The removal of an amino group (NH2) from a chemical compound.
An enzyme that catalyzes the deamination of cytidine, forming uridine. EC 3.5.4.5.
A pyrimidine base that is a fundamental unit of nucleic acids.
A methylated nucleotide base found in eukaryotic DNA. In ANIMALS, the DNA METHYLATION of CYTOSINE to form 5-methylcytosine is found primarily in the palindromic sequence CpG. In PLANTS, the methylated sequence is CpNpGp, where N can be any base.
A pyrimidine nucleoside that is composed of the base CYTOSINE linked to the five-carbon sugar D-RIBOSE.
An enzyme that catalyzes the hydrolysis of ADENOSINE to INOSINE with the elimination of AMMONIA.
An enzyme that catalyzes the HYDROLYSIS of the N-glycosidic bond between sugar phosphate backbone and URACIL residue during DNA synthesis.
A process that changes the nucleotide sequence of mRNA from that of the DNA template encoding it. Some major classes of RNA editing are as follows: 1, the conversion of cytosine to uracil in mRNA; 2, the addition of variable number of guanines at pre-determined sites; and 3, the addition and deletion of uracils, templated by guide-RNAs (RNA, GUIDE).
Nitrous acid (HNO2). A weak acid that exists only in solution. It can form water-soluble nitrites and stable esters. (From Merck Index, 11th ed)
A purine nucleoside that has hypoxanthine linked by the N9 nitrogen to the C1 carbon of ribose. It is an intermediate in the degradation of purines and purine nucleosides to uric acid and in pathways of purine salvage. It also occurs in the anticodon of certain transfer RNA molecules. (Dorland, 28th ed)
Catalyze the hydrolysis of nucleosides with the elimination of ammonia.
An enzyme that catalyzes the deamination of guanine to form xanthine. EC 3.5.4.3.
A group of enzymes including those oxidizing primary monoamines, diamines, and histamine. They are copper proteins, and, as their action depends on a carbonyl group, they are sensitive to inhibition by semicarbazide.
Uracil is a nitrogenous base, specifically a pyrimidine derivative, which constitutes one of the four nucleobases in the nucleic acid of RNA (ribonucleic acid), pairing with adenine via hydrogen bonds during base-pairing. (25 words)
Drugs that inhibit ADENOSINE DEAMINASE activity.
An enzyme which catalyzes the deamination of CYTOSINE resulting in the formation of URACIL. It can also act on 5-methylcytosine to form THYMIDINE.
A programmed mutation process whereby changes are introduced to the nucleotide sequence of immunoglobulin gene DNA during development.
The creation of an amine. It can be produced by the addition of an amino group to an organic compound or reduction of a nitro group.
An enzyme that removes THYMINE and URACIL bases mispaired with GUANINE through hydrolysis of their N-glycosidic bond. These mispaired nucleotides generally occur through the hydrolytic DEAMINATION of 5-METHYLCYTOSINE to thymine.
An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in regulating the metabolic degradation of catecholamines and serotonin in neural or target tissues. Hepatic monoamine oxidase has a crucial defensive role in inactivating circulating monoamines or those, such as tyramine, that originate in the gut and are absorbed into the portal circulation. (From Goodman and Gilman's, The Pharmacological Basis of Therapeutics, 8th ed, p415) EC 1.4.3.4.
A ribonucleoside antibiotic synergist and adenosine deaminase inhibitor isolated from Nocardia interforma and Streptomyces kaniharaensis. It is proposed as an antineoplastic synergist and immunosuppressant.
Catalyze the hydrolysis of nucleotides with the elimination of ammonia.
Aminohydrolases are a class of enzymes that catalyze the hydrolysis of various nitrogenous compounds, including proteins, nucleotides, and amines, playing a crucial role in numerous biological processes such as metabolism and signaling.
A family of DNA repair enzymes that recognize damaged nucleotide bases and remove them by hydrolyzing the N-glycosidic bond that attaches them to the sugar backbone of the DNA molecule. The process called BASE EXCISION REPAIR can be completed by a DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE which excises the remaining RIBOSE sugar from the DNA.
Inorganic salts of sulfurous acid.
An enzyme that catalyzes the deamination of AMP to IMP. EC 3.5.4.6.
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.
An inhibitor of nucleotide metabolism.
A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.
A class of enzymes involved in the hydrolysis of the N-glycosidic bond of nitrogen-linked sugars.
An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
5-Hydroxymethyl-6-methyl- 2,4-(1H,3H)-pyrimidinedione. Uracil derivative used in combination with toxic antibiotics to lessen their toxicity; also to stimulate leukopoiesis and immunity. Synonyms: pentoksil; hydroxymethylmethyluracil.
An enzyme which catalyzes an endonucleolytic cleavage near PYRIMIDINE DIMERS to produce a 5'-phosphate product. The enzyme acts on the damaged DNA strand, from the 5' side of the damaged site.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
Thymine is a pyrimidine nucleobase, one of the four nucleobases in the nucleic acid of DNA (the other three being adenine, guanine, and cytosine), where it forms a base pair with adenine.
A class of enzymes that catalyze oxidation-reduction reactions of amino acids.
An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.
Enzymes that catalyze the formation of a carbon-carbon double bond by the elimination of AMMONIA. EC 4.3.1.
Methylases that are specific for CYTOSINE residues found on DNA.
The rate dynamics in chemical or physical systems.
An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.
A nucleoside that is composed of ADENINE and D-RIBOSE. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter.
A chemically heterogeneous group of drugs that have in common the ability to block oxidative deamination of naturally occurring monoamines. (From Gilman, et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 8th ed, p414)
2'-Deoxyuridine. An antimetabolite that is converted to deoxyuridine triphosphate during DNA synthesis. Laboratory suppression of deoxyuridine is used to diagnose megaloblastic anemias due to vitamin B12 and folate deficiencies.
Gene rearrangement of the B-lymphocyte which results in a substitution in the type of heavy-chain constant region that is expressed. This allows the effector response to change while the antigen binding specificity (variable region) remains the same. The majority of class switching occurs by a DNA recombination event but it also can take place at the level of RNA processing.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Guanine is a purine nucleobase, one of the four nucleobases in the nucleic acid of DNA and RNA, involved in forming hydrogen bonds between complementary base pairs in double-stranded DNA molecules.
Proteins encoded by the VIF GENES of the HUMAN IMMUNODEFICIENCY VIRUS.

Influence of 1-[(E)-2-(2-methyl-4-nitrophenyl)diaz-1-enyl]pyrrolidine-2-carboxylic acid and diphenyliodonium chloride on ruminal protein metabolism and ruminal microorganisms. (1/339)

The effects of 1-[(E)-2-(2-methyl-4-nitrophenyl)diaz-1-enyl]pyrrolidine-2-carboxy lic acid (LY29) and diphenyliodonium chloride (DIC) on the degradation of protein to ammonia were determined in a mixed rumen microbial population taken from sheep on a grass hay-concentrate diet. Both compounds decreased NH3 production by inhibiting deamination of amino acids. LY29, but not DIC, inhibited growth of the high-activity ammonia-producing species, Clostridium aminophilum and Clostridium sticklandii.  (+info)

Effect of the ratio between essential and nonessential amino acids in the diet on utilization of nitrogen and amino acids by growing pigs. (2/339)

In 36 growing pigs (30 to 60 kg), N balance and amino acid (AA) composition of weight gain were measured to evaluate the interactive effect of the ratio between N from essential amino acids (EAA(N)) to nonessential amino acids (NEAA(N)) and total N level (T(N)) in the diet on N retention and utilization of N, EAA(N), NEAA(N), and AA. Nine diets composed from ordinary feedstuffs and supplemented with crystalline AA were used (three EAA(N):NEAA(N) ratios of 38:62, 50:50, and 62:38 at three T(N) levels of 18.8, 22.9, and 30.0 g/kg). Pigs were fed restrictedly, at a level of 2.8 x energy for maintenance. In all diets, EAA (including arginine) supply was according to or slightly above the recommended ratios to lysine. Measurements were done in four blocks of nine pigs each. In a concomitant slaughter experiment, the AA composition of deposited body protein was determined to estimate AA utilization. The effects of T(N) and EAA(N):NEAA(N) and their interaction for N retention and utilization were significant. Nitrogen retention increased with higher T(N) in the diet. Increasing EAA(N):NEAA(N) from 38:62 to 50:50 improved N retention only at the two lower T(N) levels. Increasing EAA(N): NEAA(N) above 50:50 failed to improve N retention significantly at any of the three T(N) levels. Lowering T(N) improved the utilization of total and digested N and of EAA(N) and NEAA(N). The increase in EAA(N): NEAA(N) consistently resulted in a lower utilization of EAA(N), but this was compensated by a higher utilization of NEAA(N). The utilization of T(N) was improved by increasing EAA(N):NEAA(N) from 38:62 to 50:50 at the two lower T(N) levels and was relatively unaffected by EAA(N):NEAA(N) at the highest T(N). However, a lower utilization of N was observed at a ratio of 62:38 at a T(N) level of 22.9 g/kg. The effects were similar for utilization of individual EAA and NEAA. Utilization of alanine, aspartic acid, and glycine was close to or >100% at the highest EAA(N):NEAA(N), which was expected because all of these AA are synthesized in pigs. Also, the utilization of arginine was >100% in most of the treatments, which confirms the semiessential character of this AA for maintenance. We concluded that the required ratio of EAA(N):NEAA(N) for optimal N retention and utilization is approximately 50:50. The EAA(N):NEAA(N) is more important at lower dietary protein levels. This study indicates that EAA(N): NEAA(N) can be increased up to 70:30 without lowering the utilization of N. Thus, deaminated EAA(N) was efficiently utilized for the synthesis of NEAA(N).  (+info)

Nitric oxide-induced damage to mtDNA and its subsequent repair. (3/339)

Mutations in mitochondrial DNA (mtDNA) have recently been associated with a variety of human diseases. One potential DNA-damaging agent to which cells are continually exposed that could be responsible for some of these mutations is nitric oxide (NO). To date, little information has been forthcoming concerning the damage caused by this gas to mtDNA. Therefore, this study was designed to investigate damage to mtDNA induced by NO and to evaluate its subsequent repair. Normal human fibroblasts were exposed to NO produced by the rapid decomposition of 1-propanamine, 3-(2-hydroxy-2-nitroso-1-propylhydrazino) (PAPA NONOate) and the resultant damage to mtDNA was determined by quantitative Southern blot analysis. This gas was found to cause damage to mtDNA that was alkali-sensitive. Treatment of the DNA with uracil-DNA glycosylase or 3-methyladenine DNA glycosylase failed to reveal additional damage, indicating that most of the lesions produced were caused by the deamination of guanine to xanthine. Studies using ligation-mediated PCR supported this finding. When a 200 bp sequence of mtDNA from cells exposed to NO was analyzed, guanine was found to be the predominantly damaged base. However, there also was damage to specific adenines. No lesions were observed at pyrimidine sites. The nucleotide pattern of damage induced by NO was different from that produced by either a reactive oxygen species generator or the methylating chemical, methylnitrosourea. Most of the lesions produced by NO were repaired rapidly. However, there appeared to be a subset of lesions which were repaired either slowly or not at all by the mitochondria.  (+info)

AMP deamination and purine exchange in human skeletal muscle during and after intense exercise. (4/339)

1. The present study examined the regulation of human skeletal muscle AMP deamination during intense exercise and quantified muscle accumulation and release of purines during and after intense exercise. 2. Seven healthy males performed knee extensor exercise at 64.3 W (range: 50-70 W) to exhaustion (234 s; 191-259 s). In addition, on two separate days the subjects performed exercise at the same intensity for 30 s and 80 % of exhaustion time (mean, 186 s; range, 153-207 s), respectively. Muscle biopsies were obtained from m.v. lateralis before and after each of the exercise bouts. For the exhaustive bout femoral arterio-venous concentration differences and blood flow were also determined. 3. During the first 30 s of exercise there was no change in muscle adenosine triphosphate (ATP), inosine monophosphate (IMP) and ammonia (NH3), although estimated free ADP and AMP increased 5- and 45-fold, respectively, during this period. After 186 s and at exhaustion muscle ATP had decreased (P < 0.05) by 15 and 19 %, respectively, muscle IMP was elevated (P < 0. 05) from 0.20 to 3.65 and 5.67 mmol (kg dry weight)-1, respectively, and muscle NH3 had increased (P < 0.05) from 0.47 to 2.55 and 2.33 mmol (kg d.w.)-1, respectively. The concentration of H+ did not change during the first 30 s of exercise, but increased (P < 0.05) to 245.9 nmol l-1 (pH 6.61) after 186 s and to 374.5 nmol l-1 (pH 6. 43) at exhaustion. 4. Muscle inosine and hypoxanthine did not change during exercise. In the first 10 min after exercise the muscle IMP concentration decreased (P < 0.05) by 2.96 mmol (kg d.w.)-1 of which inosine and hypoxanthine formation could account for 30 %. The total release of inosine and hypoxanthine during exercise and 90 min of recovery amounted to 1.07 mmol corresponding to 46 % of the net ATP decrease during exercise or 9 % of ATP at rest. 5. The present data suggest that AMP deamination is inhibited during the initial phase of intense exercise, probably due to accumulation of orthophosphate, and that lowered pH is an important positive modulator of AMP deaminase in contracting human skeletal muscle in vivo. Furthermore, formation and release of purines occurs mainly after intense exercise and leads to a considerable loss of nucleotides.  (+info)

Helicobacter pylori rocF is required for arginase activity and acid protection in vitro but is not essential for colonization of mice or for urease activity. (5/339)

Arginase of the Helicobacter pylori urea cycle hydrolyzes L-arginine to L-ornithine and urea. H. pylori urease hydrolyzes urea to carbon dioxide and ammonium, which neutralizes acid. Both enzymes are involved in H. pylori nitrogen metabolism. The roles of arginase in the physiology of H. pylori were investigated in vitro and in vivo, since arginase in H. pylori is metabolically upstream of urease and urease is known to be required for colonization of animal models by the bacterium. The H. pylori gene hp1399, which is orthologous to the Bacillus subtilis rocF gene encoding arginase, was cloned, and isogenic allelic exchange mutants of three H. pylori strains were made by using two different constructs: 236-2 and rocF::aphA3. In contrast to wild-type (WT) strains, all rocF mutants were devoid of arginase activity and had diminished serine dehydratase activity, an enzyme activity which generates ammonium. Compared with WT strain 26695 of H. pylori, the rocF::aphA3 mutant was approximately 1, 000-fold more sensitive to acid exposure. The acid sensitivity of the rocF::aphA3 mutant was not reversed by the addition of L-arginine, in contrast to the WT, and yielded a approximately 10, 000-fold difference in viability. Urease activity was similar in both strains and both survived acid exposure equally well when exogenous urea was added, indicating that rocF is not required for urease activity in vitro. Finally, H. pylori mouse-adapted strain SS1 and the 236-2 rocF isogenic mutant colonized mice equally well: 8 of 9 versus 9 of 11 mice, respectively. However, the rocF::aphA3 mutant of strain SS1 had moderately reduced colonization (4 of 10 mice). The geometric mean levels of H. pylori recovered from these mice (in log(10) CFU) were 6.1, 5.5, and 4.1, respectively. Thus, H. pylori rocF is required for arginase activity and is crucial for acid protection in vitro but is not essential for in vivo colonization of mice or for urease activity.  (+info)

UV filter compounds in human lenses: the origin of 4-(2-amino-3-hydroxyphenyl)-4-oxobutanoic acid O-beta-D-glucoside. (6/339)

PURPOSE: To investigate UV filter synthesis in the human lens, in particular the biosynthetic origin of the second most abundant UV filter compound, 4-(2-amino-3-hydroxyphenyl)-4-oxobutanoic acid O-beta-D-glucoside. METHODS: Human lenses were analyzed by high-performance liquid chromatography (HPLC) after separate incubation with 3H-tryptophan (3H-Trp), beta-benzoylacrylic acid, D,L-alpha-amino-beta-benzoylpropionic acid, or D,L-3-hydroxykynurenine O-beta-D-glucoside. The effect of pH on the model compound D,L-alpha-amino-beta-benzoylpropionic acid and D,L-3-hydroxykynurenine O-beta-D-glucoside was also investigated. RESULTS: UV filters were not detected in fetal lenses, despite a 5-month postnatal lens displaying measurable levels of UV filters. In adults no radiolabel was incorporated into 4-(2-amino-3-hydroxyphenyl)-4-oxobutanoic acid O-beta-D-glucoside after 3H-Trp incubations. Beta-benzoylacrylic acid was readily reduced in lenses. D,L-alpha-amino-beta-benzoylpropionic acid and D,L-3-hydroxykynurenine O-beta-D-glucoside slowly deaminated at physiological pH and were converted to beta-benzoylpropionic acid and 4-(2-amino-3-hydroxyphenyl)-4-oxobutanoic acid O-beta-D-glucoside, respectively, after lens incubations. CONCLUSIONS: UV filter biosynthesis appears to be activated at or near birth. Compounds containing the kynurenine side chain slowly deaminate, and in the lens, the newly formed double bond is rapidly reduced. These findings suggest that 4-(2-amino-3-hydroxyphenyl)-4-oxobutanoic acid O-beta-D-glucoside is derived from L-3-hydroxykynurenine O-beta-D-glucoside through this deamination-reduction process. The slowness of the deamination presumably accounts for the absence of incorporation of radiolabel from 3H-Trp into 4(2-amino-3-hydroxyphenyl)4-oxobutanoic acid O-beta-D-glucoside.  (+info)

Characterization of human lens major intrinsic protein structure. (7/339)

PURPOSE: To determine the primary covalent structure of human lens major intrinsic protein (MIP) in lenses of varying age. METHODS: MIP was isolated from single human lenses of various ages (7- 86 years) by homogenization of the lenses, followed by centrifugation and urea washes of the membranes. Proteins present in the membrane preparation were reduced, alkylated, and cleaved by CNBr. Peptide fragments were fractionated by reverse-phase high-performance liquid chromatography, and the primary structures of the peptides were determined by tandem mass spectrometry and Edman sequencing. RESULTS: Complete coverage of the human MIP sequence was observed in the form of CNBr fragments. In addition, peptide structures resulting from in vivo heterogeneous N- and C-terminal cleavage were characterized. The amount of intact MIP decreased with lens age; however, the pattern of truncation did not change from 7 to 86 years. The major site of phosphorylation was identified as serine 235. Asparagine residues 246 and 259 were completely deamidated by age 7 years. CONCLUSIONS: The major structural modifications of human lens MIP have been determined. Human MIP is heterogeneously modified in lenses ranging in age from 7 to 86 years of age by N- and C-terminal truncation, phosphorylation, and deamidation, resulting in decreased levels of native intact MIP with age.  (+info)

Effect of UV-A light on the chaperone-like properties of young and old lens alpha-crystallin. (8/339)

PURPOSE: To study the damaging effect of UV-A irradiation on the chaperone-like properties of alpha-crystallin and the subsequent recovery process of young and old bovine lenses. METHODS: Young and old bovine lenses were kept in organ culture. After 24 hours of incubation they were irradiated with UV-A at 365 nm, and optical quality measurements were performed during the experiments (192 hours). alpha-Crystallin and alpha1-, alphaA2-, alphaB1-, and alphaB2-crystallin subunits were analyzed, separated by gel filtration and cation exchange chromatography, respectively, after different culture times. Protein patterns were obtained after two-dimensional (2-D) gel electrophoresis. Chaperone-like activity was determined on the basis of insulin B-chain and betaL-crystallin aggregation assays. Aggregation of alpha-crystallin was analyzed, tryptophan fluorescence measurements were performed, and alpha-crystallin mRNA levels were determined. RESULTS: The water-soluble alpha-crystallin obtained from old lenses compared with young lenses after UV irradiation had decreased chaperone activity, a higher molecular weight, and increased loss of tryptophan fluorescence. Moreover, alpha-crystallin mRNA virtually disappeared, whereas extra spots on the 2-D protein pattern appeared, possibly because of deamidation. CONCLUSIONS: alpha-Crystallin obtained from old lenses is more affected by irradiation than alpha-crystallin derived from young lenses. Moreover, it appeared that alphaB-crystallin from UV-treated old lenses compared with control lenses was less susceptible to UV-A than alphaA-crystallin. It may well be that alphaB-crystallin protects alphaA-crystallin in vivo.  (+info)

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.

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.

Cytosine is one of the four nucleobases in the nucleic acid molecules DNA and RNA, along with adenine, guanine, and thymine (in DNA) or uracil (in RNA). The single-letter abbreviation for cytosine is "C."

Cytosine base pairs specifically with guanine through hydrogen bonding, forming a base pair. In DNA, the double helix consists of two complementary strands of nucleotides held together by these base pairs, such that the sequence of one strand determines the sequence of the other. This property is critical for DNA replication and transcription, processes that are essential for life.

Cytosine residues in DNA can undergo spontaneous deamination to form uracil, which can lead to mutations if not corrected by repair mechanisms. In RNA, cytosine can be methylated at the 5-carbon position to form 5-methylcytosine, a modification that plays a role in regulating gene expression and other cellular processes.

5-Methylcytosine (5mC) is a chemical modification of the nucleotide base cytosine in DNA, where a methyl group (-CH3) is added to the 5th carbon atom of the cytosine ring. This modification is catalyzed by DNA methyltransferase enzymes and plays an essential role in epigenetic regulation of gene expression, genomic imprinting, X-chromosome inactivation, and suppression of transposable elements in eukaryotic cells. Abnormal DNA methylation patterns have been associated with various diseases, including cancer.

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 (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.

Uracil-DNA glycosylase (UDG) is an enzyme that plays a crucial role in the maintenance of genomic stability by removing uracil residues from DNA. These enzymes are essential because uracil can arise in DNA through the deamination of cytosine or through the misincorporation of dUMP during DNA replication. If left unrepaired, uracil can pair with adenine, leading to C:G to T:A transitions during subsequent rounds of replication.

UDGs initiate the base excision repair (BER) pathway by cleaving the N-glycosidic bond between the uracil base and the deoxyribose sugar, releasing the uracil base and creating an abasic site. The resulting apurinic/apyrimidinic (AP) site is then processed further by AP endonucleases, DNA polymerases, and ligases to complete the repair process.

There are several subtypes of UDGs that differ in their substrate specificity, cellular localization, and regulation. For example, some UDGs specifically remove uracil from single-stranded or double-stranded DNA, while others have broader substrate specificity and can also remove other damaged bases. Understanding the function and regulation of these enzymes is important for understanding the mechanisms that maintain genomic stability and prevent mutations.

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.

I'm sorry for any confusion, but "Nitrous Acid" is not a term used in medical definitions. Nitrous acid is a chemical compound with the formula HNO2. It is a weak acid and a powerful oxidizing agent. It is used as a reducing agent in organic synthesis and as a laboratory reagent to produce nitric oxide.

If you have any questions related to medical terminology or health concerns, I would be happy to help with those!

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.

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.

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.

Uracil is not a medical term, but it is a biological molecule. Medically or biologically, uracil can be defined as one of the four nucleobases in the nucleic acid of RNA (ribonucleic acid) that is linked to a ribose sugar by an N-glycosidic bond. It forms base pairs with adenine in double-stranded RNA and DNA. Uracil is a pyrimidine derivative, similar to thymine found in DNA, but it lacks the methyl group (-CH3) that thymine has at the 5 position of its ring.

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.

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.

Somatic hypermutation is a process that occurs in the immune system, specifically within B cells, which are a type of white blood cell responsible for producing antibodies. This process involves the introduction of point mutations into the immunoglobulin (Ig) genes, which encode for the variable regions of antibodies.

Somatic hypermutation occurs in the germinal centers of lymphoid follicles in response to antigen stimulation. The activation-induced cytidine deaminase (AID) enzyme is responsible for initiating this process by deaminating cytosines to uracils in the Ig genes. This leads to the introduction of point mutations during DNA replication and repair, which can result in changes to the antibody's binding affinity for the antigen.

The somatic hypermutation process allows for the selection of B cells with higher affinity antibodies that can better recognize and neutralize pathogens. This is an important mechanism for the development of humoral immunity and the generation of long-lived memory B cells. However, excessive or aberrant somatic hypermutation can also contribute to the development of certain types of B cell malignancies, such as lymphomas and leukemias.

Amination is a chemical process or reaction that involves the addition of an amino group (-NH2) to a molecule. This process is often used in organic chemistry to create amines, which are compounds containing a basic nitrogen atom with a lone pair of electrons.

In the context of biochemistry, amination reactions play a crucial role in the synthesis of various biological molecules, including amino acids, neurotransmitters, and nucleotides. For example, the enzyme glutamine synthetase catalyzes the amination of glutamate to form glutamine, an essential amino acid for many organisms.

It is important to note that there are different types of amination reactions, depending on the starting molecule and the specific amino group donor. The precise mechanism and reagents used in an amination reaction will depend on the particular chemical or biological context.

Thymine DNA Glycosylase (TDG) is an enzyme that plays a crucial role in the process of base excision repair (BER), which is a mechanism for correcting damaged or mismatched bases in DNA. Specifically, TDG is responsible for removing thymine bases that have been improperly incorporated into DNA opposite to guanine, forming a so-called "mismatch" or "lesion." This type of lesion can arise due to errors during DNA replication or from the mutagenic effects of environmental agents such as chemicals and radiation.

TDG recognizes and binds to the thymine-guanine mismatch, then catalyzes the removal of the thymine base by cleaving the N-glycosidic bond that links it to the deoxyribose sugar in the DNA backbone. This creates an abasic site, which is subsequently processed by other enzymes involved in BER to restore the original DNA sequence.

In addition to its role in DNA repair, TDG has been implicated in various cellular processes such as transcriptional regulation and epigenetic modification, due to its ability to interact with other proteins and regulatory elements in the genome. Dysregulation of TDG function has been linked to several human diseases, including cancer and neurological disorders.

Monoamine oxidase (MAO) is an enzyme found on the outer membrane of mitochondria in cells throughout the body, but primarily in the gastrointestinal tract, liver, and central nervous system. It plays a crucial role in the metabolism of neurotransmitters and dietary amines by catalyzing the oxidative deamination of monoamines. This enzyme exists in two forms: MAO-A and MAO-B, each with distinct substrate preferences and tissue distributions.

MAO-A preferentially metabolizes serotonin, norepinephrine, and dopamine, while MAO-B is mainly responsible for breaking down phenethylamines and benzylamines, as well as dopamine in some cases. Inhibition of these enzymes can lead to increased neurotransmitter levels in the synaptic cleft, which has implications for various psychiatric and neurological conditions, such as depression and Parkinson's disease. However, MAO inhibitors must be used with caution due to their potential to cause serious adverse effects, including hypertensive crises, when combined with certain foods or medications containing dietary amines or sympathomimetic agents.

Coformycin is an antimetabolite antibiotic, which means it interferes with the growth of bacteria by inhibiting the synthesis of nucleic acids, the genetic material of bacteria. It is derived from Streptomyces coelicolor and is used primarily in research to study bacterial metabolism.

Coformycin is a potent inhibitor of bacterial enzyme adenosine deaminase, which is involved in purine biosynthesis. By inhibiting this enzyme, Coformycin prevents the bacteria from synthesizing the building blocks needed to make DNA and RNA, thereby inhibiting their growth.

Coformycin has not been approved for use as a therapeutic drug in humans or animals due to its narrow spectrum of activity and potential toxicity. However, it is still used in research settings to study bacterial metabolism and the mechanisms of antibiotic resistance.

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.

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.

DNA glycosylases are a group of enzymes that play a crucial role in the maintenance of genetic material. They are responsible for initiating the base excision repair (BER) pathway, which is one of the major DNA repair mechanisms in cells.

The function of DNA glycosylases is to remove damaged or mismatched bases from DNA molecules. These enzymes recognize and bind to specific types of damaged or incorrect bases, and then cleave the N-glycosidic bond between the base and the deoxyribose sugar in the DNA backbone. This results in the formation of an apurinic/apyrimidinic (AP) site, which is subsequently processed by other enzymes in the BER pathway.

There are several different types of DNA glycosylases that recognize and remove specific types of damaged or incorrect bases. For example, some DNA glycosylases specialize in removing oxidized bases, while others are responsible for removing mismatched bases or those that have been alkylated or methylated.

Overall, the proper functioning of DNA glycosylases is essential for maintaining genomic stability and preventing the accumulation of mutations that can lead to diseases such as cancer.

Sulfites are a group of chemical compounds that contain the sulfite ion (SO3−2), which consists of one sulfur atom and three oxygen atoms. In medical terms, sulfites are often used as food additives or preservatives, serving to prevent bacterial growth and preserve the color of certain foods and drinks.

Sulfites can be found naturally in some foods, such as wine, dried fruits, and vegetables, but they are also added to a variety of processed products like potato chips, beer, and soft drinks. While sulfites are generally considered safe for most people, they can cause adverse reactions in some individuals, particularly those with asthma or a sensitivity to sulfites.

In the medical field, sulfites may also be used as medications to treat certain conditions. For example, they may be used as a vasodilator to widen blood vessels and improve blood flow during heart surgery or as an antimicrobial agent in some eye drops. However, their use as a medication is relatively limited due to the potential for adverse reactions.

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.

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

Tetrahydrouridine (THU) is not a medication itself, but rather a metabolic inhibitor. It is a derivative of the nucleoside uridine and has been studied in the context of its ability to inhibit the enzyme cytidine deaminase. This enzyme is responsible for the breakdown of certain antiviral medications, such as zidovudine (AZT) and stavudine (d4T), which are used in the treatment of HIV infection.

By inhibiting cytidine deaminase, THU can help to increase the levels and effectiveness of these antiviral drugs, while also reducing some of their side effects. However, it is important to note that THU is not currently approved for use as a medication by itself and is typically used in research or experimental settings in combination with other antiretroviral therapies.

Ammonia is a colorless, pungent-smelling gas with the chemical formula NH3. It is a compound of nitrogen and hydrogen and is a basic compound, meaning it has a pH greater than 7. Ammonia is naturally found in the environment and is produced by the breakdown of organic matter, such as animal waste and decomposing plants. In the medical field, ammonia is most commonly discussed in relation to its role in human metabolism and its potential toxicity.

In the body, ammonia is produced as a byproduct of protein metabolism and is typically converted to urea in the liver and excreted in the urine. However, if the liver is not functioning properly or if there is an excess of protein in the diet, ammonia can accumulate in the blood and cause a condition called hyperammonemia. Hyperammonemia can lead to serious neurological symptoms, such as confusion, seizures, and coma, and is treated by lowering the level of ammonia in the blood through medications, dietary changes, and dialysis.

N-Glycosyl hydrolases (or N-glycanases) are a class of enzymes that catalyze the hydrolysis of the glycosidic bond between an N-glycosyl group and an aglycon, which is typically another part of a larger molecule such as a protein or lipid. N-Glycosyl groups refer to carbohydrate moieties attached to an nitrogen atom, usually in the side chain of an amino acid such as asparagine (Asn) in proteins.

N-Glycosyl hydrolases play important roles in various biological processes, including the degradation and processing of glycoproteins, the modification of glycolipids, and the breakdown of complex carbohydrates. These enzymes are widely distributed in nature and have been found in many organisms, from bacteria to humans.

The classification and nomenclature of N-Glycosyl hydrolases are based on the type of glycosidic bond they cleave and the stereochemistry of the reaction they catalyze. They are grouped into different families in the Carbohydrate-Active enZymes (CAZy) database, which provides a comprehensive resource for the study of carbohydrate-active enzymes.

It is worth noting that N-Glycosyl hydrolases can have both beneficial and detrimental effects on human health. For example, they are involved in the normal turnover and degradation of glycoproteins in the body, but they can also contribute to the pathogenesis of certain diseases, such as lysosomal storage disorders, where mutations in N-Glycosyl hydrolases lead to the accumulation of undigested glycoconjugates and cellular damage.

Ethanolamine ammonia-lyase (EAL) is an enzyme that plays a role in the breakdown and metabolism of certain compounds in the body. Its primary function is to catalyze the conversion of ethanolamine, a type of amino alcohol, into acetaldehyde and ammonia. This reaction is an important step in the catabolism of phosphatidylethanolamines, which are major components of cell membranes.

EAL is also known as "ethanolamine deaminase" or "N-ethanolamine deaminase." It requires the cofactor pyridoxal phosphate (PLP) to facilitate the reaction. The enzyme's activity has been identified in various organisms, including bacteria, archaea, and plants, but not in mammals. In some bacterial species, EAL is involved in the biosynthesis of certain amino acids and other biomolecules.

The reaction catalyzed by ethanolamine ammonia-lyase:

Ethanolamine + H2O + PLP → Acetaldehyde + Ammonia + Methylglyoxal + PLP

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.

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.

I'm sorry for any confusion, but "Pentoxyl" doesn't seem to be a recognized term in medical terminology or pharmacology. It's possible that there might be a spelling mistake or it could be a brand name of a drug that is not widely known.

If you meant "Pentoxifylline," however, I can provide a definition. Pentoxifylline is a medication that belongs to a class of drugs known as methylxanthines. It works by improving the flow of blood in the body, particularly in the hands and feet, by decreasing the thickness (viscosity) of the blood. This medication is used to treat conditions such as intermittent claudication (pain in the legs due to poor blood flow) and certain types of Raynaud's phenomenon.

Please make sure that you have the correct spelling when looking for medical information, as it's crucial to have accurate details when researching health-related topics.

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.

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.

Thymine is a pyrimidine nucleobase that is one of the four nucleobases in the nucleic acid double helix of DNA (the other three being adenine, guanine, and cytosine). It is denoted by the letter T in DNA notation and pairs with adenine via two hydrogen bonds. Thymine is not typically found in RNA, where uracil takes its place pairing with adenine. The structure of thymine consists of a six-membered ring (pyrimidine) fused to a five-membered ring containing two nitrogen atoms and a ketone group.

Amino acid oxidoreductases are a class of enzymes that catalyze the reversible oxidation and reduction reactions involving amino acids. They play a crucial role in the metabolism of amino acids by catalyzing the interconversion of L-amino acids to their corresponding α-keto acids, while simultaneously reducing a cofactor such as NAD(P)+ or FAD.

The reaction catalyzed by these enzymes can be represented as follows:

L-amino acid + H2O + Coenzyme (Oxidized) → α-keto acid + NH3 + Coenzyme (Reduced)

Amino acid oxidoreductases are classified into two main types based on their cofactor requirements and reaction mechanisms. The first type uses FAD as a cofactor and is called amino acid flavoprotein oxidoreductases. These enzymes typically catalyze the oxidative deamination of L-amino acids to form α-keto acids, ammonia, and reduced FAD. The second type uses pyridine nucleotides (NAD(P)+) as cofactors and is called amino acid pyridine nucleotide-dependent oxidoreductases. These enzymes catalyze the reversible interconversion of L-amino acids to their corresponding α-keto acids, while simultaneously reducing or oxidizing NAD(P)H/NAD(P)+.

Amino acid oxidoreductases are widely distributed in nature and play important roles in various biological processes, including amino acid catabolism, nitrogen metabolism, and the biosynthesis of various secondary metabolites. Dysregulation of these enzymes has been implicated in several diseases, including neurodegenerative disorders and cancer. Therefore, understanding the structure, function, and regulation of amino acid oxidoreductases is crucial for developing novel therapeutic strategies to treat these diseases.

Alanine Dehydrogenase (ADH) is an enzyme that catalyzes the reversible conversion between alanine and pyruvate with the reduction of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide hydride (NADH). This reaction plays a role in the metabolism of amino acids, particularly in the catabolism of alanine.

In humans, there are multiple isoforms of ADH that are expressed in different tissues and have different functions. The isoform known as ALDH4A1 is primarily responsible for the conversion of alanine to pyruvate in the liver. Deficiencies or mutations in this enzyme can lead to a rare genetic disorder called 4-hydroxybutyric aciduria, which is characterized by elevated levels of 4-hydroxybutyric acid in the urine and neurological symptoms.

Ammonia-lyases are a class of enzymes that catalyze the removal of an amino group from a substrate, releasing ammonia in the process. These enzymes play important roles in various biological pathways, including the biosynthesis and degradation of various metabolites such as amino acids, carbohydrates, and aromatic compounds.

The reaction catalyzed by ammonia-lyases typically involves the conversion of an alkyl or aryl group to a carbon-carbon double bond through the elimination of an amine group. This reaction is often reversible, allowing the enzyme to also catalyze the addition of an amino group to a double bond.

Ammonia-lyases are classified based on the type of substrate they act upon and the mechanism of the reaction they catalyze. Some examples of ammonia-lyases include aspartate ammonia-lyase, which catalyzes the conversion of aspartate to fumarate, and tyrosine ammonia-lyase, which converts tyrosine to p-coumaric acid.

These enzymes are important in both plant and animal metabolism and have potential applications in biotechnology and industrial processes.

DNA cytosine methylases are a type of enzyme that catalyze the transfer of a methyl group (-CH3) to the carbon-5 position of the cytosine ring in DNA, forming 5-methylcytosine. This process is known as DNA methylation and plays an important role in regulating gene expression, genomic imprinting, X-chromosome inactivation, and suppression of transposable elements in eukaryotic organisms.

In mammals, the most well-studied DNA cytosine methylases are members of the DNMT (DNA methyltransferase) family, including DNMT1, DNMT3A, and DNMT3B. DNMT1 is primarily responsible for maintaining existing methylation patterns during DNA replication, while DNMT3A and DNMT3B are involved in establishing new methylation patterns during development and differentiation.

Abnormal DNA methylation patterns have been implicated in various diseases, including cancer, where global hypomethylation and promoter-specific hypermethylation can contribute to genomic instability, chromosomal aberrations, and silencing of tumor suppressor genes.

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.

Leucine dehydrogenase (LDH) is an enzyme that catalyzes the reversible conversion of leucine to α-ketoisocaproate, while simultaneously reducing NAD+ to NADH. It plays a crucial role in the metabolism of branched-chain amino acids and is widely distributed in various tissues such as liver, kidney, heart, skeletal muscle, and brain.

In clinical settings, LDH is often measured in serum or plasma as a biomarker for tissue damage since it is released into the bloodstream upon cell death or injury. Elevated levels of LDH can be observed in various conditions such as myocardial infarction, hemolysis, liver disease, muscle damage, and some types of cancer. However, an isolated increase in LDH may not be specific to a particular condition, and further diagnostic tests are usually required for accurate diagnosis.

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.

Monoamine oxidase inhibitors (MAOIs) are a class of drugs that work by blocking the action of monoamine oxidase, an enzyme found in the brain and other organs of the body. This enzyme is responsible for breaking down certain neurotransmitters, such as serotonin, dopamine, and norepinephrine, which are chemicals that transmit signals in the brain.

By inhibiting the action of monoamine oxidase, MAOIs increase the levels of these neurotransmitters in the brain, which can help to alleviate symptoms of depression and other mood disorders. However, MAOIs also affect other chemicals in the body, including tyramine, a substance found in some foods and beverages, as well as certain medications. As a result, MAOIs can have serious side effects and interactions with other substances, making them a less commonly prescribed class of antidepressants than other types of drugs.

MAOIs are typically used as a last resort when other treatments for depression have failed, due to their potential for dangerous interactions and side effects. They require careful monitoring and dosage adjustment by a healthcare provider, and patients must follow strict dietary restrictions while taking them.

Deoxyuridine is a chemical compound that is a component of DNA. It is a nucleoside, which means it consists of a sugar (deoxyribose) linked to a nitrogenous base (uracil). In the case of deoxyuridine, the uracil is not methylated, which differentiates it from thymidine.

Deoxyuridine can be converted into deoxyuridine monophosphate (dUMP) by the enzyme thymidine kinase. The dUMP can then be converted into deoxythymidine triphosphate (dTTP), which is a building block of DNA, through a series of reactions involving other enzymes.

Deoxyuridine has been used in research and medicine as a marker for DNA synthesis and repair. It can also be used to inhibit the growth of certain types of cells, such as cancer cells, by disrupting their DNA synthesis.

Immunoglobulin class switching, also known as isotype switching or class switch recombination (CSR), is a biological process that occurs in B lymphocytes as part of the adaptive immune response. This mechanism allows a mature B cell to change the type of antibody it produces from one class to another (e.g., from IgM to IgG, IgA, or IgE) while keeping the same antigen-binding specificity.

During immunoglobulin class switching, the constant region genes of the heavy chain undergo a DNA recombination event, which results in the deletion of the original constant region exons and the addition of new constant region exons downstream. This switch allows the B cell to express different effector functions through the production of antibodies with distinct constant regions, tailoring the immune response to eliminate pathogens more effectively. The process is regulated by various cytokines and signals from T cells and is critical for mounting an effective humoral immune response.

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

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

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

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.

... of guanine results in the formation of xanthine. Xanthine, however, still pairs with cytosine. Deamination of ... this spontaneous deamination is corrected for by the removal of uracil (product of cytosine deamination and not part of DNA) by ... Deamination is the removal of an amino group from a molecule. Enzymes that catalyse this reaction are called deaminases. In the ... Spontaneous deamination is the hydrolysis reaction of cytosine into uracil, releasing ammonia in the process. This can occur in ...
... is a form of deamination that generates α-keto acids and other oxidized products from amine-containing ... Another enzyme responsible for oxidative deamination is monoamine oxidase, which catalyzes the deamination of monoamines via ... Oxidative deamination is an important step in the catabolism of amino acids, generating a more metabolizable form of the amino ... Oxidative deamination is stereospecific, meaning it contains different stereoisomers as reactants and products; this process is ...
Oxidative deamination is the first step to breaking down the amino acids so that they can be converted to sugars. The process ... "Oxidative Deamination". chemistry.elmhurst.edu. Retrieved 2016-10-25. "GLYCOLYSIS AND THE KREBS CYCLE". homepage.smc.edu. ... Transamination leads to the same result as deamination: the remaining acid will undergo either glycolysis or the TCA cycle to ... Among the several degrading processes for amino acids are Deamination (removal of an amino group), transamination (transfer of ...
A Stereospecific Deamination". Journal of the American Chemical Society. 88 (6): 1335-1336. doi:10.1021/ja00958a056. ISSN 0002- ...
METZLER DE, SNELL EE (1952). "Deamination of serine. II. D-Serine dehydrase, a vitamin B6 enzyme from Escherichia coli". J. ...
The predicted deamination reaction is driven by a direct nucleophilic attack on position 4 of the cytidine pyrimidine ring by ... The deamination activity ultimately results in G→A hypermutations at "hot spots" of the proviral DNA. Such hypermutation ... Water is needed as a source of both a proton and hydroxyl group donor (Figure 2). The deamination (and resulting oxidation) at ... APOBEC3G belongs to the family of cytidine deaminases that catalyze the deamination of cytidine to uridine in the single ...
There is no deamination step. Instead, the demethylation of the N-methyl group on sarcosine occurs directly. The reduced FADH− ...
ISBN 978-1-4292-7635-1. Umbarger HE, Brown B (January 1957). "Threonine deamination in Escherichia coli. II. Evidence for two L ... the threonine deamination capabilities of the enzyme go unchecked. This degrades threonine before the herbivore can absorb it, ...
2. Substitutive deamination of arylamines by alkyl nitrites and copper(II) halides. A direct and remarkably efficient ... M. P. Doyle, B. Siegfried and J. F. Dellaria (1977). "Alkyl nitrite-metal halide deamination reactions. ...
ITP results from deamination of ATP. Incorporation of ITP into the DNA from the nucleotide pool can lead to DNA damage, ...
Deamination of Guanine is not mutagenic. Nitrous acid-induced mutations also are induced to mutate back to wild-type using ... It can cause deamination of the amino groups of Adenine, Guanine and Cytosine. Adenine is deaminated to hypoxanthine, which ... not used as xanthine is a deamination product) However, correct DNA structure can form even when the bases are not paired via ...
Umbarger, H. E.; Brown, B. (1957). "Threonine deamination in Escherichia coli II. Evidence for two L-threonine deaminases". ...
Xanthine formed from deamination of guanine. (Thymidine products following deamination of 5-methylcytosine are more difficult ... Jayanta Chaudhuri & Frederick W. Alt (2004). "Class-switch recombination: interplay of transcription, DNA deamination and DNA ... the most common ones being deamination, oxidation, and alkylation. These modifications can affect the ability of the base to ... Uracil inappropriately incorporated in DNA or formed by deamination of cytosine In addition to base lesions, the downstream ...
Ammonia poisoning Deamination Chris M. Wood; R.S. Munger; D.P. Toews (1989). "Ammonia, urea, and H+ distribution and the ...
I. The enzymatic deamination of deoxycytidine 5'-phosphate and of 5-methyldeoxycytidine 5-methyldeoxycytidine 5'-phosphate". ... Scarano E, Bonaduce L (December 1960). "The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides. II. Purification ... Deoxycytidine monophosphate Deoxyuridine monophosphate Scarano E (March 1960). "The enzymatic deamination of 6-aminopyrimidine ...
Similarly, deamination of cytosine results in uracil. Example of comparing and determining the % difference between two ... both of them through deamination (replacement of the amine-group with a carbonyl-group). Hypoxanthine is produced from adenine ...
Mulder, L. C. F.; Harari, A.; Simon, V. (2008-04-07). "Cytidine deamination induced HIV-1 drug resistance". Proceedings of the ...
Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (Jun 2003). "DNA deamination ... Goff SP (Aug 2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281-3. doi:10.1016/S0092- ... Harris RS, Sheehy AM, Craig HM, Malim MH, Neuberger MS (Jul 2003). "DNA deamination: not just a trigger for antibody ...
Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (Jun 2003). "DNA deamination ... Goff SP (Aug 2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281-3. doi:10.1016/S0092- ... Harris RS, Sheehy AM, Craig HM, Malim MH, Neuberger MS (Jul 2003). "DNA deamination: not just a trigger for antibody ...
Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (Jun 2003). "DNA deamination ... Goff SP (Aug 2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281-3. doi:10.1016/S0092- ...
Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (Jun 2003). "DNA deamination ... Harris RS, Sheehy AM, Craig HM, Malim MH, Neuberger MS (Jul 2003). "DNA deamination: not just a trigger for antibody ... "Entrez Gene: PSME4 proteasome (prosome, macropain) activator subunit 4". Goff SP (Aug 2003). "Death by deamination: a novel ...
A1's deamination of the cytosine base yields uracil, which creates a stop codon in the mRNA. A1 has been linked with both ... Hydrolytic deamination of the cytosine amine group then occurs, catalyzed by the proton transfer from the nearby glutamic acid ... A1 modifies the cytosine base at position 6666 on the ApoB mRNA strand through a deamination. An A1 dimer first binds to ACF, ... The antiviral properties of A1 extend to both DNA and RNA due to its deamination function, which can hinder DNA replication and ...
Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (Jun 2003). "DNA deamination ... Goff SP (Aug 2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281-3. doi:10.1016/S0092- ...
Garrick NA, Murphy DL (1980). "Species differences in the deamination of dopamine and other substrates for monoamine oxidase in ... Monoamine oxidases catalyze the oxidative deamination of monoamines. In the first part of reaction, cofactor FAD oxidase ...
Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (2003). "DNA deamination mediates ... Goff SP (2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281-3. doi:10.1016/S0092-8674 ... Harris RS, Sheehy AM, Craig HM, Malim MH, Neuberger MS (2003). "DNA deamination: not just a trigger for antibody ...
Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (June 2003). "DNA deamination ... Harris RS, Sheehy AM, Craig HM, Malim MH, Neuberger MS (July 2003). "DNA deamination: not just a trigger for antibody ... "Enhancing the Catalytic Deamination Activity of APOBEC3C Is Insufficient to Inhibit Vif-Deficient HIV-1". Journal of Molecular ... "Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome". Nature Structural & Molecular ...
Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (Jun 2003). "DNA deamination ... Goff SP (Aug 2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281-3. doi:10.1016/S0092- ... Harris RS, Sheehy AM, Craig HM, Malim MH, Neuberger MS (Jul 2003). "DNA deamination: not just a trigger for antibody ...
The initial step is deamination via an aminotransferase. The second step is catalyzed by a nonribosomal peptide synthetase-like ... 4-HPP is produced from a deamination via an aminotransferase. The genetic basis of these two genes is clustered (i.e., adjacent ...
Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (2003). "DNA deamination mediates ... Goff SP (2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281-3. doi:10.1016/S0092-8674 ...
G deamination gradients. DNA becomes susceptible to deamination events when it is single stranded. When replication forks form ... the strand not being copied is single stranded, and thus at risk for A → G deamination. Therefore, gradients in deamination ... Deamination occurs when an amino group is lost and is a mutation that often results in base changes. When adenine is deaminated ... In addition to the early microscopy experiments, this model is also supported by the amounts of deamination seen in cpDNA. ...
Deamination of guanine results in the formation of xanthine. Xanthine, however, still pairs with cytosine. Deamination of ... this spontaneous deamination is corrected for by the removal of uracil (product of cytosine deamination and not part of DNA) by ... Deamination is the removal of an amino group from a molecule. Enzymes that catalyse this reaction are called deaminases. In the ... Spontaneous deamination is the hydrolysis reaction of cytosine into uracil, releasing ammonia in the process. This can occur in ...
Inhibition of recombinant human DAAO assessed as oxidative deamination of D-serine in presence of molecular oxygen and FAD ...
Deamination is rapidly followed by excision of uracil residues and can lead to double-stranded breaks. It is not known to which ...
Cytosine Deamination Repair. What are the Most Important Types of DNA Repair?. Leave a Comment / Biochemistry, Biochemistry II ...
... deamination definition,what does iridology reveal  iridology pictures and meanings ... ... Heim / BLOG / Bilder und Bedeutungen der Iridologie,deamination definition,what does iridology reveal ...
Evidence for deamination by glutamate dehydrogenase in higher plants: Commentary Fox GG., Ratcliffe RG., Robinson SA., Stewart ...
Structural basis of sequence-specific cytosine deamination by double-stranded DNA deaminase toxin DddA.. Publication Type:. ... Home » Structural basis of sequence-specific cytosine deamination by double-stranded DNA deaminase toxin DddA. ...
Deamination * Electrophoresis, Gel, Two-Dimensional * Humans * Lens, Crystalline / chemistry* * Light * Molecular Chaperones / ...
Insertion, deletion, substitution, deamination, methylation, demethylation.. Note 1 to entry: Genome editing components can ...
d-Amino acidity oxidase (DAAO) catalyzes the oxidative deamination of d-amino acids. d-Amino acidity oxidase (DAAO) catalyzes ... the oxidative deamination of d-amino acids including d-serine, a complete agonist on the glycine modulatory site from the (gene ...
Deamination of cytosine to uracil. Yes. Nicks and gaps. Yes. Oxidized bases. Yes. ...
what highly toxic byproduct is produced as a result of deamination of aa during protein catabolism?. ... What remains after deamination of aa in protein catabolism is converted to. ...
The suisse of the ischaemia sweepings, deamination of the where c compare phentermine prices; the sars badge of the drug ...
THE EFFECTS OF RING-METHYOXYL GROUPS ON BIOLOGICAL DEAMINATION OF PHEN... J Med Chem. 1965. ...
APOBEC3B interacts with R-loops and helps mediate their resolution in a deamination-dependent way. This association also ...
Regions of Slow C-to-T Deamination. The majority of CpG islands are normally unmethylated and undergo slow C-to-T deamination. ... CpG stability in these elements can be explained by the neutral effect of slow deamination alone, that goes with the lack of ...
Scheme 15. (A) SmI2-Promoted Reductive Deamination of α-Amino Esters and Ketones; (B) Synthesis of Chiral Piperidines by ... Scheme 15. (A) SmI2-Promoted Reductive Deamination of α-Amino Esters and Ketones; (B) Synthesis of Chiral Piperidines by ... Honda, T.; Ishikawa, F. Reductive deamination of α-amino carbonyl compounds by means of samarium iodide. Chem. Commun. 1999, 12 ... Although simple phenylalanine derivatives undergo efficient deamination, the synthetic value of this method hinges upon the use ...
Azacitidine undergoes spontaneous hydrolysis and deamination mediated by cytidine deaminase.. Excretion Following the ...
Two-phase anaerobic fermentation pre-deamination system device and method CN107697969A (en) 2018-02-16. A kind of system and ... Two-phase anaerobic fermentation pre-deamination system device CN106277685A (en) 2017-01-04. A kind of sludge treating system ...
The deamination pathway was mainly inhibited by CYP3A inhibitors, including troleandomycin and azole antifungals. Dihydrodiol ... N-demethylation is primarily mediated by CYP2C9, CYP2C8, and CYP1A2; dihydrodiol formation by CYP2C9 and CYP1A2; deamination by ... deamination, 3) alkyl side chain oxidation, and 4) dihydrodiol formation. Michaelis-Menten kinetics for the pathways revealed ...
S: (v) deaminate, deaminize (remove the amino radical (usually by hydrolysis) from an amino compound; to perform deamination) ...
TRANSDEAMINATION AND DEAMINATION por Minhaz Ahmed. TRANSDEAMINATION AND DEAMINATION. Minhaz Ahmed•106.9K. vistas ...
Catalyzing Deamination and Dechlorination." Journal of Bacteriology 189.19 (2007): 6989-. 6997. (co-authored with J. L. ...
The sequences all harbored signs of cytosine deamination, which is common among ancient samples. ...
Zemojtel, T.; Kielbasa, S. M.; Arndt, P. F.; Behrens, S.; Bourque, G.; Vingron, M.: CpG deamination creates transcription ...
Alanine deamination increases glutamine, which promotes ammonia generation; pyruvate escalates gluconeogenesis. The collective ... and deamination of adenosine monophosphate (AMP) for energy. Treatment with valproic acid, an antiepileptic drug, can inhibit ...
Herpesviral Pseudo-enzymes Induce RIG-I Deamination and Ligand-independent Activation. 2015 Mol Cell 58:134. ...
MAO-A (monoamine oxidase-A) is a flavin enzyme which catalyzes the oxidative deamination of serotonin to produce 5- ... It catalyzes the oxidative deamination of serotonin to produce hydrogen peroxide and metabolized products. In the CNS, the ...
A positive phenylalanine deamination reaction is indicated by the development of a light to dark green color (PDA) or purple to ... What does a positive phenylalanine deamination test mean?. What does a positive test result mean in the Phenylalanine deaminase ... What does a positive phenylalanine deamination test mean?. *Which are the only Enterobacteriaceae that are phenylalanine ...
  • In DNA, this spontaneous deamination is corrected for by the removal of uracil (product of cytosine deamination and not part of DNA) by uracil-DNA glycosylase, generating an abasic (AP) site. (wikipedia.org)
  • Structural basis of sequence-specific cytosine deamination by double-stranded DNA deaminase toxin DddA. (anl.gov)
  • I propose an explanation of these cytosine deamination. (cdc.gov)
  • The sequences all harbored signs of cytosine deamination, which is common among ancient samples. (genomeweb.com)
  • Active demethylation in mouse zygotes involves cytosine deamination and base excision repair. (uni-muenchen.de)
  • Cytosine deamination and base excision repair cause R-loop-induced CAG repeat fragility and instability in Saccharomyces cerevisiae . (bvsalud.org)
  • The enzyme catalyses a two-step reaction - an oxidative deamination, followed by cyclization. (genome.jp)
  • An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. (curehunter.com)
  • Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity. (umassmed.edu)
  • Spontaneous deamination is the hydrolysis reaction of cytosine into uracil, releasing ammonia in the process. (wikipedia.org)
  • Deamination is rapidly followed by excision of uracil residues and can lead to double-stranded breaks. (pasteur.fr)
  • Excises uracil residues from the DNA which can arise as a result of misincorporation of dump residues by DNA polymerase or due to deamination of cytosine. (lu.se)
  • A positive phenylalanine deamination reaction is indicated by the development of a light to dark green color (PDA) or purple to black color (TDA) within 1 to 5 min after applying ferric chloride reagent. (bigsurspiritgarden.com)
  • What does a positive phenylalanine deamination test mean? (bigsurspiritgarden.com)
  • Phenylalanine is first converted to cinnamic acid by deamination. (kegg.jp)
  • The terbinafine metabolites represented four major pathways: 1) N- demethylation, 2) deamination, 3) alkyl side chain oxidation, and 4) dihydrodiol formation. (aspetjournals.org)
  • Thymine DNA Glycosylase Is Essential for Active DNA Demethylation by Linked Deamination-Base Excision Repair. (uni-muenchen.de)
  • However, treating DNA with bisulfite prior to sequencing leads to deamination of cytosine, but leaves the modified cytosine residues unchanged. (helsinki.fi)
  • In situations of excess protein intake, deamination is used to break down amino acids for energy. (wikipedia.org)
  • what highly toxic byproduct is produced as a result of deamination of aa during protein catabolism? (flashcardmachine.com)
  • Ammonia is toxic to the human system, and enzymes convert it to urea or uric acid by addition of carbon dioxide molecules (which is not considered a deamination process) in the urea cycle, which also takes place in the liver. (wikipedia.org)
  • Spontaneous deamination of 5-methylcytosine results in thymine and ammonia. (wikipedia.org)
  • CpG stability in these elements can be explained by the neutral effect of slow deamination alone, that goes with the lack of methylation, with no evidence of selection on CpG densities going on. (epigenie.com)
  • CIBA-Geigy) inhibited MAO, but had less effect on the deamination of PE than on 5-HT or DA. (erowid.org)
  • Deamination is the removal of an amino group from a molecule. (wikipedia.org)
  • A known result of cytosine methylation is the increase of C-to-T transition mutations through the process of deamination. (wikipedia.org)
  • Deamination of guanine results in the formation of xanthine. (wikipedia.org)
  • Deamination of adenine results in the formation of hypoxanthine. (wikipedia.org)
  • Note that the left tube contents exhibited a greenish coloration, indicating the enzymatic deamination of the phenylalanine contained within, converting it to phenylpyruvic acid. (cdc.gov)
  • DNA adducts of propylene oxide and acrylonitrile epoxide: hydrolytic deamination of 3-alkyl-dCyd to 3-alkyl-dUrd. (nih.gov)
  • 3-HP-dUrd was formed after initial alkylation at N-3 of dCyd followed by conversion of the adjacent exocyclic imino group at C-4 to an oxygen (hydrolytic deamination) with the formation of a dUrd adduct. (nih.gov)
  • As with 3-HP-dUrd, 3-HOCE-dUrd resulted from hydrolytic deamination of an initially formed dCyd adduct. (nih.gov)
  • Adenosine deaminases that act on RNA (ADARs) * are a family of RNA-editing enzymes that catalyze the hydrolytic deamination of adenosines to inosines in a diverse group of mostly double-stranded RNA substrates. (rupress.org)
  • A known result of cytosine methylation is the increase of C-to-T transition mutations through the process of deamination. (wikipedia.org)
  • Methylation and deamination of CpGs generate p53-binding sites on a genomic scale. (mpg.de)
  • Cytosine residues in CpG dinucleotides often undergo various types of modification, such as methylation, deamination, and halogenation. (biomedcentral.com)
  • Adenosine residues in RNA are most targeted for modification and can undergo for example, methylation or deamination. (helsinki.fi)
  • Thyroid hormones can be metabolized in peripheral tissue by deiodination, conjugation, deamination, and decarboxylation enzyme reactions. (nih.gov)
  • Figure 3: Arginine Decarboxylation and Deamination Arginine decarboxylation requires a combination of decarboxylase and dihydrolase to achieve the complete decarboxylation of arginine to putrescine. (asm.org)
  • 25. Allosteric regulation of glutamate dehydrogenase deamination activity. (nih.gov)
  • In situations of excess protein intake, deamination is used to break down amino acids for energy. (wikipedia.org)
  • Urea is synthesized in the liver from ammonia, as a result of deamination of amino acids. (randox.com)
  • Spontaneous deamination is the hydrolysis reaction of cytosine into uracil, releasing ammonia in the process. (wikipedia.org)
  • Spontaneous deamination of 5-methylcytosine results in thymine and ammonia. (wikipedia.org)
  • Mutations are correlated over a 15 nt distance in multiply mutated clones, suggesting that deaminations are catalyzed processively within a stalled or backtracked transcription bubble. (nih.gov)
  • Mutations can be induced by environmental factors but also arise spontaneously during DNA replication or due to deamination of methylated cytosines at CpG dinucleotides. (muni.cz)
  • Ammonia is toxic to the human system, and enzymes convert it to urea or uric acid by addition of carbon dioxide molecules (which is not considered a deamination process) in the urea cycle, which also takes place in the liver. (wikipedia.org)
  • Be able to explain why ammonia must be converted to urea (deamination) for excretion. (docbrown.info)
  • The transcription elongation complex directs activation-induced cytidine deaminase-mediated DNA deamination (angol nyelven), 2006. (wikipedia.org)
  • APOBEC3 proteins are incorporated into virus particles and interfere with viral replication complexes by editing cDNA via cytidine deamination and suppressing reverse transcription. (kcl.ac.uk)
  • Correlation between cytidine deaminase genotype and gemcitabine deamination in blood samples. (cdc.gov)
  • The products of deamination of amines (3) and (4) were similar but not identical and included large amounts of hydrocarbon and products derived from carbon migration. (stir.ac.uk)
  • Here, we reconstitute AID-catalyzed deamination during Pol II transcription elongation in conjunction with DSIF transcription factor. (nih.gov)
  • Title: Deamination and related reactions of some bicyclo-octylamines Author(s): Wilson, Alan A Abstract: The bicyclo-octylamines (1-5) have been deaminated by the nitrous acid method and by the decomposition of their nitrosocarbamates in ethanol. (stir.ac.uk)
  • Deamination is a means of amino acid degradation that predominantly occurs in the liver. (gpnotebook.com)
  • AID-RNA polymerase II transcription-dependent deamination of IgV DNA. (nih.gov)
  • CpG deamination creates transcription factor-binding sites with high efficiency. (mpg.de)
  • selection of hypermutable (mutator) increased risk for deamination [email protected] alleles based on alterations in DNA because of the production of reactive repair genes. (cdc.gov)
  • NOseq: amplicon sequencing evaluation method for RNA m6A sites after chemical deamination. (unil.ch)
  • The base excision repair (BER) pathway corrects most endogenous base lesions, including alkylation, oxidation and deamination, apurinic/apyrimidinic (AP) sites as well as single-strand breaks. (springer.com)
  • Site-by-site comparisons for biochemical and human memory B-cell mutational spectra in an IGHV3-23*01 target show strongly favored deaminations occurring in the antigen-binding complementarity determining regions (CDR) compared to the framework regions (FW). (nih.gov)