Aminoimidazole carboxamide is a compound that is involved in the metabolic pathways of nucleotide synthesis in cells. It is also known as AICA ribonucleotide, and is a precursor to an important energy molecule in the body called adenosine triphosphate (ATP).

In medical terms, aminoimidazole carboxamide is sometimes used as a research tool to study cellular metabolism and has been investigated for its potential therapeutic use in various conditions such as neurodegenerative disorders and ischemia-reperfusion injury. However, it is not commonly used as a medication in clinical practice.

Glutamate Formimidoyltransferase (FTCD) is an enzyme that plays a role in the metabolism of histidine, one of the essential amino acids. The enzyme catalyzes the transfer of a formimidoyl group from the derivative of histidine, formiminoglutamate (FIGLU), to the amino group of glutamate, forming formiminoglutamic acid and freeing up tetrahydrofolate in the process.

The reaction catalyzed by FTCD is as follows:

formiminoglutamate + glutamate -> formiminoglutamic acid + glutamate

This enzyme is found in various organisms, including humans, and is located in the mitochondria. A deficiency in FTCD can lead to an accumulation of FIGLU and may be associated with certain neurological disorders.

Phosphoribosylaminoimidazolecarboxamide formyltransferase (AIRFT) is an enzyme involved in the purine nucleotide biosynthesis pathway. The systematic medical name for this enzyme is "phosphoribosylaminoimidazole carboxamide formyltransferase, IMP cyclohydrolase, and GMP synthase."

The primary function of AIRFT is to catalyze the conversion of 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) to formylated AICAR (FAICAR), which is an essential step in the synthesis of inosine monophosphate (IMP). IMP is a key precursor for the biosynthesis of both adenine and guanine nucleotides.

The enzyme's activity can be measured by determining the rate of conversion of AICAR to FAICAR, which requires the presence of 10-formyltetrahydrofolate (10-Formyl-THF) as a cofactor. Deficiency in this enzyme can lead to impaired purine synthesis and may result in various clinical manifestations such as developmental delay, neurological symptoms, and immunodeficiency.

Hydroxymethyl and Formyl Transferases are a class of enzymes that catalyze the transfer of hydroxymethyl or formyl groups from one molecule to another. These enzymes play important roles in various metabolic pathways, including the synthesis and modification of nucleotides, amino acids, and other biomolecules.

One example of a Hydroxymethyl Transferase is DNA methyltransferase (DNMT), which catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to the 5-carbon of cytosine residues in DNA, forming 5-methylcytosine. This enzyme can also function as a Hydroxymethyl Transferase by catalyzing the transfer of a hydroxymethyl group from SAM to cytosine residues, forming 5-hydroxymethylcytosine.

Formyl Transferases are another class of enzymes that catalyze the transfer of formyl groups from one molecule to another. One example is formyltransferase domain containing protein 1 (FTCD1), which catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to methionine, forming N5-formiminotetrahydrofolate and methionine semialdehyde.

These enzymes are essential for maintaining proper cellular function and are involved in various physiological processes, including gene regulation, DNA repair, and metabolism. Dysregulation of these enzymes has been implicated in several diseases, including cancer, neurological disorders, and cardiovascular disease.

Ribonucleotides are organic compounds that consist of a ribose sugar, a phosphate group, and a nitrogenous base. They are the building blocks of RNA (ribonucleic acid), one of the essential molecules in all living organisms. The nitrogenous bases found in ribonucleotides include adenine, uracil, guanine, and cytosine. These molecules play crucial roles in various biological processes, such as protein synthesis, gene expression, and cellular energy production. Ribonucleotides can also be involved in cell signaling pathways and serve as important cofactors for enzymatic reactions.

Carbon-Nitrogen (C-N) ligases are a class of enzymes that catalyze the joining of a carbon atom from a donor molecule to a nitrogen atom in an acceptor molecule through a process called ligase reaction. This type of enzyme plays a crucial role in various biological processes, including the biosynthesis of amino acids, nucleotides, and other biomolecules that contain both carbon and nitrogen atoms.

C-N ligases typically require ATP or another energy source to drive the reaction forward, as well as cofactors such as metal ions or vitamins to facilitate the chemical bond formation between the carbon and nitrogen atoms. The specificity of C-N ligases varies depending on the enzyme, with some acting only on specific donor and acceptor molecules while others have broader substrate ranges.

Examples of C-N ligases include glutamine synthetase, which catalyzes the formation of glutamine from glutamate and ammonia, and asparagine synthetase, which catalyzes the formation of asparagine from aspartate and ammonia. Understanding the function and regulation of C-N ligases is important for understanding various biological processes and developing strategies to modulate them in disease states.

Phosphoribosylglycinamide formyltransferase (PGTF) is an enzyme involved in the biosynthesis of purine nucleotides, which are essential components of DNA and RNA. The systematic medical definition of PGTF is:

"An enzyme that catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to the amino group of phosphoribosylglycinamide, forming N-formylphosphoribosylglycinamide and tetrahydrofolate as byproducts. This reaction is the fourth step in the de novo synthesis pathway of purine nucleotides."

PGTF's gene name is GART (Glycinamide Ribonucleotide Transformylase), and it is located on human chromosome 10q24.32-q25.1. Mutations in the GART gene can lead to a rare autosomal recessive disorder called Lesch-Nyhan syndrome, which is characterized by hyperuricemia, neurological symptoms, and self-mutilating behavior.

Thiamine, also known as vitamin B1, is a water-soluble vitamin that plays a crucial role in certain metabolic reactions, particularly in the conversion of carbohydrates into energy in the body. It is essential for the proper functioning of the heart, nerves, and digestive system. Thiamine acts as a cofactor for enzymes involved in the synthesis of neurotransmitters and the metabolism of carbohydrates, lipids, and proteins. Deficiency in thiamine can lead to serious health complications, such as beriberi (a disease characterized by peripheral neuropathy, muscle wasting, and heart failure) and Wernicke-Korsakoff syndrome (a neurological disorder often seen in alcoholics due to chronic thiamine deficiency). Thiamine is found in various foods, including whole grains, legumes, pork, beef, and fortified foods.

Carbon-Nitrogen (C-N) ligases with glutamine as amide-N-donor are a class of enzymes that catalyze the joining of a carbon atom and a nitrogen atom from different molecules, with glutamine serving as the nitrogen donor. The reaction specifically involves the transfer of the amide nitrogen from glutamine to a carbonyl carbon atom, resulting in the formation of a new C-N bond.

This type of enzyme is involved in various biological processes, including the biosynthesis of amino acids, nucleotides, and other biomolecules. The reaction catalyzed by these enzymes often requires ATP as an energy source to drive the formation of the new bond.

An example of a C-N ligase with glutamine as amide-N-donor is glutamine synthetase, which catalyzes the formation of glutamine from glutamate and ammonia using ATP as an energy source. The enzyme uses the amide nitrogen of glutamine to transfer the nitrogen atom to the carbonyl carbon of glutamate, forming a new C-N bond in the process.

"Agelas" is a genus of demosponges, also known as marine sponges, that belong to the family Agelasidae. These sponges are commonly found in tropical and subtropical waters around the world. They are known for their distinctive skeletal structures, which are made up of fused spicules (small, needle-like structures) that form a rigid framework. Some species of Agelas contain compounds with potential medicinal properties, such as anti-inflammatory and antiviral agents. However, there is no specific medical definition or use of the term "Agelas."

Purines are heterocyclic aromatic organic compounds that consist of a pyrimidine ring fused to an imidazole ring. They are fundamental components of nucleotides, which are the building blocks of DNA and RNA. In the body, purines can be synthesized endogenously or obtained through dietary sources such as meat, seafood, and certain vegetables.

Once purines are metabolized, they are broken down into uric acid, which is excreted by the kidneys. Elevated levels of uric acid in the body can lead to the formation of uric acid crystals, resulting in conditions such as gout or kidney stones. Therefore, maintaining a balanced intake of purine-rich foods and ensuring proper kidney function are essential for overall health.

Imidazoles are a class of heterocyclic organic compounds that contain a double-bonded nitrogen atom and two additional nitrogen atoms in the ring. They have the chemical formula C3H4N2. In a medical context, imidazoles are commonly used as antifungal agents. Some examples of imidazole-derived antifungals include clotrimazole, miconazole, and ketoconazole. These medications work by inhibiting the synthesis of ergosterol, a key component of fungal cell membranes, leading to increased permeability and death of the fungal cells. Imidazoles may also have anti-inflammatory, antibacterial, and anticancer properties.

Carboxy-lyases are a class of enzymes that catalyze the removal of a carboxyl group from a substrate, often releasing carbon dioxide in the process. These enzymes play important roles in various metabolic pathways, such as the biosynthesis and degradation of amino acids, sugars, and other organic compounds.

Carboxy-lyases are classified under EC number 4.2 in the Enzyme Commission (EC) system. They can be further divided into several subclasses based on their specific mechanisms and substrates. For example, some carboxy-lyases require a cofactor such as biotin or thiamine pyrophosphate to facilitate the decarboxylation reaction, while others do not.

Examples of carboxy-lyases include:

1. Pyruvate decarboxylase: This enzyme catalyzes the conversion of pyruvate to acetaldehyde and carbon dioxide during fermentation in yeast and other organisms.
2. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): This enzyme is essential for photosynthesis in plants and some bacteria, as it catalyzes the fixation of carbon dioxide into an organic molecule during the Calvin cycle.
3. Phosphoenolpyruvate carboxylase: Found in plants, algae, and some bacteria, this enzyme plays a role in anaplerotic reactions that replenish intermediates in the citric acid cycle. It catalyzes the conversion of phosphoenolpyruvate to oxaloacetate and inorganic phosphate.
4. Aspartate transcarbamylase: This enzyme is involved in the biosynthesis of pyrimidines, a class of nucleotides. It catalyzes the transfer of a carboxyl group from carbamoyl aspartate to carbamoyl phosphate, forming cytidine triphosphate (CTP) and fumarate.
5. Urocanase: Found in animals, this enzyme is involved in histidine catabolism. It catalyzes the conversion of urocanate to formiminoglutamate and ammonia.

Ligases are a group of enzymes that catalyze the formation of a covalent bond between two molecules, usually involving the joining of two nucleotides in a DNA or RNA strand. They play a crucial role in various biological processes such as DNA replication, repair, and recombination. In DNA ligases, the enzyme seals nicks or breaks in the phosphodiester backbone of the DNA molecule by catalyzing the formation of an ester bond between the 3'-hydroxyl group and the 5'-phosphate group of adjacent nucleotides. This process is essential for maintaining genomic integrity and stability.

"Salmonella enterica" is a gram-negative, facultatively anaerobic bacterium that belongs to the family Enterobacteriaceae. It is a common cause of foodborne illnesses worldwide, often resulting in gastroenteritis, which is characterized by symptoms such as diarrhea, abdominal cramps, fever, and vomiting.

"Salmonella enterica" is further divided into several serovars or subspecies, with some of the most common ones causing human illness being Typhimurium and Enteritidis. These bacteria are typically transmitted to humans through contaminated food or water sources, such as raw or undercooked meat, poultry, eggs, and dairy products.

Once ingested, "Salmonella enterica" can colonize the gastrointestinal tract and release endotoxins that cause inflammation and damage to the intestinal lining. In some cases, the bacteria can spread to other parts of the body, leading to more severe and potentially life-threatening infections, particularly in individuals with weakened immune systems.

Preventing "Salmonella enterica" infections involves proper food handling and preparation practices, such as washing hands and surfaces thoroughly, cooking meats and eggs to appropriate temperatures, and avoiding cross-contamination between raw and cooked foods.

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.

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.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.