides are molecules that consist of a nitrogenous base called adenine, which is linked to a sugar molecule (ribose in the case of adenosine monophosphate or AMP, and deoxyribose in the case of adenosine diphosphate or ADP and adenosine triphosphate or ATP) and one, two, or three phosphate groups. These molecules play a crucial role in energy transfer and metabolism within cells.
AMP contains one phosphate group, while ADP contains two phosphate groups, and ATP contains three phosphate groups. When a phosphate group is removed from ATP, energy is released, which can be used to power various cellular processes such as muscle contraction, nerve impulse transmission, and protein synthesis. The reverse reaction, in which a phosphate group is added back to ADP or AMP to form ATP, requires energy input and often involves the breakdown of nutrients such as glucose or fatty acids.
In addition to their role in energy metabolism, adenine nucleotides also serve as precursors for other important molecules, including DNA and RNA, coenzymes, and signaling molecules.
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.
Adenosine deaminase inhibitors are a class of medications that work by blocking the action of the enzyme adenosine deaminase. This enzyme is responsible for breaking down adenosine, a chemical in the body that helps regulate the immune system and is involved in the inflammatory response.
By inhibiting the activity of adenosine deaminase, these medications can increase the levels of adenosine in the body. This can be useful in certain medical conditions where reducing inflammation is important. For example, adenosine deaminase inhibitors are sometimes used to treat rheumatoid arthritis, a chronic autoimmune disease characterized by inflammation and damage to the joints.
One common adenosine deaminase inhibitor is called deoxycoformycin (also known as pentostatin). This medication is typically given intravenously and is used to treat hairy cell leukemia, a rare type of cancer that affects white blood cells.
It's important to note that adenosine deaminase inhibitors can have serious side effects, including suppression of the immune system, which can make people more susceptible to infections. They should only be used under the close supervision of a healthcare provider.
A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.
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.
I'm happy to help! However, it seems there might be a slight misunderstanding in your question. RNA, or ribonucleic acid, is typically single-stranded. Unlike DNA, which is double-stranded and forms a double helix, RNA usually exists as a single strand of nucleotides.
There are exceptions to this rule, such as certain types of RNA molecules that can form double-stranded structures in specific contexts. For example:
1. Double-Stranded RNA (dsRNA) viruses: These viruses have genomes made entirely of RNA, which is double-stranded throughout or partially double-stranded. The dsRNA viruses include important pathogens such as rotaviruses and reoviruses.
2. Hairpin loops in RNA structures: Some single-stranded RNA molecules can fold back on themselves to form short double-stranded regions, called hairpin loops, within their overall structure. These are often found in ribosomal RNA (rRNA), transfer RNA (tRNA), and messenger RNA (mRNA) molecules.
So, while 'double-stranded RNA' is not a standard medical definition for RNA itself, there are specific instances where RNA can form double-stranded structures as described above.
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.
L-serine dehydratase is an enzyme that plays a role in the metabolism of certain amino acids. Specifically, it catalyzes the conversion of L-serine to pyruvate and ammonia. This reaction is part of the pathway that breaks down L-serine to produce energy and intermediates for other biochemical processes in the body.
The systematic name for this enzyme is L-serine deaminase (pyruvate-forming). It is classified as a member of the lyase family of enzymes, which are characterized by their ability to catalyze the breaking of various chemical bonds using a cofactor to provide the energy needed for the reaction. In the case of L-serine dehydratase, the cofactor is a derivative of vitamin B6 called pyridoxal 5'-phosphate (PLP).
Deficiencies or mutations in the gene that encodes L-serine dehydratase can lead to various metabolic disorders, including hypermethioninemia and homocystinuria. These conditions are characterized by abnormal levels of certain amino acids in the blood and urine, which can have serious health consequences if left untreated.
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.
Nucleic acid conformation refers to the three-dimensional structure that nucleic acids (DNA and RNA) adopt as a result of the bonding patterns between the atoms within the molecule. The primary structure of nucleic acids is determined by the sequence of nucleotides, while the conformation is influenced by factors such as the sugar-phosphate backbone, base stacking, and hydrogen bonding.
Two common conformations of DNA are the B-form and the A-form. The B-form is a right-handed helix with a diameter of about 20 Å and a pitch of 34 Å, while the A-form has a smaller diameter (about 18 Å) and a shorter pitch (about 25 Å). RNA typically adopts an A-form conformation.
The conformation of nucleic acids can have significant implications for their function, as it can affect their ability to interact with other molecules such as proteins or drugs. Understanding the conformational properties of nucleic acids is therefore an important area of research in molecular biology and medicine.
AMP deaminase is an enzyme that is responsible for the conversion of adenosine monophosphate (AMP) to inosine monophosphate (IMP), which is a part of the purine nucleotide cycle. This enzyme plays a crucial role in energy metabolism, particularly in muscles during exercise. A deficiency in AMP deaminase has been linked to muscle fatigue and weakness.
Phylogeny is the evolutionary history and relationship among biological entities, such as species or genes, based on their shared characteristics. In other words, it refers to the branching pattern of evolution that shows how various organisms have descended from a common ancestor over time. Phylogenetic analysis involves constructing a tree-like diagram called a phylogenetic tree, which depicts the inferred evolutionary relationships among organisms or genes based on molecular sequence data or other types of characters. This information is crucial for understanding the diversity and distribution of life on Earth, as well as for studying the emergence and spread of diseases.
Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.
In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.
'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.
Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.
Adenosine is a purine nucleoside that is composed of a sugar (ribose) and the base adenine. It plays several important roles in the body, including serving as a precursor for the synthesis of other molecules such as ATP, NAD+, and RNA.
In the medical context, adenosine is perhaps best known for its use as a pharmaceutical agent to treat certain cardiac arrhythmias. When administered intravenously, it can help restore normal sinus rhythm in patients with paroxysmal supraventricular tachycardia (PSVT) by slowing conduction through the atrioventricular node and interrupting the reentry circuit responsible for the arrhythmia.
Adenosine can also be used as a diagnostic tool to help differentiate between narrow-complex tachycardias of supraventricular origin and those that originate from below the ventricles (such as ventricular tachycardia). This is because adenosine will typically terminate PSVT but not affect the rhythm of VT.
It's worth noting that adenosine has a very short half-life, lasting only a few seconds in the bloodstream. This means that its effects are rapidly reversible and generally well-tolerated, although some patients may experience transient symptoms such as flushing, chest pain, or shortness of breath.
HIV-1 (Human Immunodeficiency Virus type 1) is a species of the retrovirus genus that causes acquired immunodeficiency syndrome (AIDS). It is primarily transmitted through sexual contact, exposure to infected blood or blood products, and from mother to child during pregnancy, childbirth, or breastfeeding. HIV-1 infects vital cells in the human immune system, such as CD4+ T cells, macrophages, and dendritic cells, leading to a decline in their numbers and weakening of the immune response over time. This results in the individual becoming susceptible to various opportunistic infections and cancers that ultimately cause death if left untreated. HIV-1 is the most prevalent form of HIV worldwide and has been identified as the causative agent of the global AIDS pandemic.
Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).
Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.
Substrate specificity can be categorized as:
1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.
Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.
Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.
In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.
The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.
In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.
A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.
Alu elements are short, repetitive sequences of DNA that are found in the genomes of primates, including humans. These elements are named after the restriction enzyme Alu, which was used to first identify them. Alu elements are derived from a 7SL RNA molecule and are typically around 300 base pairs in length. They are characterized by their ability to move or "jump" within the genome through a process called transposition.
Alu elements make up about 11% of the human genome and are thought to have played a role in shaping its evolution. They can affect gene expression, regulation, and function, and have been associated with various genetic disorders and diseases. Additionally, Alu elements can also serve as useful markers for studying genetic diversity and evolutionary relationships among primates.
Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.
Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.
Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.
RNA (Ribonucleic Acid) is a single-stranded, linear polymer of ribonucleotides. It is a nucleic acid present in the cells of all living organisms and some viruses. RNAs play crucial roles in various biological processes such as protein synthesis, gene regulation, and cellular signaling. There are several types of RNA including messenger RNA (mRNA), ribosomal RNA (rRNA), transfer RNA (tRNA), small nuclear RNA (snRNA), microRNA (miRNA), and long non-coding RNA (lncRNA). These RNAs differ in their structure, function, and location within the cell.
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.
Adenosine monophosphate deaminase deficiency type 1
Cytidine deaminase
Adenosine-phosphate deaminase
RNA editing
Discovery and development of nucleoside and nucleotide reverse-transcriptase inhibitors
Purine nucleoside phosphorylase
AMPD3
Inosinic acid
Metabolic myopathy
Nucleic acid metabolism
Vidarabine
AMP deaminase
ADAR
AICA ribonucleotide
Nucleotide salvage
Atrazine chlorohydrolase
APOBEC1
RNA interference
Phage-assisted continuous evolution
Glycogen phosphorylase
FLNA
IGFBP7
CYFIP2
Purine metabolism
List of MeSH codes (D08)
Phycodnaviridae
Adenosine deaminase
APOBEC3G
Adenosine monophosphate
Amp
Activation-induced cytidine deaminase
ADAbase: Adenosine deaminase deficiency (ADA) | Nucleotide substitutions
Cytosine nucleoside/nucleotide deaminases and apolipoprotein B mRNA editing - Centre for Human Genetics
GNPDA1 glucosamine-6-phosphate deaminase 1 [Homo sapiens (human)] - Gene - NCBI
Adenosine monophosphate deaminase deficiency type 1 - Wikipedia
Metabolic Myopathies: Overview, Types of Myopathies, Classification
Vaccine-Derived Poliovirus Infection among Patients with Primary Immunodeficiency and Effect of Patient Screening on Disease...
PDF) A case of severe combined immunodeficiency caused by adenosine deaminase deficiency with a new mutation
1p6o.1 | SWISS-MODEL Template Library
ADAR gene: MedlinePlus Genetics
MedlinePlus - Search Results for: Adenosine
Research Consortium for Sickle Cell Disease | St. Jude Research
Adenosine Deaminase, Bovine Intestine CAS 9026-93-1 | 116880
5-Aza-dCTP, Nucleotides for Application in Epigenetics - Jena Bioscience
ProQR Announces First Quarter 2023 Operating and Financial
Mizoribine: A New Approach in the Treatment of Renal Disease
Post-transcriptional regulation (video) | Khan Academy
DNA damage induced by exercise in middle gluteal muscle of thoroughbreds horses
Frontiers | Association Mapping and Development of Marker-Assisted Selection Tools for the Resistance to White Pine Blister...
ADARB1 | Cancer Genetics Web
Controllable genome editing with split-engineered base editors | Nature Chemical Biology
Plus it
Human Metabolome Database: Showing metabocard for Water (HMDB0002111)
Gene Therapies Push Viral Vector Production
Nucleotide metabolism
NIST Genome Editing Lexicon | NIST
A putative osmoreceptor system that controls neutrophil function through the release of ATP, its conversion to adenosine, and...
Deaminases and Why Mice Sometimes Lie in Immuno-Oncology Pre-Clinical Trials? | Annals of Clinical Oncology | Science...
catabolism of purine nucleotides ppt
Clinical translation of epigenetics in cancer: eN-CORe-a report on the second workshop | Molecular Cancer Therapeutics |...
Cytosine6
- The crystal structure of yeast cytosine deaminase bound to 4(R)-hydroxyl-3,4-dihydropyrimidine at 1.14 angstroms. (expasy.org)
- The 1.14 a crystal structure of yeast Cytosine deaminase. (expasy.org)
- Here, we reveal sites that permit splitting of DNA cytosine deaminases into two inactive fragments, whose reapproximation reconstitutes activity. (nature.com)
- As predicted from the presence of the catalytic zinc-coordinating sequence motif conserved in the cytosine nucleoside/nucleotide deaminase family, BSD also contained one zinc per deaminase subunit. (rhea-db.org)
- The human DNA consists of approximately 3 billion nucleotides of four types: Adenine (A), cytosine (C), guanine (G), and thymine (T). In some cases, the difference of just one nucleotide can bring serious consequences. (medicilon.com)
- We are currently attempting to engineer SECURE adenine base editors and exploring the off-target RNA effects of cytosine base editors that use other deaminase enzymes than the one in the editor we investigated. (irbic.ir)
Myoadenylate deaminase3
- The disease was formerly known as myoadenylate deaminase deficiency (MADD). (wikipedia.org)
- Additionally, the presence of an abnormal allele in some patients, such as with myoadenylate deaminase deficiency, may not result in a specific muscular disorder. (medscape.com)
- Treatment of myoadenylate deaminase deficiency is exercise modulation as appropriate. (msdmanuals.com)
Enzymes7
- Evolution of nucleotide salvage enzymes and implications for genetic chemotherapy. (expasy.org)
- DNA deaminase enzymes play key roles in immunity and have recently been harnessed for their biotechnological applications. (nature.com)
- It is catalyzed by ADAR (adenosine deaminase acting on RNA) enzymes, which exist throughout the body but are most prevalent in the central nervous system. (biomedcentral.com)
- A-to-I editing, which is catalyzed by enzymes of the adenosine deaminase acting on RNA (ADAR) family, is most prevalent in the central nervous system (CNS) but occurs in many tissues [ 1 - 3 ]. (biomedcentral.com)
- All of these enzymes contain a conserved deaminase domain, shown in blue. (biomedcentral.com)
- Genetic defects involving enzymes essential for pyrimidine nucleotide metabolism have provided new insights into the vital physiological functions of these molecules in addition to nucleic acid synthesis. (tempsite.ws)
- To investigate the possibility of reducing or eliminating unwanted RNA edits, the MGH team screened 16 editors with engineered versions of the deaminase enzymes, identifying two that were as efficient as the original version in inducing on-target DNA effects while inducing markedly fewer RNA edits. (irbic.ir)
Adenine5
- The release of adenosine from adipocytes in which the nucleotide pool was labeled by incubation with either [ 14 C]- or [ 3 H]adenine was readily detected after 5 min of incubation and was maximal after 30 min. (aspetjournals.org)
- 3). Xanthosine, the initial substrate of purine alkaloid syn-thesis, is supplied by at least four diï¬ erent pathways: de novo purine biosynthesis (de novo route), the degradation pathways of adenine nucleotides (AMP route) and guanine nucleotides (GMP route), and the S-adenosyl-L-methionine (SAM) cycle (SAM route) (Fig. No public clipboards found for this slide. (hotelsunshine.co.in)
- ATP.E. Disorders of Purine and Pyrimidine Metabolism Rebecca S. Wappner PURINE AND PYRIMIDINE METABOLISM Purine and pyrimidine nucleotides are important constituents of RNA, DNA, nucleotide sugars, and other high-energy compounds and of cofactors such as adenosine triphosphate and nicotinamide-adenine dinucleotide. (euroasfalti.net)
- Adenosine kinase in red blood cells converts adenosine into adenine nucleotides. (turkupetcentre.net)
- Oxidative stress depletes adenosine triphosphate (ATP) and adenine nucleotides, whereas adenosine monophosphate (AMP) deaminase seems to depress energy metabolism by blocking the salvage pathway of purine nucleotides. (unisi.it)
Nucleoside6
- Nucleotidases Nucleoside phosphorylases Deaminases Xanthine oxidases 3. (hotelsunshine.co.in)
- Pyrimidine nucleotides are broken down first to the nucleoside and then to the base, as purine nucleotides are. (hotelsunshine.co.in)
- AMP, GMP, and IMP shift PRPP amido transferase from a small form to a large form.B. Human diseases that involve abnormalities in purine metabolism include gout, Lesch-Nyhan syndrome, adenosine deaminase deficiency, and purine nucleoside phosphorylase deficiency. (euroasfalti.net)
- Adenosine is rapidly catabolized by adenosine deaminases to inosine, which can be further deribosylated by purine nucleoside phosphorylase to hypoxantine . (turkupetcentre.net)
- Human diseases that involve abnormalities in purine metabolism include gout, Lesch-Nyhan syndrome, adenosine deaminase deficiency, and purine nucleoside phosphorylase deficiency. (tempsite.ws)
- See "Adenosine deaminase deficiency: Treatment and prognosis" and "Purine nucleoside phosphorylase deficiency" . (medilib.ir)
Single nucleotide po2
- Earlier studies systematically analyzed sequence variations in human pri-miRNAs/pre-miRNA and experimentally discovered that single nucleotide polymorphisms (SNPs) in miR-125a obstruct the processing of pri-miRNA to pre-miRNA [ 16 ]. (biomedcentral.com)
- CBEs are important genetic tools and could potentially correct more than 5,000 pathogenic single-nucleotide polymorphisms (SNPs) associated with human-inherited diseases. (biotechscope.com)
ADAR3
- The ADAR gene provides instructions for making a protein called RNA-specific adenosine deaminase 1 (ADAR1). (medlineplus.gov)
- These developments lead us to reappraise the likely impact of AID/APOBEC and ADAR deaminases in human cancer progression with their expected lesser impact on somatic mutagenesis in mouse cancer model systems. (sciencerepository.org)
- T transitions among the new genomes suggested that host restriction factors from the immune system such as ADAR and AID/APOBEC deaminases might be driving the genetic diversity of the chikungunya virus in Brazil. (butantan.gov.br)
Novo synthesis1
- Adenosine and deoxyadenosine are also converted to 5'-deoxyadenosine triphosphate (dATP), which inhibits ribonucleotide reductase and prevents de novo synthesis of nucleotides and deoxynucleotides. (medilib.ir)
Severe combined immunod3
- Adenosine deaminase (ADA) deficiency is a rare autosomal recessive disorder of purine metabolism that leads to severe combined immunodeficiency (SCID) by primarily affecting lymphocyte development and function. (researchgate.net)
- Adenosine deaminase (ADA) deficiency is an inherited disorder that damages the immune system and causes severe combined immunodeficiency (SCID). (nih.gov)
- Mutation in genes for adenosine deaminase (ADA) leads to severe combined immunodeficiency (SCID) in which both T-cells and B-cells are affected. (euroasfalti.net)
Deamination3
- The catabolism of pyrimidine nucleotides, like that of purine nucleotides (Chapter 10), involves dephosphorylation, deamination, and glycosidic bond cleavage. (hotelsunshine.co.in)
- Fludarabine Phosphate Injection, USP contains fludarabine phosphate, a fluorinated nucleotide analog of the antiviral agent vidarabine, 9-ß-D-arabinofuranosyladenine (ara-A) that is relatively resistant to deamination by adenosine deaminase. (guidelinecentral.com)
- By building on previous work demonstrating that the cytodine deaminase APOBEC3G (A3G) exhibited preferential deamination of the third C in the 5′-CCC-3′ motif, the team here sort out to determine whether this motif preference could be preserved in a CBE. (biotechscope.com)
Specific nucleotide1
- Also, these systems incorporate a base-altering enzyme-such as rat APOBEC1, a deaminase-to modify a specific nucleotide, thereby implementing changes that can lead to specific DNA alterations. (irbic.ir)
Pathways4
- Disorders of Purine and Pyrimidine Metabolism Georges van den Berghe PURINE METABOLISM METABOLIC PATHWAYS Purines comprise bases, nucleosides in association with ribose or deoxyribose, and nucleotides with one or more added phosphate groups. (euroasfalti.net)
- Mar 25, 2016 prpp purine nucleotides pyrimidine nucleotides denovo and salvage pathways. (web.app)
- Purine and pyrimidine nucleotides are synthesized by both de novo and salvage pathways (Figures 46-1 and 46-2).The de novo pathways create these complex phosphorylated molecules from simple precursors, such as CO 2, glycine, and glutamine, in stepwise fashion, whereas the salvage pathways serve the reuse of purine and pyrimidine bases of metabolic and dietary sources. (tempsite.ws)
- As we've just stated, inosine is an intermediate in several purine nucleotide pathways that affect muscle function. (tigerfitness.com)
Degradation2
- Catabolism of purinespurine nucleotide degradation refers to a regulated series of reactionsby which purine ribonucleotides and deoxyribonucleotides are degradedto uric acid in humans. (web.app)
- Disorders that involve abnormalities of nucleotide metabolism range from relatively common diseases such as hyperuricemia and gout, in which there is increased production or impaired excretion of a metabolic end product of purine metabolism (uric acid), to rare enzyme deficiencies that affect purine and pyrimidine synthesis or degradation. (tempsite.ws)
Deficiency10
- Adenosine monophosphate deaminase deficiency type 1 or AMPD1, is a human metabolic disorder in which the body consistently lacks the enzyme AMP deaminase, in sufficient quantities. (wikipedia.org)
- citation needed] AMPD1 deficiency is caused by a defect in the mechanism for production of AMP deaminase - an enzyme that converts adenosine monophosphate (AMP) to inosine monophosphate (IMP). (wikipedia.org)
- Adenosine deaminase 2 (ADA2) deficiency is a disorder characterized by abnormal inflammation of various tissues. (nih.gov)
- Adenosine monophosphate (AMP) deaminase deficiency is a condition that can affect the muscles used for movement (skeletal muscles). (nih.gov)
- The A3G-BEs had higher targeting precision than BE4max for reversing pathogenic SNPs for all three diseases and in the case of holocarboxylase synthetase deficiency, one A3G-BEs variant perfectly corrected only the target C nucleotide in more than 50% of the sequences, with up to a 6,496-fold higher correction frequencies than BE4max. (biotechscope.com)
- Nevertheless, it has been shown that in nucleated cells, P5′N‐1 deficiency results in abnormal pyrimidine nucleotide metabolism (Hopkinson et al, 1990). (tempsite.ws)
- INTRODUCTION - Adenosine deaminase (ADA) deficiency (MIM #102700) was the first immunodeficiency in which the specific molecular defect was identified. (medilib.ir)
- Cladribine and its rage of energy Carson et al 50, 51 discfromed that the lymphopenia observed in an inherited disstraighten out of adenosine deaminase deficiency was caworn not later than the accumulation of deoxyadenosine nucleotides within lymphocytes. (upb.ro)
- Diagnosis of adenosine deaminase deficiency is by DNA analysis. (msdmanuals.com)
- Treatment of adenosine deaminase deficiency is by bone marrow or stem cell transplantation and enzyme replacement therapy. (msdmanuals.com)
Blocks of nucleic acids1
- The purines and pyrimidines are nucleotides which form the building blocks of nucleic acids. (web.app)
Metabolism8
- Nucleotides are very important as cosubstrates in metabolism. (heresy.is)
- Textbook of Biochemistry: With Clinical Correlations 7th, Purine and Pyrimidine Nucleotide Metabolism. (euroasfalti.net)
- As a phosphoribosyltransferase is … metabolism of purine & pyrimidine nucleotides participate in many organisms carbamoyl phosphate is by. (euroasfalti.net)
- Break down purines that are inhibited by anticancer drugs, may nevertheless be metabolism of purine and pyrimidine nucleotides DNA. (euroasfalti.net)
- 17. Hohl CM. AMP deaminase in piglet cardiac myocytes: effect on nucleotide metabolism during ischemia. (oaepublish.com)
- Multiple choice questions chemistry and metabolism of nucleotides solved 1 which statement best describes xanthine. (web.app)
- 1) Lesch-Nyhan syndrome (pages 6-7) The Lesch-Nyhan syndrome is a sex linked defect of the Hypoxanthine, guanine, phosphoribosyl transferase (HGPRT) gene … Nucleotide Metabolism is an important issue in medical studies and therefore you can learn in this biochemistry article everything about purine & pyrimidines. (tempsite.ws)
- NUCLEOTIDE METABOLISM Mark Rush Nucleotides serve various metabolic functions. (tempsite.ws)
Synthesis3
- Bio-synthesis of Purines and Pyrimidines PPT) How nucleotides are synthesized in the cells? (hotelsunshine.co.in)
- Salvage pathway, c must come from exogenous uridine providing substrate for synthesis nucleotides! (euroasfalti.net)
- Purine Nucleotide Synthesis Disorders. (tempsite.ws)
Mutation1
- Cystic fibrosis, sickle cell anemia, Huntington's disease and phenylketonuria are all examples of disorders caused by the mutation of a single nucleotide, a building block of DNA. (medicilon.com)
Catabolism4
- Catabolism of the pyrimidine nucleotides leads ultimately to β-alanine (when CMP and UMP are degraded) or β-aminoisobutyrate (when dTMP is degraded) and NH 3 and CO 2.The β-alanine and β-aminoisobutyrate serve as -NH 2 donors in transamination of α-ketoglutarate to glutamate. (hotelsunshine.co.in)
- Catabolism of purine nucleotides. (hotelsunshine.co.in)
- Stomp On Step 1 59,204 views Catabolism Of Purine Nucleotides PPT. (hotelsunshine.co.in)
- uric acid is a breakdown product of purines (ATP, GTP, nucleic acids) and its excretion permits the necessary removal of nitrogen waste from the body Overview of purine catabolism - may also play a role in immunity as an adjuvant vaccination of an organism with antigen alone is likely to induce tolerance contains adequate amounts of the nucleotides. (hotelsunshine.co.in)
Purines1
- Purines are biologically synthesized as nucleotides and in particular as ribotides, i.e. (tempsite.ws)
APOBEC2
- While the AID/APOBEC deaminase specificity repertoire in dogs is likely to be less than in humans, it will be far greater than in the mouse and thus more likely to better mimic dysregulated Ig like somatic hypermutation responses during cancer progression in humans. (sciencerepository.org)
- However, a role for the APOBEC family of cytidine deaminases is proposed. (lu.se)
Cytidine2
- In the current study, the investigators used a variation of the Cas9 protein (nickase Cas9, or nCas9) fused with an enzyme called cytidine deaminase, which can substitute one nucleotide into another-generating single-nucleotide substitutions without DNA deletions. (medicilon.com)
- The IBS researchers were able to show the efficiency of the CRISPR-nCas9-cytidine deaminase fusion by generating mice that had changes to a single nucleotide in the dystrophin gene (Dmd) or the tyrosinase gene (Tyr). (medicilon.com)
CRISPR6
- In base editors (BEs), the combination of DNA deaminase mutator activity with CRISPR-Cas localization confers the powerful ability to directly convert one target DNA base into another. (nature.com)
- However, it is technically challenging to replace a single nucleotide with the current gene editing tool, CRISPR-Cas9. (medicilon.com)
- Scientists at the Center for Genome Engineering, within the Institute for Basic Science (IBS) have used a variation of the popular gene editing technique CRISPR-Cas9 to produce mice with a single nucleotide difference. (medicilon.com)
- Although genome editing with programmable nucleases such as CRISPR-Cas9 or Cpf1 systems holds promise for gene correction to repair genetic defects that cause genetic diseases, it is technically challenging to induce single-nucleotide substitutions in a targeted manner," the authors wrote. (medicilon.com)
- The most frequently used CRISPR/Cas9 technique works by cutting around the faulty nucleotide in both strands of the DNA and cuts out a small part of DNA. (medicilon.com)
- We evolved a tRNA adenosine deaminase to operate on DNA when fused to a catalytically impaired CRISPR-Cas9. (scentoferos.com)
Gene4
- The human glucosamine-6-phosphate deaminase gene: cDNA cloning and expression, genomic organization and chromosomal localization. (nih.gov)
- ADA gene provides instructions for producing the enzyme adenosine deaminase. (nih.gov)
- gene provides instructions for making an enzyme called adenosine deaminase 2. (nih.gov)
- gene provides instructions for producing an enzyme called adenosine monophosphate (AMP) deaminase. (nih.gov)
Cas92
- CRC researchers created base editors - modified types of Cas9 protein fused to a nucleotide deaminase. (stjude.org)
- Base editors comprise deaminases fused to either Cas9 nickase or catalytically-dead Cas9. (biotechscope.com)
SNPs1
- However, nearly 38% of the SNPs that are caused by T-to-C disease point mutations lie in the context of CC, therefore there is a need to develop new CBEs that can accurately edit just the target nucleotide. (biotechscope.com)
Converts3
- AMP deaminase is an enzyme that converts adenosine monophosphate (AMP) to inosine monophosphate (IMP), freeing an ammonia molecule in the process. (wikipedia.org)
- The enzyme myoadenylate deaminase converts AMP to inosine and ammonia. (msdmanuals.com)
- Adenosine deaminase converts adenosine and deoxyadenosine to inosine and deoxyinosine, which are further broken down and excreted. (msdmanuals.com)
Guanosine1
- Once an adenosine nucleotide is converted to an inosine, it acts in a manner similar to a guanosine nucleotide, with a number of potential consequences [ 4 ]. (biomedcentral.com)
Biosynthesis2
- State the relevance of coordinated control of purine and pyrimidine nucleotide biosynthesis. (hotelsunshine.co.in)
- Purine Biosynthesis Purine nucleotide biosynthesis is a complex 10 step process. (hotelsunshine.co.in)
Substitutions4
- As a result, insertion/deletions (indels) are obtained much more frequently at a nuclease target site than are single-nucleotide substitutions. (medicilon.com)
- Moreover, these single-nucleotide substitutions appeared only in the target position. (medicilon.com)
- We showed here for the first time that programmable deaminases efficiently induced base substitutions in animal embryos, producing mutant mice with disease phenotypes," remarked senior study investigator Jin-Soo Kim, Ph.D., director of the Center for Genome Engineering at IBS. (medicilon.com)
- They reported the use of RNA-programmable deaminases to make various animal models with single amino-acid substitutions.They linked the single amino acid substitutions from the correction of nonsense mutations in the future to the correction of genetic defects in human embryos. (scentoferos.com)
Inosine monophosphate1
- Remove adenosine via the adenosine deaminase enzyme to form inosine monophosphate. (tigerfitness.com)
CDNA1
- We established an efficient overproduction-purification system for blasticidin S deaminase (BSD) using the cDNA cloned from Aspergillus terreus. (rhea-db.org)
MRNA1
- When this conversion occurs in the coding region of mRNA, it results in an altered nucleotide codon and, therefore, can change the amino acid sequence of the coded protein in what is referred to as a re-coding editing event. (biomedcentral.com)
Isoform2
- Allosteric kinetics of the isoform 1 of human glucosamine-6-phosphate deaminase. (nih.gov)
- Adenosine deaminase isoform 1 (ADA1) is found in most cells, including blood cells. (turkupetcentre.net)
ADAR11
- instructions for making a protein called RNA-specific adenosine deaminase 1 (ADAR1). (nih.gov)
Peptides1
- Why, then, do cosubstrates so often possess nucleotides as their binding tags, rather than for example amino acids or peptides? (heresy.is)
Catalytic1
- Expression, purification, and characterization of blasticidin S deaminase (BSD) from Aspergillus terreus: the role of catalytic zinc in enzyme structure. (rhea-db.org)
Sequence3
- RNA editing refers to post-transcriptional processes that alter the nucleotide sequence of an RNA transcript by insertion, deletion or nucleotide conversion. (biomedcentral.com)
- We developed number of models using various types of features and achieved maximum accuracy of 66% using binary profile of nucleotide sequence taken from 5p arm of hairpin. (biomedcentral.com)
- Now, a team of scientists, led by Zue Gao and Erwei Zuo, from Rice University, US, the University of Chinese Academy of Sciences and the Chinese Academy of Agricultural Sciences, have identified a human deaminase as a candidate for developing sequence-specific BEs in mulitple C contexts. (biotechscope.com)
Genes1
- Based on linkage disequilibrium (LD)-based association mapping used to detect single nucleotide polymorphism (SNP) markers associated with MGR against C. ribicola , MGR in these seed families appears to be controlled by Cr4 or other R genes in very close proximity to Cr4 . (frontiersin.org)
Editing3
- We show that the seBE strategy facilitates robust regulated editing with BE scaffolds containing diverse deaminases, offering a generalizable solution for temporally controlling precision genome editing. (nature.com)
- The work here demonstrates the next step towards enhancing CBEs to recognise a specific CC motif, and permitting accurate and predictable edits of the target nucleotide whilst eliminating bystander editing. (biotechscope.com)
- In fact, these SECURE (SElective Curbing of Unwanted RNA Editing) variants were even more precise than the unaltered deaminase in inducing the desired DNA edits. (irbic.ir)
Cleavage1
- We used the dataset of experimentally validated human miRNA hairpins from miRBase, and extracted fourteen nucleotides around Dicer cleavage sites. (biomedcentral.com)
Kinase1
- Metformin activates AMP kinase through inhibition of AMP deaminase. (oaepublish.com)
Genomic1
- They avoid inflicting anything so extreme as a double-strand break, and they confine their genomic activities to single-nucleotide changes-reasonably on-target changes. (irbic.ir)
Phosphate groups1
- Structurally speaking, ATP is simply an RNA nucleotide with a "tail" comprised of three phosphate groups. (tigerfitness.com)
Occur1
- Nucleotides also occur as parts of more complex cosubstrates and coenzymes, three of which are shown here. (heresy.is)