An enzyme that catalyzes the deamination of AMP to IMP. EC 3.5.4.6.
Catalyze the hydrolysis of nucleotides with the elimination of ammonia.
An enzyme that catalyzes the hydrolysis of ADENOSINE to INOSINE with the elimination of AMMONIA.
Inosine 5'-Monophosphate. A purine nucleotide which has hypoxanthine as the base and one phosphate group esterified to the sugar moiety.
Drugs that inhibit ADENOSINE DEAMINASE activity.
An enzyme that catalyzes the deamination of cytidine, forming uridine. EC 3.5.4.5.
A ribonucleoside antibiotic synergist and adenosine deaminase inhibitor isolated from Nocardia interforma and Streptomyces kaniharaensis. It is proposed as an antineoplastic synergist and immunosuppressant.
Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position.
An enzyme which catalyzes the deamination of CYTOSINE resulting in the formation of URACIL. It can also act on 5-methylcytosine to form THYMIDINE.
An enzyme that catalyzes the hydrolytic deamination of deoxycytidylic acid to deoxyuridylic acid and ammonia. It plays an important role in the regulation of the pool of deoxynucleotides in higher organisms. The enzyme also acts on some 5-substituted deoxycytidylic acids. EC 3.5.4.12.
Catalyze the hydrolysis of nucleosides with the elimination of ammonia.
An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.
An enzyme that catalyzes the deamination of guanine to form xanthine. EC 3.5.4.3.
Adenine nucleotides are molecules that consist of an adenine base attached to a ribose sugar and one, two, or three phosphate groups, including adenosine monophosphate (AMP), adenosine diphosphate (ADP), and adenosine triphosphate (ATP), which play crucial roles in energy transfer and signaling processes within cells.
Nucleosides in which the purine or pyrimidine base is combined with ribose. (Dorland, 28th ed)
The rate dynamics in chemical or physical systems.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
Inorganic salts of phosphoric acid.
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)
A glycoprotein enzyme present in various organs and in many cells. The enzyme catalyzes the hydrolysis of a 5'-ribonucleotide to a ribonucleoside and orthophosphate in the presence of water. It is cation-dependent and exists in a membrane-bound and soluble form. EC 3.1.3.5.
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.
Contractile tissue that produces movement in animals.
An enzyme that catalyzes the tetrapolymerization of the monopyrrole PORPHOBILINOGEN into the hydroxymethylbilane preuroporphyrinogen (UROPORPHYRINOGENS) in several discrete steps. It is the third enzyme in the 8-enzyme biosynthetic pathway of HEME. In humans, deficiency in this enzyme encoded by HMBS (or PBGD) gene results in a form of neurological porphyria (PORPHYRIA, ACUTE INTERMITTENT). This enzyme was formerly listed as EC 4.3.1.8
Purines attached to a RIBOSE and a phosphate that can polymerize to form DNA and RNA.
A purine and a reaction intermediate in the metabolism of adenosine and in the formation of nucleic acids by the salvage pathway.

Regulation of AMP deaminase from chicken erythrocytes. A kinetic study of the allosteric interactions. (1/194)

The allosteric properties of AMP deaminase [EC 3.5.4.6] from chicken erythrocytes have been qualitatively and quantitatively accounted for by the concerted transition theory of Monod et al., on the assumption that this enzyme has different numbers of binding sites for each ligand. Theoretical curves yield a satisfactory fit for all experimental saturation functions with respect to activation by alkali metals and inhibition by Pi, assuming that the numbers of binding sites for AMP, alkali metals, and Pi are 4, 2, and 4, respectively. The enzyme was inhibited by concentrations of ATP and GTP below 0.1 and 0.25 mM, respectively, whereas activation of the enzyme was observed at ATP and GTP concentrations above 0.4 and 1.5 mM, respectively. These unusual kinetics with respect to ATP and GTP could be also accounted for by assuming 2 inhibitory and 4 activating sites for each ligand.  (+info)

Regulation of chicken erythrocyte AMP deaminase by phytic acid. (2/194)

AMP deaminase [EC 3.5.6.4] purified from chicken erythrocytes was inhibited by phytic acid (inositol hexaphosphate), which is the principal organic phosphate in chicken red cells. Kinetic analysis has indicated that this inhibition is of an allosteric type. The estimated Ki value was within the normal range of phytic acid concentration, suggesting that this compound acts as a physiological effector. Divalent cations such as Ca2+ and Mg2+ were shown to affect AMP deaminase by potentiating inhibition by lower concentrations of phytic acid, and by relieving the inhibition at higher concentrations of phytic acid. These results suggests that Ca2+ and Mg2+ can modify the inhibition of AMP deaminase by phytic acid in chicken red cells.  (+info)

Common variant in AMPD1 gene predicts improved clinical outcome in patients with heart failure. (3/194)

BACKGROUND: This study was undertaken to identify gene(s) that may be associated with improved clinical outcome in patients with congestive heart failure (CHF). The adenosine monophosphate deaminase locus (AMPD1) was selected for study. We hypothesized that inheritance of the mutant AMPD1 allele is associated with increased probability of survival without cardiac transplantation in patients with CHF. METHODS AND RESULTS: AMPD1 genotype was determined in 132 patients with advanced CHF and 91 control reference subjects by use of a polymerase chain reaction-based, allele-specific oligonucleotide detection assay. In patients with CHF, those heterozygous (n=20) or homozygous (n=1) for the mutant AMPD1 allele (AMPD1 +/- or -/-, respectively) experienced a significantly longer duration of heart failure symptoms before referral for transplantation evaluation than CHF patients homozygous for the wild-type allele (AMPD1 +/+; n=111; 7.6+/-6.5 versus 3.2+/-3.6 years; P<0.001). The OR of surviving without cardiac transplantation >/=5 years after initial hospitalization for CHF symptoms was 8.6 times greater (95% CI: 3.05, 23.87) in those patients carrying >/=1 mutant AMPD1 allele than in those carrying 2 wild-type AMPD1 +/+ alleles. CONCLUSIONS: After the onset of CHF symptoms, the mutant AMPD1 allele is associated with prolonged probability of survival without cardiac transplantation. The mechanism by which the presence of the mutant AMPD1 allele may modify the clinical phenotype of heart failure remains to be determined.  (+info)

AMP deaminase in piglet cardiac myocytes: effect on nucleotide metabolism during ischemia. (4/194)

The purpose of this study was to examine in situ regulation of AMP deaminase in newborn piglet cardiac myocytes and to determine its role in nucleotide metabolism during ischemia. When a rapid deenergization paradigm was used to assay AMP deaminase, enzyme activity depended on the hormonal and metabolic status of cells just before deenergization. Inosine 5'-monophosphate (IMP) formation was increased 150% in deenergized myocytes pretreated with phorbol 12-myristate 13-acetate (PMA; EC50 = 4.7 x 10(-8) M). This effect was 90% blocked with the protein kinase C (PKC) inhibitor staurosporine. In addition, the beta-adrenergic agonist isoproterenol stimulated AMP deaminase activity (EC50 = 1.5 x 10(-8) M), and IMP formation was directly correlated to intracellular cAMP levels (r2 = 0.9). Furthermore, adenosine increased IMP formation, whereas nonrespiring, glycolyzing piglet myocytes had reduced AMP deaminase activity. Pretreatment of perfused piglet hearts with adenosine, but not PMA, before exposure to global ischemia resulted in enhanced conversion of AMP to IMP during the ischemic period. Similar results were obtained in piglet myocytes preincubated with adenosine or PMA before exposure to simulated ischemia. These results may be relevant to the preconditioning phenomenon.  (+info)

5'-Nucleotidase as a marker of both general and local inflammation in rheumatoid arthritis patients. (5/194)

OBJECTIVES: To evaluate measurements of serum and synovial fluid 5'-nucleotidase (5'N) activity as a marker of general and local inflammation in arthritis, and to resolve a contradiction in the literature as to whether or not the activity of 5'N in the synovial fluids of rheumatoid arthritis (RA) patients is raised in comparison with that in the synovial fluids of other arthritis patients. METHODS: Assays for 5'N were carried out in the presence of inhibitors of other phosphatases, AMP deaminase and of 5'N itself. RESULTS: The 5'N activity in the synovial fluid of RA patients was both significantly higher (mean 1.7-fold) and had a greater variance than that in the synovial fluids of other arthritis patients, and the contradiction in the literature was resolved. There was a strong correlation between the 5'N activity in the sera of RA patients and their erythrocyte sedimentation rate. There was no significant correlation between the 5'N in the serum and synovial fluid for the RA patients, in marked contrast to the strong correlation between the two 5'N activities shown by the osteoarthritis patients. The 5'N activity was greater in the synovial fluid than in the serum for virtually all the patients, showing that it was being made locally. CONCLUSIONS: The 5'N activity in the serum (which came mostly from the liver) could be used as a marker of general inflammation, whereas the 5'N in the synovial fluid was mostly produced locally, and could be used as a marker of joint inflammation, particularly for the RA patients.  (+info)

Regulation of AMP deaminase by phosphoinositides. (6/194)

AMP deaminase (AMPD) converts AMP to IMP and is a diverse and highly regulated enzyme that is a key component of the adenylate catabolic pathway. In this report, we identify the high affinity interaction between AMPD and phosphoinositides as a mechanism for regulation of this enzyme. We demonstrate that endogenous rat brain AMPD and the human AMPD3 recombinant enzymes specifically bind inositide-based affinity probes and to mixed lipid micelles that contain phosphatidylinositol 4,5-bisphosphate. Moreover, we show that phosphoinositides specifically inhibit AMPD catalytic activity. Phosphatidylinositol 4,5-bisphosphate is the most potent inhibitor, effecting pure noncompetitive inhibition of the wild type human AMPD3 recombinant enzyme with a K(i) of 110 nM. AMPD activity can be released from membrane fractions by in vitro treatment with neomycin, a phosphoinositide-binding drug. In addition, in vivo modulation of phosphoinositide levels leads to a change in the soluble and membrane-associated pools of AMPD activity. The predicted human AMPD3 sequence contains pleckstrin homology domains and (R/K)X(n)(R/K)XKK sequences, both of which are characterized phosphoinositide-binding motifs. The interaction between AMPD and phosphoinositides may mediate membrane localization of the enzyme and function to modulate catalytic activity in vivo.  (+info)

Energy metabolism and lipid peroxidation of human erythrocytes as a function of increased oxidative stress. (7/194)

To study the influence of oxidative stress on energy metabolism and lipid peroxidation in erythrocytes, cells were incubated with increasing concentrations (0.5-10 mM) of hydrogen peroxide for 1 h at 37 degrees C and the main substances of energy metabolism (ATP, AMP, GTP and IMP) and one index of lipid peroxidation (malondialdehyde) were determined by HPLC on cell extracts. Using the same incubation conditions, the activity of AMP-deaminase was also determined. Under nonhaemolysing conditions (at up to 4 mM H2O2), oxidative stress produced, starting from 1 mM H2O2, progressive ATP depletion and a net decrease in the intracellular sum of adenine nucleotides (ATP + ADP + AMP), which were not paralleled by AMP formation. Concomitantly, the IMP level increased by up to 20-fold with respect to the value determined in control erythrocytes, when cells were challenged with the highest nonhaemolysing H2O2 concentration (4 mM). Efflux of inosine, hypoxanthine, xanthine and uric acid towards the extracellular medium was observed. The metabolic imbalance of erythrocytes following oxidative stress was due to a dramatic and unexpected activation of AMP-deaminase (a twofold increase of activity with respect to controls) that was already evident at the lowest dose of H2O2 used; this enzymatic activity increased with increasing H2O2 in the medium, and reached its maximum at 4 mM H2O2-treated erythrocytes (10-fold higher activity than controls). Generation of malondialdehyde was strictly related to the dose of H2O2, being detectable at the lowest H2O2 concentration and increasing without appreciable haemolysis up to 4 mM H2O2. Besides demonstrating a close relationship between lipid peroxidation and haemolysis, these data suggest that glycolytic enzymes are moderately affected by oxygen radical action and strongly indicate, in the change of AMP-deaminase activity, a highly sensitive enzymatic site responsible for a profound modification of erythrocyte energy metabolism during oxidative stress.  (+info)

IMP and AMP deaminase in reperfusion injury down-regulates neutrophil recruitment. (8/194)

We examined gene regulation in murine lungs after hind-limb vessel occlusion and reperfusion. A rapid increase of transcript for the AMP deaminase 3 gene (AMPD3) and its enzymatic activity (EC) generating inosine monophosphate (IMP) were identified with transcripts located in bronchial and alveolar epithelium. AMP deaminase inhibitor decreased IMP levels and significantly enhanced neutrophil recruitment within lung tissue during reperfusion. In addition, IMP inhibited cytokine-initiated neutrophil infiltration in vivo and selectively attenuated neutrophil rolling by 90% in microvessels. We prepared labeled IMP and demonstrated that IMP specifically binds to neutrophils. IMP also stimulated binding of gamma-[(35)S]thio-GTP, suggesting that IMP is a potent regulator of neutrophils. Taken together, these results elucidate a previously unrecognized mechanism that protects tissues from the potentially deleterious consequences of aberrant neutrophil accumulation. Moreover, they are relevant for new therapeutic approaches to regulate neutrophil responses in inflammation and vascular disease.  (+info)

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.

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.

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.

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

Adenosine 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.

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.

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.

Adenosine monophosphate (AMP) is a nucleotide that is the monophosphate ester of adenosine, consisting of the nitrogenous base adenine attached to the 1' carbon atom of ribose via a β-N9-glycosidic bond, which in turn is esterified to a phosphate group. It is an important molecule in biological systems as it plays a key role in cellular energy transfer and storage, serving as a precursor to other nucleotides such as ADP and ATP. AMP is also involved in various signaling pathways and can act as a neurotransmitter in the central nervous system.

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.

DCMP deaminase is an enzyme that catalyzes the deamination of deoxycytidine monophosphate (dCMP) to deoxyuridine monophosphate (dUMP). This reaction is a part of the pyrimidine nucleotide biosynthesis pathway. The enzyme's systematic name is "deoxycytidine monophosphate deaminase." It plays a crucial role in DNA synthesis and maintenance by providing the necessary precursor (dUMP) for thymidylate synthesis, which is essential for the production of thymidine triphosphate (dTTP), one of the four building blocks of DNA.

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.

Cyclic adenosine monophosphate (cAMP) is a key secondary messenger in many biological processes, including the regulation of metabolism, gene expression, and cellular excitability. It is synthesized from adenosine triphosphate (ATP) by the enzyme adenylyl cyclase and is degraded by the enzyme phosphodiesterase.

In the body, cAMP plays a crucial role in mediating the effects of hormones and neurotransmitters on target cells. For example, when a hormone binds to its receptor on the surface of a cell, it can activate a G protein, which in turn activates adenylyl cyclase to produce cAMP. The increased levels of cAMP then activate various effector proteins, such as protein kinases, which go on to regulate various cellular processes.

Overall, the regulation of cAMP levels is critical for maintaining proper cellular function and homeostasis, and abnormalities in cAMP signaling have been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Guanine Deaminase is an enzyme that catalyzes the chemical reaction in which guanine, one of the four nucleotides that make up DNA and RNA, is deaminated to form xanthine. This reaction is part of the purine catabolism pathway, which is the breakdown of purines to produce energy and eliminate nitrogenous waste. The gene that encodes this enzyme in humans is located on chromosome 2 and is called GDA. Deficiency in guanine deaminase has been associated with Lesch-Nyhan syndrome, a rare genetic disorder characterized by mental retardation, self-mutilation, spasticity, and uric acid overproduction.

Adenine nucleotides are molecules that consist of a nitrogenous base called adenine, which is linked to a sugar molecule (ribose in the case of adenosine monophosphate or AMP, and deoxyribose in the case of adenosine diphosphate or ADP and adenosine triphosphate or ATP) and one, two, or three phosphate groups. These molecules play a crucial role in energy transfer and metabolism within cells.

AMP contains one phosphate group, while ADP contains two phosphate groups, and ATP contains three phosphate groups. When a phosphate group is removed from ATP, energy is released, which can be used to power various cellular processes such as muscle contraction, nerve impulse transmission, and protein synthesis. The reverse reaction, in which a phosphate group is added back to ADP or AMP to form ATP, requires energy input and often involves the breakdown of nutrients such as glucose or fatty acids.

In addition to their role in energy metabolism, adenine nucleotides also serve as precursors for other important molecules, including DNA and RNA, coenzymes, and signaling molecules.

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

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

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

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

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

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

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

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

Phosphates, in a medical context, refer to the salts or esters of phosphoric acid. Phosphates play crucial roles in various biological processes within the human body. They are essential components of bones and teeth, where they combine with calcium to form hydroxyapatite crystals. Phosphates also participate in energy transfer reactions as phosphate groups attached to adenosine diphosphate (ADP) and adenosine triphosphate (ATP). Additionally, they contribute to buffer systems that help maintain normal pH levels in the body.

Abnormal levels of phosphates in the blood can indicate certain medical conditions. High phosphate levels (hyperphosphatemia) may be associated with kidney dysfunction, hyperparathyroidism, or excessive intake of phosphate-containing products. Low phosphate levels (hypophosphatemia) might result from malnutrition, vitamin D deficiency, or certain diseases affecting the small intestine or kidneys. Both hypophosphatemia and hyperphosphatemia can have significant impacts on various organ systems and may require medical intervention.

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.

5'-Nucleotidase is an enzyme that is found on the outer surface of cell membranes, including those of liver cells and red blood cells. Its primary function is to catalyze the hydrolysis of nucleoside monophosphates, such as adenosine monophosphate (AMP) and guanosine monophosphate (GMP), to their corresponding nucleosides, such as adenosine and guanosine, by removing a phosphate group from the 5' position of the nucleotide.

Abnormal levels of 5'-Nucleotidase in the blood can be indicative of liver or bone disease. For example, elevated levels of this enzyme in the blood may suggest liver damage or injury, such as that caused by hepatitis, cirrhosis, or alcohol abuse. Conversely, low levels of 5'-Nucleotidase may be associated with certain types of anemia, including aplastic anemia and paroxysmal nocturnal hemoglobinuria.

Medical professionals may order a 5'-Nucleotidase test to help diagnose or monitor the progression of these conditions. It is important to note that other factors, such as medication use or muscle damage, can also affect 5'-Nucleotidase levels, so results must be interpreted in conjunction with other clinical findings and diagnostic tests.

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.

A muscle is a soft tissue in our body that contracts to produce force and motion. It is composed mainly of specialized cells called muscle fibers, which are bound together by connective tissue. There are three types of muscles: skeletal (voluntary), smooth (involuntary), and cardiac. Skeletal muscles attach to bones and help in movement, while smooth muscles are found within the walls of organs and blood vessels, helping with functions like digestion and circulation. Cardiac muscle is the specific type that makes up the heart, allowing it to pump blood throughout the body.

Hydroxymethylbilane Synthase (HMBS) is an enzyme that plays a crucial role in the metabolic pathway known as heme biosynthesis. Heme is an essential component of various proteins, including hemoglobin, which is responsible for oxygen transport in the blood.

The HMBS enzyme catalyzes the conversion of aminolevulinic acid (ALA) and glycine into a linear tetrapyrrole intermediate called hydroxymethylbilane. This reaction is the third step in the heme biosynthesis pathway, and it takes place in the mitochondria of cells.

Deficiencies in HMBS can lead to a rare genetic disorder called acute intermittent porphyria (AIP), which is characterized by neurovisceral attacks and neurological symptoms such as abdominal pain, vomiting, hypertension, tachycardia, and mental disturbances.

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

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

Purine nucleotides have several vital functions within cells:

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

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

Hypoxanthine is a purine derivative and an intermediate in the metabolic pathways of nucleotide degradation, specifically adenosine to uric acid in humans. It is formed from the oxidation of xanthine by the enzyme xanthine oxidase. In the body, hypoxanthine is converted to xanthine and then to uric acid, which is excreted in the urine. Increased levels of hypoxanthine in the body can be indicative of various pathological conditions, including tissue hypoxia, ischemia, and necrosis.

... 1 is an enzyme that in humans is encoded by the AMPD1 gene. Adenosine monophosphate deaminase is an enzyme that ... by directly inhibiting AMP deaminase, thereby increasing cellular AMP. It has been shown that in environments with high ... "Metformin activates AMP kinase through inhibition of AMP deaminase". J. Biol. Chem. 286 (1): 1-11. doi:10.1074/jbc.M110.121806 ... is a disorder in which the body produces insufficient AMP deaminase. adenosine monophosphate (AMP) inosine monophosphate (IMP) ...
... is an enzyme that in humans is encoded by the AMPD2 gene. High AMPD2 expression levels correlate with poor ... Mahnke-Zizelman DK, Sabina RL (Nov 1992). "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene ... Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL (1992). "Molecular cloning of AMP deaminase isoform L. Sequence and ... Van den Bergh F, Sabina RL (1996). "Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative ...
AMP deaminase 2 protein; the gains in AMPD2 protein immunoreactivity were associated with copy number gains in the AMPD2 gene ...
AMP deaminase 3 is an enzyme that in humans is encoded by the AMPD3 gene. This gene encodes a member of the AMP deaminase gene ... Mahnke-Zizelman DK, Sabina RL (October 1992). "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene ... Ogasawara N, Goto H, Yamada Y, Nishigaki I, Itoh T, Hasegawa I, Park KS (January 1987). "Deficiency of AMP deaminase in ... Yamada Y, Goto H, Wakamatsu N, Ogasawara N (2001). "A rare case of complete human erythrocyte AMP deaminase deficiency due to ...
1998). "Control of AMP deaminase 1 binding to myosin heavy chain". Am. J. Physiol. 275 (3 Pt 1): C870-81. doi:10.1152/ajpcell. ...
AMP is normally converted into IMP by myoadenylate deaminase-so myoadenylate deaminase deficiency reduces energy that would be ... AMP deaminase is an enzyme that converts adenosine monophosphate (AMP) to inosine monophosphate (IMP), freeing an ammonia ... Fischer, H.; Esbjornsson, M.; Sabina, R. L.; Stromberg, A.; Peyrard-Janvid, M.; Norman, B. (2007). "AMP deaminase deficiency is ... The first effect-the loss of AMP-is mostly significant because AMP contains ribose, a sugar molecule that is also used to make ...
It can also be formed by the deamination of adenosine monophosphate by AMP deaminase. It can be hydrolysed to inosine. The ... AMP differs from inosinate by the replacement of IMP's carbon-6 carbonyl with an amino group. The interconversion of AMP and ... Finally, carbon 2 gains the amino group by spending an ATP molecule (which becomes AMP+2Pi). While AMP synthesis requires GTP, ... Within a few steps inosinate becomes AMP or GMP. Both compounds are RNA nucleotides. ...
Mitochondrial myopathies AMP deaminase deficiency (myoadenylate deaminase deficiency, MADD) "Metabolic Myopathies". www. ... Nucleotide metabolism disorder-defect in purine nucleotide cycle enzyme (such as AMP deaminase deficiency). Purine nucleotide ... the majority of those with AMP-deaminase deficiency are asymptomatic). H2O + ATP → H+ + ADP + Pi + energy → muscle contraction ... Nucleotide Metabolism: Myoadenylate Deaminase Deficiency Bonnet D, Martin D, Villain E, Jouvet P, Rabier D, Brivet M, Saudubray ...
... as well as in the R or T states based on the presence of AMP. AMP deaminase deficiency (MADD) Glycogenolysis McArdle Disease ( ... Glycogen phosphorylase b is not always inactive in muscle, as it can be activated allosterically by AMP. An increase in AMP ... This change increases phosphorylase activity up to 25% even in the absence of AMP, and enhances AMP activation further. The ... Binding of AMP at this site, corresponding in a change from the T state of the enzyme to the R state, results in small changes ...
It has also been recognized that AMP deaminase protein and activity is upregulated in mouse hearts that overexpress HIF-1α, ... their mechanism of action is inhibition of adenosine deaminase. Adenosine deaminase deficiency GRCh38: Ensembl release 89: ... Adenosine deaminase (also known as adenosine aminohydrolase, or ADA) is an enzyme (EC 3.5.4.4) involved in purine metabolism. ... Adenosine deaminase deficiency leads to pulmonary fibrosis, suggesting that chronic exposure to high levels of adenosine can ...
... such as AMP deaminase deficiency), and those involving enzymes or transport proteins within the mitochondrion (mitochondrial ...
... synthase converts IMP to adenylosuccinate adenylosuccinate lyase converts adenylosuccinate into AMP AMP deaminase converts AMP ... then adenosine deaminase creates inosine Alternatively, AMP deaminase creates inosinic acid, then a nucleotidase creates ... The enzyme is an allosteric enzyme, so it can be converted from IMP, GMP and AMP in high concentration binds the enzyme to ... So IMP, GMP and AMP are inhibitors while PRPP is an activator. Between the formation of 5'-phosphoribosyl, aminoimidazole and ...
... nucleotide deaminases MeSH D08.811.277.151.653.060 - amp deaminase MeSH D08.811.277.151.653.200 - dcmp deaminase MeSH D08.811. ... adenosine deaminase MeSH D08.811.277.151.486.250 - cytidine deaminase MeSH D08.811.277.151.486.625 - cytosine deaminase MeSH ... cyclic amp-dependent protein kinases MeSH D08.811.913.696.620.682.700.150.125.500 - beta-adrenergic-receptor kinase MeSH ... guanine deaminase MeSH D08.811.277.151.418 - methenyltetrahydrofolate cyclohydrolase MeSH D08.811.277.151.486 - nucleoside ...
... encoding enzyme AMP deaminase 3 API5: encoding protein Apoptosis inhibitor 5 APLNR: Apelin receptor (APJ receptor) APOA4: ...
... dCMP deaminase (DCTD) AMP deaminase (AMPD1) Adenosine Deaminase acting on tRNA (ADAT) Adenosine Deaminase acting on dsRNA (ADAR ... APOBEC1 APOBEC3A-H, APOBEC3G - affects HIV Activation-induced cytidine deaminase (AICDA) Cytidine deaminase (CDA) ... Guanine Deaminase (GDA) Adenosine monophosphate deaminase deficiency type 1 Hofmann elimination Smith, Michael B.; March, Jerry ... Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver; ...
... encoding enzyme AMP deaminase 2 ARID1A (1p36) ATXN7L2: Ataxin 7-like 2 AZIN2: encoding enzyme Antizyme inhibitor 2 (AzI2) also ...
The turnover number for adenosine-phosphate deaminase is 690 ATP, 630 ADP, and 710 AMP. The km value is 0.047 for 5'-AMP. the ... Other names in common use include adenylate deaminase, adenine nucleotide deaminase, and adenosine (phosphate) deaminase. The ... AMP, and 3',5'-cyclic AMP. Inhibitors of adenosine-phosphate deaminase include Mn2+ (neutral or alkaline pH), F−, Fe3+, CN−, ... Adenosine-phosphate deaminase binds to 5'-AMP using water to break the C-N bond and replacing it with a carbonyl group. ...
... a nucleotide found in RNA AMP deaminase, a human enzyme encoded by the AMPD1 gene Antimicrobial peptides, immune system ... Look up AMP or amp in Wiktionary, the free dictionary. Amp or AMP may refer to: Ampere, a unit of electric current, often ... AMPS (disambiguation) Amped (disambiguation) Ampere (disambiguation) All pages with titles beginning with AMP All pages with ... NYSE symbol The AMP, a youth center and music venue in Minot, North Dakota, U.S. AMP Incorporated, U.S. connector company AMP ...
AMP deaminase is needed to convert AMP into IMP in the purine nucleotide cycle. Without this enzyme, the excessive AMP buildup ... AMP deaminase deficiency (formally known as myoadenylate deaminase deficiency or MADD) is a metabolic myopathy which results in ... In AMP deaminase deficiency, excess adenosine is converted into uric acid in the following reaction: AMP → Adenosine → Inosine ... ATP), the purine nucleotide cycle produces ammonia (NH3) when it converts AMP into IMP. (With the exception of AMP deaminase ...
... deaminase deficiency is a known cause of immunodeficiency. The adenosine analog NITD008 has been reported to directly ... Adenosine used as a second messenger can be the result of de novo purine biosynthesis via adenosine monophosphate (AMP), though ... When adenosine enters the circulation, it is broken down by adenosine deaminase, which is present in red blood cells and the ... Its derivatives include the energy carriers adenosine mono-, di-, and triphosphate, also known as AMP/ADP/ATP. Cyclic adenosine ...
... adenine deaminase EC 3.5.4.3: guanine deaminase EC 3.5.4.4: adenosine deaminase EC 3.5.4.5: cytidine deaminase EC 3.5.4.6: AMP ... adenosine-phosphate deaminase EC 3.5.4.18: ATP deaminase EC 3.5.4.19: phosphoribosyl-AMP cyclohydrolase EC 3.5.4.20: ... pterin deaminase EC 3.5.4.12: dCMP deaminase EC 3.5.4.13: dCTP deaminase EC 3.5.4.14: Now included in EC 3.5.4.5, (deoxy) ... dCTP deaminase (dUMP-forming) EC 3.5.4.31: S-methyl-5′-thioadenosine deaminase EC 3.5.4.32: 8-oxoguanine deaminase EC 3.5.4.33 ...
Phillips, A.T.; Wood, W.A. (1964). "Basis for AMP activation of "Biodegradative" threonine dehydrase from". Biochemical and ... "Subunit structure of biodegradative threonine deaminase". The Journal of Biological Chemistry. 252 (7): 2206-8. doi:10.1016/ ...
... adenosine deaminase deficiency - adenovirus - adenylyl-(glutamate-ammonia ligase) hydrolase - agarose gel electrophoresis - ... agarose gel - akaryocyte - Alagille syndrome - alkaline lysis - allele - amino acids - amino terminus - amp resistance - ...
AMP and GMP can then be converted into ATP and GTP, respectively, by kinases that add additional phosphates. ATP stimulates ... Guanine is then deaminated via guanine deaminase to form xanthine which is then converted to uric acid. Oxygen is the final ... "Adenosine deaminase (ADA) deficiency". Learn.Genetics. Archived from the original on 3 November 2014. Retrieved 31 October 2014 ... IMP is then converted to AMP (adenosine monophosphate) using GTP and aspartate, which is converted into fumarate. While IMP can ...
Glutamine donates an ammonium group, which reacts with β-aspartyl-AMP to form asparagine and free AMP. Two asparagine ... In terms of regulation, the enzymes threonine deaminase, dihydroxy acid dehydrase, and transaminase are controlled by end- ... The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP. In ... Phosphoribosyl-ATP converts to phosphoribosyl-AMP (PRAMP). His4 then catalyzes the formation of phosphoribosylformiminoAICAR- ...
AICAR is an analog of adenosine monophosphate (AMP) that is capable of stimulating AMP-dependent protein kinase (AMPK) activity ... AICAR is able to enter the de novo synthesis pathway for adenosine synthesis to inhibit adenosine deaminase causing an increase ... Potential role of AMP-activated protein kinase". Basic & Clinical Pharmacology & Toxicology. 105 (1): 10-16. doi:10.1111/j.1742 ... is an analog of adenosine that enters cardiac cells to inhibit adenosine kinase and adenosine deaminase. It enhances the rate ...
The AdK from mammalian sources, in addition to carrying out ATP-dependent phosphorylation of Ado, also catalyzes an Ado-AMP ... adenosine kinase and adenosine deaminase in tissues from vertebrates and invertebrates in relation to the control of the ... Gupta RS (June 1996). "Adenosine-AMP exchange activity is an integral part of the mammalian adenosine kinase". Biochemistry and ... Explanation of exchange reaction between adenosine and AMP". The Journal of Biological Chemistry. 269 (27): 17820-5. doi: ...
Adenosine is quickly broken down by adenosine deaminase, which is present in red cells and the vessel wall. A decrease in SVR ( ... AMP). Most of the adenosine that is produced leaves the cell and acts as a direct vasodilator on the vascular wall. Because ...
AMP can be converted into IMP by the enzyme myoadenylate deaminase, freeing an ammonia group. In a catabolic pathway, the ... AMP Or AMP may be produced by the hydrolysis of one high energy phosphate bond of ADP: ADP + H2O → AMP + Pi AMP can also be ... AMP is also a component in the synthesis of RNA. AMP is present in all known forms of life. AMP does not have the high energy ... AMP can be regenerated to ATP as follows: AMP + ATP → 2 ADP (adenylate kinase in the opposite direction) ADP + Pi → ATP (this ...
EHNA is also a very potent adenosine deaminase inhibitor with an IC50 ~2 nM. This dual inhibition would lead to the ... van Calker D, Müller M, Hamprecht B (1978). "Adenosine inhibits the accumulation of cyclic AMP in cultured brain cells". Nature ... Although EHNA potently inhibits adenosine deaminase, it has been successfully used with the proper controls as a tool to probe ... Theoretically, this problem can be resolved if the effect of adenosine accumulated by EHNA, a result of adenosine deaminase ...
AMP deaminase 1 is an enzyme that in humans is encoded by the AMPD1 gene. Adenosine monophosphate deaminase is an enzyme that ... by directly inhibiting AMP deaminase, thereby increasing cellular AMP. It has been shown that in environments with high ... "Metformin activates AMP kinase through inhibition of AMP deaminase". J. Biol. Chem. 286 (1): 1-11. doi:10.1074/jbc.M110.121806 ... is a disorder in which the body produces insufficient AMP deaminase. adenosine monophosphate (AMP) inosine monophosphate (IMP) ...
... it was hoped that overproduction of AMP deaminase could be detected in yeast, by selecting for resistance to the AMP deaminase ... Attempts were made to clone the yeast adenosine-5-monophosphate deaminase (AMP deaminase) gene from S. cerevisiae using a ... MacKenzie, Jane (1989) AMP Deaminase From Saccharomyces cerevisiae. PhD thesis, University of Glasgow. ... Although yeast AMP deaminase is sensitive to dCF in vitro no effect was observed in vivo (possibly due to lack of uptake of the ...
... deaminase deficiency is a condition that can affect the muscles used for movement (skeletal muscles). Explore symptoms, ... AMP deaminase deficiency is caused by mutations in the AMPD1 gene, which provides instructions for producing an enzyme called ... The lack of AMP deaminase activity can result in fatigue, muscle weakness or pain, or other muscle problems in some people with ... AMP deaminase deficiency is one of the most common inherited muscle disorders in white populations, affecting 1 in 50 to 100 ...
Bovine Intestine CAS 9026-93-1 Native adenosine deaminase from bovine intestine. - Find MSDS or SDS, a COA, data sheets and ... Alkaline Phosphatase, AMP-deaminase, Guanase, Nucleotide Phosphorylase: Specific activity. ≥200 units/mg protein. ... Native adenosine deaminase from bovine intestine.. More,, Native adenosine deaminase from bovine intestine. Less,, Adenosine ... Native adenosine deaminase from bovine intestine. A cytosolic enzyme that catalyzes the hydrolysis of adenosine to inosine and ...
AMP deaminase 2 (isoform L; AMPD2) NM_004037.5 2.989 DNAJA1 DnaJ (Hsp40) homologue, subfamily A, member 1 NM_001539.1 3.184 ...
Variation in the gene for muscle-specific AMP deaminase is associated with insulin clearance, a highly heritable trait. ...
Adenylate deaminase is an enzyme that catalyzes the transformation of adenosine monophosphate (AMP) to inosine monophosphate ( ... Myoadenylate Deaminase Deficiency. Most patients with myoadenylate deaminase (MAD) deficiency, a disorder of purine nucleotide ... Myoadenylate deaminase deficiency is the result of a relatively common mutant allele with a heterogeneous clinical presentation ... Myoadenylate deaminase deficiency: absence of correlation with exercise intolerance in 452 muscle biopsies. J Neurol. 1987 Aug ...
1Hancock Chad R. "Protecting the cellular energy state during contractions: role of AMP deaminase." Journal of Physiology and ... A specific version of the AMPD1 gene has been associated with a decreased ability to remove AMP in muscle cells1-3. This is ... It does this by eliminating a byproduct of ATP known as AMP (or adenosine monophosphate)1-3. Removing this byproduct is similar ... to unclogging a drain-failure to do so can cause a buildup of AMP and prevent the body from making more ATP1. ...
Ecto-AMP deaminase blunts the ATP-derived adenosine A2A receptor facilitation of acetylcholine release at rat motor nerve ... ATP is broken down to ADP and AMP by extracellular ATPases [29]. Further, as shown directly in the rat NMJ, AMP was either ... nucleotidase or deaminated into inosine monophosphate by ecto-AMP deaminase [39]. Inosine is an inactive metabolite [40], but ... Calcitonin gene-related peptide and cyclic AMP stimulate phosphoinositide turnover in skeletal muscle cells. Interaction ...
Clonidine inhibited cyclic AMP accumulation to a greater extent in the presence of either adenosine deaminase or theophylline. ... The antilipolytic activity of clonidine was dramatically enhanced by addition of adenosine deaminase or theophylline to ... was also enhanced by the presence of adenosine deaminase. The release of adenosine from adipocytes in which the nucleotide pool ...
AMP, which was deaminated by AMP deaminase (AMP + H2O ® IMP + NH3). Therefore, adenine nucleotides in the muscle cells were ... The intracellular and plasma concentrations of ATP, ADP, AMP, GTP, GDP, IMP, HX and Uric acid were measured with an HPLC system ... Meyer, R.A., and Terjung, R.L. AMP deamination and IMP reamination in working skeletal muscle. Am. J. Physiol., 239: C32-C38, ... The level of IMP significantly augmented (p, .001) after 45 min of exercise, while no remarkable changes of GTP and AMP levels ...
... transformylase and adenosine deaminase, leading to a rise in intracellular concentrations of AICAR-monophosphate (ZMP) and AMP. ... AMP-activated protein kinase: greater AMP dependence, and preferential nuclear localization, of complexes containing the α2 ... Methotrexate (MTX) activates an AMP-activated protein kinase (AMPK) and cyclic AMP-response element binding protein (CREB) ... consistent with inhibition of AICAR transformylase and adenosine deaminase leading to accumulation of ZMP and AMP. These ...
... and weakly inhibits AMP deaminase, MMP-1, -7, -9, and -14. ...
This leads to upregulation of myokinase and AMP deaminase activity that ultimately increases production of inosine ... If we perform a series of hydrolysis reactions, we then convert ADP to adenosine monophosphate (AMP). From here, adenosine ... Remove adenosine via the adenosine deaminase enzyme to form inosine monophosphate. This is then followed by dephosphorylation ( ... Additionally, levels of adenosine diphosphate (ADP) and adenosine monophosphate (AMP) increase. ...
AMP is catabolized by AMP deaminase to inosine monophosphate in the inosine pathway, which would circumvent the production of ... AMP deaminase in rat brain extracts, however, is inhibited at ischemic ATP concentrations resulting in AMP breakdown to ... and AMP,[. 207 ] inosine[. 11 170 ] and adenosine[. 138 ] all activate A1 receptors. ... Reduced hepatic oxygen in rat and mouse hepatocytes has been shown to increase the dephosphorylation of AMP to adenosine, ...
... occurs in the adenosine monophosphate deaminase 3 (AMPD3) gene. This is known to cause erythrocyte AMP deaminase deficiency ...
Human N6-Methyl-AMP/DAMP Aminohydrolase (Abacavir 5-Monophosphate Deaminase) is Capable of Metabolizing N6-Substituted Purine ... N6-methyl-AMP hydrolase activates N6-substituted purine ANPs. Symposium Series 2005, Vol. 7, pp. 463-464 [Abstract] Published ... Phosphorylation of Purine (Phosphonomethoxy)alkyl Derivatives by Mitochondrial AMP Kinase (AK2 Type) from L1210 Cells. 2000, ...
AMP deaminase. AMP deaminase. 3.5.4.6 PF3D7_0204500 PFB0200c. aspartate aminotransferase. aspartate transaminase. 2.6.1.1 ...
AMP deaminase, putative n=1 Tax=Ricinus communis RepID=B9T1I5_RICCO. 0.0 ...
AMP]i/[ATP]i and [ADP]i/[ATP]i ratios[29][30][31][32]. Moreover, MF decreases the activity of the enzyme AMP-deaminase (AMPD), ... Ouyang, J.; Parakhia, R.A.; Ochs, R.S. Metformin activates AMP kinase through inhibition of AMP deaminase. J. Biol. Chem. 2011 ... AMP deaminase; AMPK, the heterotrimeric AMP-activated protein kinase consisting of the α1/2 (the target for activation ... and suppression of the activity of AMP deaminase [48] (Figure). A decrease in the activity of cAMP-dependent pathways in the ...
AMP deaminase. General function:. Involved in deaminase activity. Specific function:. AMP deaminase plays a critical role in ... N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. Gene Name:. ADE13. Uniprot ID:. Q05911 Molecular weight:. 54509.89844. Reactions ... ATP + L-serine + tRNA(Ser) → AMP + diphosphate + L-seryl-tRNA(Ser).. ATP + L-serine + tRNA(Sec) → AMP + diphosphate + L-seryl- ... ATP + L-serine + tRNA(Ser) → AMP + diphosphate + L-seryl-tRNA(Ser).. ATP + L-serine + tRNA(Sec) → AMP + diphosphate + L-seryl- ...
keywords = "2-deoxy-D-glucose, AMP deaminase, Adenosine deaminase, Anoxia, EHNA, Isolated rat heart, NMR", ... The difference between the two models has been ascribed to the inhibition of AMP deaminase by P(i) in the anoxic heart. We ... The difference between the two models has been ascribed to the inhibition of AMP deaminase by P(i) in the anoxic heart. We ... The difference between the two models has been ascribed to the inhibition of AMP deaminase by P(i) in the anoxic heart. We ...
AMP deaminase 1 (AMPD1; AMP â IMP + NH3) deficiency in skeletal muscle results in an inordinate accumulation of AMP during ... Proteínas Quinases Ativadas por AMP/metabolismo , AMP Desaminase/genética , AMP Desaminase/metabolismo , AMP Desaminase/ ... we overexpressed an AMP degrading enzyme, AMP deaminase 3 (AMPD3), via adenovirus in C2C12 myotubes. RESULTS: Overexpression of ... One of the most highly upregulated genes in atrophic muscle is AMP deaminase 3 (AMPD3: AMPâ ¯â â ¯IMPâ ¯+â ¯NH3), which ...
Recent Advances in Molecular Biology of AMP Deaminase Takayuki Morisaki, Hiroko Morisaki ...
The AMP deaminase reaction is shown in the next slide; the adenosine deaminase reaction is analogous. The guanase and xanthine ... If the supply of AMP exceeds demand, it can be converted back to IMP by AMP deaminase, either for degradation or for conversion ... Enzymes: 1, AMP deaminase; 2, IMP dehydrogenase; 3, adenosine deaminase; 4, guanase; 5, xanthine dehydrogenase or oxidase. ... However, it seems that a genetic deficiency for AMP deaminase is quite common and usually asymptomatic [111], suggesting that ...
","adenosine deaminase [Ensembl]. Adenosine/AMP deaminase domain [InterProScan].","protein_coding" "AGT24118","N559_2422"," ... ","Enamine/imine deaminase [Ensembl]. Endoribonuclease L-PSP [Interproscan].","protein_coding" "CRO27447","rpoZ","Pseudomonas ...
AMPD2: encoding enzyme AMP deaminase 2. *ARID1A (1p36). *ATXN7L2: Ataxin 7-like 2 ...
muscle AMP deaminase deficiency, see adenosine monophosphate deaminase deficiency. *muscle glycogen phosphorylase deficiency, ... myoadenylate deaminase deficiency, see adenosine monophosphate deaminase deficiency. *myoclonic dystonia, see myoclonus- ... MAD deficiency, see adenosine monophosphate deaminase deficiency. *MADA deficiency, see adenosine monophosphate deaminase ...
... or muscle adenosine monophosphate deaminase deficiency) The enzyme myoadenylate deaminase converts AMP to inosine and ammonia. ... Adenosine deaminase deficiency Adenosine deaminase converts adenosine and deoxyadenosine to inosine and deoxyinosine, which are ... Immune cells are especially sensitive to this defect; adenosine deaminase deficiency causes one form of severe combined ... Treatment of adenosine deaminase deficiency is by bone marrow or stem cell transplantation and enzyme replacement therapy. ...
  • Adenosine monophosphate deaminase is an enzyme that converts adenosine monophosphate (AMP) to inosine monophosphate (IMP), freeing an ammonia molecule in the process. (wikipedia.org)
  • Adenosine monophosphate deaminase 1 catalyzes the deamination of AMP to IMP in skeletal muscle and plays an important role in the purine nucleotide cycle. (wikipedia.org)
  • Adenosine monophosphate (AMP) deaminase deficiency is a condition that can affect the muscles used for movement (skeletal muscles). (medlineplus.gov)
  • It does this by eliminating a byproduct of ATP known as AMP (or adenosine monophosphate)1-3. (helix.com)
  • MTX increases intracellular accumulation of adenosine monophosphate (AMP) and 5-aminoimidazole-4-carboxamide ribonucleotide which activates AMP-activated protein kinase (AMPK). (bmj.com)
  • If we perform a series of hydrolysis reactions, we then convert ADP to adenosine monophosphate (AMP). (tigerfitness.com)
  • Adenosine monophosphate, also known as adenylic acid or 5'-AMP, belongs to the class of organic compounds known as purine ribonucleoside monophosphates. (ymdb.ca)
  • Oxidative stress depletes adenosine triphosphate (ATP) and adenine nucleotides, whereas adenosine monophosphate (AMP) deaminase seems to depress energy metabolism by blocking the salvage pathway of purine nucleotides. (unisi.it)
  • AMPD1 deficiency, also known as myoadenylate deaminase deficiency, is a disorder in which the body produces insufficient AMP deaminase. (wikipedia.org)
  • A G468-T AMPD1 mutant allele contributes to the high incidence of myoadenylate deaminase deficiency in the Caucasian population. (medlineplus.gov)
  • Myoadenylate deaminase deficiency caused by alternative splicing due to a novel intronic mutation in the AMPD1 gene. (medlineplus.gov)
  • Additionally, the presence of an abnormal allele in some patients, such as with myoadenylate deaminase deficiency, may not result in a specific muscular disorder. (medscape.com)
  • Approximately 2% of the population is homozygous for mutant alleles of myoadenylate deaminase, although not all have clinical symptoms. (medscape.com)
  • The enzyme myoadenylate deaminase converts AMP to inosine and ammonia. (msdmanuals.com)
  • Treatment of myoadenylate deaminase deficiency is exercise modulation as appropriate. (msdmanuals.com)
  • AMP deaminase 1 is an enzyme that in humans is encoded by the AMPD1 gene. (wikipedia.org)
  • AMP deaminase deficiency is caused by mutations in the AMPD1 gene, which provides instructions for producing an enzyme called AMP deaminase. (medlineplus.gov)
  • Mutations in the AMPD1 gene often result in an AMP deaminase enzyme that cannot function and as a result, energy production in skeletal muscle cells is decreased. (medlineplus.gov)
  • Remove adenosine via the adenosine deaminase enzyme to form inosine monophosphate. (tigerfitness.com)
  • Treatment of adenosine deaminase deficiency is by bone marrow or stem cell transplantation and enzyme replacement therapy. (msdmanuals.com)
  • In many affected individuals, AMP deaminase deficiency does not cause any symptoms. (medlineplus.gov)
  • In rare cases, affected individuals have more severe symptoms including severe muscle weakness, low muscle tone (hypotonia), and muscle wasting (atrophy), but it is unclear whether these symptoms are due solely to AMP deaminase deficiency or additional health conditions. (medlineplus.gov)
  • Exercise intolerance associated with AMP deaminase deficiency usually becomes apparent in childhood or early adulthood. (medlineplus.gov)
  • AMP deaminase deficiency is one of the most common inherited muscle disorders in white populations, affecting 1 in 50 to 100 people. (medlineplus.gov)
  • The lack of AMP deaminase activity can result in fatigue, muscle weakness or pain, or other muscle problems in some people with AMP deaminase deficiency. (medlineplus.gov)
  • Researchers speculate that additional factors, both genetic and environmental, may determine whether a person develops the signs and symptoms of AMP deaminase deficiency. (medlineplus.gov)
  • Fischer H, Esbjornsson M, Sabina RL, Stromberg A, Peyrard-Janvid M, Norman B. AMP deaminase deficiency is associated with lower sprint cycling performance in healthy subjects. (medlineplus.gov)
  • Hanisch F, Joshi P, Zierz S. AMP deaminase deficiency in skeletal muscle is unlikely to be of clinical relevance. (medlineplus.gov)
  • AMP â IMP + NH 3 ) deficiency in skeletal muscle results in an inordinate accumulation of AMP during strenuous exercise, with some but not all studies reporting premature fatigue and reduced work capacity. (bvsalud.org)
  • To further explore these inconsistencies, we investigated the extent to which AMPD1 deficiency impacts skeletal muscle contractile function of different muscles and the [AMP]/AMPK responses to different intensities of fatiguing contractions. (bvsalud.org)
  • NEW & NOTEWORTHY AMP deaminase 1 (AMPD1) deficiency has been associated with premature muscle fatigue and reduced work capacity, but this finding has been inconsistent. (bvsalud.org)
  • Diagnosis of adenosine deaminase deficiency is by DNA analysis. (msdmanuals.com)
  • This seemingly paradoxical phenotype is due to lower glucose utilization and greater lipid oxidation in HDAC3 -depleted muscles, a fuel switch caused by the activation of anaplerotic reactions driven by AMP deaminase 3 (Ampd3) and catabolism of branched-chain amino acids. (haidut.me)
  • Elevated levels of AMP lead to an inhibition of PP2C activity, which allows AMPK to remain stable in the active Thr 172 -phosphorylated state [ 27 ] [ 28 ] . (encyclopedia.pub)
  • The difference between the two models has been ascribed to the inhibition of AMP deaminase by P(i) in the anoxic heart. (elsevierpure.com)
  • This involved the construction of ade, hpt1 yeast strains in which the AMP deaminase reaction is the major source of inosine-5'-monophosphate (IMP). (gla.ac.uk)
  • Adenosine deaminase converts adenosine and deoxyadenosine to inosine and deoxyinosine, which are further broken down and excreted. (msdmanuals.com)
  • Using the adenosine deaminase inhibitor erythro-9-(2-hydroxy-3-nonyl) adenine (EHNA), we determine the contribution of the adenosine pathway to the abundant purine release of two Langendorff-perfused rat heart models which differ particularly in inorganic phosphate (P(i)) content: the 2-deoxy-D-glucose (2DG) perfused heart and the anoxic heart. (elsevierpure.com)
  • 3). Xanthosine, the initial substrate of purine alkaloid syn-thesis, is supplied by at least four diï¬ erent pathways: de novo purine biosynthesis (de novo route), the degradation pathways of adenine nucleotides (AMP route) and guanine nucleotides (GMP route), and the S-adenosyl-L-methionine (SAM) cycle (SAM route) (Fig. No public clipboards found for this slide. (hotelsunshine.co.in)
  • A specific version of the AMPD1 gene has been associated with a decreased ability to remove AMP in muscle cells1-3. (helix.com)
  • In addition, AMPD1 knockdown in EDL exaggerated the AMP response to contractions at LOW (+100%) and MOD (+54%) duty cycles, but not at HIGH duty cycle. (bvsalud.org)
  • Furthermore, AMPD1 knockdown differentially affects the [AMP]/AMPK responses to fatiguing contractions in an intensity-dependent manner in EDL muscle. (bvsalud.org)
  • Initially, it was hoped that overproduction of AMP deaminase could be detected in yeast, by selecting for resistance to the AMP deaminase inhibitor, deoxycoformycin (dCF). (gla.ac.uk)
  • A research report shows that the widely prescribed diabetes medication metformin works on AMP-activated kinase (AMPK) by directly inhibiting AMP deaminase, thereby increasing cellular AMP. (wikipedia.org)
  • Mechanistically, MTX treatment led to cyclic AMP response element-binding protein (CREB) Ser133 phosphorylation, while AMPK depletion attenuated this response and the induction of MnSOD and HO-1. (bmj.com)
  • Fludarabine Phosphate Injection, USP contains fludarabine phosphate, a fluorinated nucleotide analog of the antiviral agent vidarabine, 9-ß-D-arabinofuranosyladenine (ara-A) that is relatively resistant to deamination by adenosine deaminase. (guidelinecentral.com)
  • Attempts were made to clone the yeast adenosine-5'-monophosphate deaminase (AMP deaminase) gene from S. cerevisiae using a number of strategies. (gla.ac.uk)
  • The goal of this work was to evaluate the activity of AMP deaminase and 5-nucleotidase in the cytosolic kidney fraction of rats under the conditions of different protein and sucrose content in a diet. (edu.ua)
  • It has been shown that in environments with high potassium concentrations, AMP-deaminase is regulated by ATP and ADP through a "Km-type" mechanism. (wikipedia.org)
  • Depletion of ATP and activation of AMP deaminase are related to calcium ion concentrations. (unisi.it)
  • After the five daily doses of 25 mg 2-fluoro-ara-AMP/m 2 to cancer patients infused over 30 minutes, 2-fluoro-ara-A concentrations show a moderate accumulation. (guidelinecentral.com)
  • 1Hancock Chad R. "Protecting the cellular energy state during contractions: role of AMP deaminase. (helix.com)
  • Clonidine inhibited cyclic AMP accumulation to a greater extent in the presence of either adenosine deaminase or theophylline. (aspetjournals.org)
  • Cyclic AMP (slide 7.5.4 )and cyclic GMP (slide 9.3.6 ) function as intracellular second messengers. (heresy.is)
  • The antilipolytic activity of clonidine was dramatically enhanced by addition of adenosine deaminase or theophylline to incubation media, suggesting that the substance is adenosine. (aspetjournals.org)
  • The antilipolytic activity of prostaglandin E 1 and nicotinic acid, but not insulin, was also enhanced by the presence of adenosine deaminase. (aspetjournals.org)
  • Methods drawing on technological innovations for delivering expert mental health treatment are already being incorporated into routine care in large nonmetropolitan regions and show high parent satisfaction and preliminary evidence of efficacy, AMP deaminase tolerability, and sustainability ( Myers et al. (pde-inhibitors.com)
  • Removing this byproduct is similar to unclogging a drain-failure to do so can cause a buildup of AMP and prevent the body from making more ATP1. (helix.com)
  • AMPD1 deficiency, also known as myoadenylate deaminase deficiency, is a disorder in which the body produces insufficient AMP deaminase. (wikipedia.org)
  • A G468-T AMPD1 mutant allele contributes to the high incidence of myoadenylate deaminase deficiency in the Caucasian population. (medlineplus.gov)
  • Myoadenylate deaminase deficiency caused by alternative splicing due to a novel intronic mutation in the AMPD1 gene. (medlineplus.gov)
  • Additionally, the presence of an abnormal allele in some patients, such as with myoadenylate deaminase deficiency, may not result in a specific muscular disorder. (medscape.com)
  • Approximately 2% of the population is homozygous for mutant alleles of myoadenylate deaminase, although not all have clinical symptoms. (medscape.com)
  • The enzyme myoadenylate deaminase converts AMP to inosine and ammonia. (msdmanuals.com)
  • Treatment of myoadenylate deaminase deficiency is exercise modulation as appropriate. (msdmanuals.com)
  • Myoadenylate deaminase (MAD) is an enzyme active in skeletal muscle, probably during exercise of moderate intensity but certainly during vigorous exercise, when the deamination of AMP leads to increased levels of IMP and ammonia. (portlandpress.com)
  • In adenosine deaminase deficiency, adenosine and adenine accumulate in the plasma. (medscape.com)
  • To explore this phenomenon, we considered the putative role(s) of two AMP degradative enzymes, AMP phosphatase (AMPP) and AMP deaminase (AMPD), which indirectly control the adenylate pool size by adjusting the rate of AMP degradation [ 10 ]. (hindawi.com)
  • AMP deaminase (AMPD) deficiency is an inherited disorder of skeletal muscle found in approximately 2% of the Caucasian population. (nih.gov)
  • There also were significant differences in AMP-deaminase (AMPD), adenosine deaminase (ADA) and purine nucleoside phosphorylase (PNP) activities. (umn.edu)
  • Adenosine monophosphate deaminase 1 catalyzes the deamination of AMP to IMP in skeletal muscle and plays an important role in the purine nucleotide cycle. (wikipedia.org)
  • Hanisch F, Joshi P, Zierz S. AMP deaminase deficiency in skeletal muscle is unlikely to be of clinical relevance. (medlineplus.gov)
  • Acute activation of AMP-activated protein kinase (AMPK) increases monocarboxylate transporter (MCT) expression in skeletal muscle. (bvsalud.org)
  • Adenosine deaminase (ADA) deficiency is an inherited disorder that damages the immune system and causes severe combined immunodeficiency (SCID). (nih.gov)
  • We further show that the deaminase ADAL preferentially catabolizes N 6 -methyl-2'-deoxyadenosine monophosphate (6mdAMP) in vitro and in vivo , and adenylate kinase 1 restricts the phosphorylation rate of 6mdAMP, together contributing to the identified checkpoint. (researchsquare.com)
  • 5'-IMP is converted from 5'-AMP by adenylate deaminase. (yamasa-biochem.com)
  • A yeast strain deficient in AMP deaminase activity was produced and shown to be deficient in AMP deaminase protein by Western blot analysis. (elsevierpure.com)
  • instructions for making a protein called RNA-specific adenosine deaminase 1 (ADAR1). (nih.gov)
  • The protein encoded by this gene is important in purine metabolism by converting AMP to IMP. (nih.gov)
  • The encoded protein, which acts as a homotetramer, is one of three AMP deaminases found in mammals. (nih.gov)
  • Adenosine deaminase 2 (ADA2) deficiency is a disorder characterized by abnormal inflammation of various tissues. (nih.gov)
  • Adenosine deaminase 2 deficiency (DADA2) is a complex systemic autoinflammatory disorder in which vasculopathy/vasculitis, dysregulated immune function, and/or hematologic abnormalities may predominate. (nih.gov)
  • [ 2 , 3 ] One disorder is adenosine deaminase (ADA) deficiency, which is Online Mendelian Inheritance in Man (OMIM) subject number 102700, and the other is purine nucleoside phosphorylase (PNP) deficiency, which is OMIM subject number 164050. (medscape.com)
  • Human adenosine deaminase deficiency, OMIM 102700 (ADA deficiency) is a genetic disorder which causes severe combined immunodeficiency (SCID). (jumdc.com)
  • Adenosine deaminase converts adenosine and deoxyadenosine to inosine and deoxyinosine, which are further broken down and excreted. (msdmanuals.com)
  • Adenosine enhances electrophysiological effects of intracellular cyclic AMP secondary to sympathetic stimulation. (pharmacology2000.com)
  • 아데노신(Adenosine)은 ADP 와 ATP 형태의 에너지 전달 반응과 cyclic AMP 형태의 세포 신호 전달에서 중요한 역할을하는 purine nucleoside 입니다. (komabiotech.co.kr)
  • In both adenosine deaminase and purine nucleoside phosphorylase deficiencies, thymocytes are thought to be selectively destroyed because of elevated levels of dATP and dGTP. (medscape.com)
  • A research report shows that the widely prescribed diabetes medication metformin works on AMP-activated kinase (AMPK) by directly inhibiting AMP deaminase, thereby increasing cellular AMP. (wikipedia.org)
  • Because of the relatively high activity of intracellular adenosine kinase (converting adenosine to AMP), adenosine concentrations inside cells are normally low, so the net flux through these transporters is inwardly directed. (medscape.com)
  • Examples: ADA for adenosine deaminase UMPK for uridine monophosphate kinase Gd for glucose~6-phosphate dehydrogenase (Obviously, when lower case letters are used to designate one locus, it is undesirable to use the same letters but in capi- tals (e.g. (nih.gov)
  • No overall homology was found between yeast AMP deaminase and E. coli AMP nucleosidase. (elsevierpure.com)
  • The nucleic acid degradation method follows the steps of (1) hydrolyzing yeast RNA with Nuclease P1 to produce 5'-AMP, 5'-CMP, 5'-GMP and 5'-UMP and (2) separating and refining these 5'-nucleotides using ion-exchange column chromatography. (yamasa-biochem.com)
  • In rare cases, affected individuals have more severe symptoms including severe muscle weakness, low muscle tone (hypotonia), and muscle wasting (atrophy), but it is unclear whether these symptoms are due solely to AMP deaminase deficiency or additional health conditions. (medlineplus.gov)
  • AMP deaminase plays a critical role in energy metabolism. (nih.gov)
  • Exercise intolerance associated with AMP deaminase deficiency usually becomes apparent in childhood or early adulthood. (medlineplus.gov)
  • Diagnosis of adenosine deaminase deficiency is by DNA analysis. (msdmanuals.com)
  • In many affected individuals, AMP deaminase deficiency does not cause any symptoms. (medlineplus.gov)
  • Researchers speculate that additional factors, both genetic and environmental, may determine whether a person develops the signs and symptoms of AMP deaminase deficiency. (medlineplus.gov)
  • in particular, an ice worm-specific amino acid substitution near the AMP binding site (i.e. (hindawi.com)
  • 1] An amino group is removed from AMP to produce IMP by AMP deaminase or from adenosine to produce inosine (hypoxanthine-ribose) by adenosine deaminase. (pharmacy180.com)
  • Adenosine monophosphate (AMP) deaminase deficiency is a condition that can affect the muscles used for movement (skeletal muscles). (medlineplus.gov)
  • The extracellular levels of adenosine are mostly regulated by cytosolic 5'-nucleotidase (converting AMP into adenosine) and adenosine, involved in the conversion of adenosine to AMP (Figure 3). (medscape.com)