Amidophosphoribosyltransferase
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Amidophosphoribosyltransferase
Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an enzyme responsible for catalyzing the conversion of Phosphoribosylpyrophosphate, 5-phosphoribosyl-1-pyrophosphate (PRPP) into Phosphoribosylamine, 5-phosphoribosyl-1-amine (PRA), using the amine group from a glutamine side-chain. This is the committing step in de novo purine synthesis. In humans it is encoded by the ''PPAT'' (phosphoribosyl pyrophosphate amidotransferase) gene. ATase is a member of the purine/pyrimidine phosphoribosyltransferase family. Structure and function The enzyme consists of two domains: a glutaminase domain that produces ammonia from glutamine by hydrolysis and a phosphoribosyltransferase domain that binds the ammonia to ribose-5-phosphate. Coordination between the two active sites of enzyme give it special complexity. The glutaminase domain is homologous to other N-terminal nucleophile (Ntn) hydrolases such as carbamoyl phosphate ...
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Catalytic Triad
A catalytic triad is a set of three coordinated amino acids that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An acid- base-nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to release the product and regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine or even selenocysteine. The 3D structure of the enzyme brings together the triad residues in a precise orientation, even though they may be far apart in the sequence (primary structure). As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show some ...
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Phosphoribosylpyrophosphate
Phosphoribosyl pyrophosphate (PRPP) is a pentose phosphate. It is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, as well as in pyrimidine nucleotide formation. Hence it is a building block for DNA and RNA. The vitamins thiamine and cobalamin, and the amino acid tryptophan also contain fragments derived from PRPP. It is formed from ribose 5-phosphate (R5P) by the enzyme ribose-phosphate diphosphokinase: : It plays a role in transferring phospho-ribose groups in several reactions, some of which are salvage pathways: In '' de novo'' generation of purines, the enzyme amidophosphoribosyltransferase acts upon PRPP to create phosphoribosylamine. The histidine biosynthesis pathway involves the reaction between PRPP and ATP, which activates the latter to ring cleavage. Carbon atoms from ribose in PRPP form the linear chain and part of the imidazole ring in histidine. The same is true for the biosynthesis of tryptophan, with th ...
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Phosphoribosylpyrophosphate
Phosphoribosyl pyrophosphate (PRPP) is a pentose phosphate. It is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, as well as in pyrimidine nucleotide formation. Hence it is a building block for DNA and RNA. The vitamins thiamine and cobalamin, and the amino acid tryptophan also contain fragments derived from PRPP. It is formed from ribose 5-phosphate (R5P) by the enzyme ribose-phosphate diphosphokinase: : It plays a role in transferring phospho-ribose groups in several reactions, some of which are salvage pathways: In '' de novo'' generation of purines, the enzyme amidophosphoribosyltransferase acts upon PRPP to create phosphoribosylamine. The histidine biosynthesis pathway involves the reaction between PRPP and ATP, which activates the latter to ring cleavage. Carbon atoms from ribose in PRPP form the linear chain and part of the imidazole ring in histidine. The same is true for the biosynthesis of tryptophan, with th ...
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5-phosphoribosylamine
Phosphoribosylamine (PRA) is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, and hence is a building block for DNA and RNA. The vitamins thiamine and cobalamin also contain fragments derived from PRA. : It is the product of the enzyme amidophosphoribosyltransferase which attaches ammonia from glutamine to phosphoribosyl pyrophosphate (PRPP) at its anomeric carbon: : + → + + PPi The biosynthesis pathway next combines PRA with glycine in a process driven by ATP giving glycineamide ribonucleotide (GAR). The enzyme phosphoribosylamine—glycine ligase catalyses the reaction forming an amide bond: : + + ATP → + ADP + Pi See also * 5-Aminoimidazole ribotide * Purine metabolism Purine metabolism refers to the metabolic pathways to synthesize and break down purines that are present in many organisms. Biosynthesis Purines are biologically synthesized as nucleotides and in particular as ribotides, i.e. bases attached to ri ... Refe ...
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Phosphoribosylamine
Phosphoribosylamine (PRA) is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, and hence is a building block for DNA and RNA. The vitamins thiamine and cobalamin also contain fragments derived from PRA. : It is the product of the enzyme amidophosphoribosyltransferase which attaches ammonia from glutamine to phosphoribosyl pyrophosphate (PRPP) at its anomeric carbon: : + → + + PPi The biosynthesis pathway next combines PRA with glycine in a process driven by ATP giving glycineamide ribonucleotide (GAR). The enzyme phosphoribosylamine—glycine ligase catalyses the reaction forming an amide bond: : + + ATP → + ADP + Pi See also * 5-Aminoimidazole ribotide 5′-Phosphoribosyl-5-aminoimidazole (or aminoimidazole ribotide, AIR) is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, and hence is a building block for DNA and RNA. The vitamins thiamine and coba ... * Purine met ...
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Glutamine
Glutamine (symbol Gln or Q) is an α-amino acid that is used in the biosynthesis of proteins. Its side chain is similar to that of glutamic acid, except the carboxylic acid group is replaced by an amide. It is classified as a charge-neutral, polar amino acid. It is non-essential and conditionally essential in humans, meaning the body can usually synthesize sufficient amounts of it, but in some instances of stress, the body's demand for glutamine increases, and glutamine must be obtained from the diet. It is encoded by the codons CAA and CAG. In human blood, glutamine is the most abundant free amino acid. The dietary sources of glutamine include especially the protein-rich foods like beef, chicken, fish, dairy products, eggs, vegetables like beans, beets, cabbage, spinach, carrots, parsley, vegetable juices and also in wheat, papaya, Brussels sprouts, celery, kale and fermented foods like miso. Functions Glutamine plays a role in a variety of biochemical functions: * Pr ...
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Tyrosine
-Tyrosine or tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a non-essential amino acid with a polar side group. The word "tyrosine" is from the Greek ''tyrós'', meaning ''cheese'', as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. It is called tyrosyl when referred to as a functional group or side chain. While tyrosine is generally classified as a Hydrophobe, hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is Genetic code, encoded by the Genetic code#Codons, codons UAC and UAU in messenger RNA. Functions Aside from being a proteinogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. It occurs in proteins that are part of signal transduction processes and functions as a receiver of phosphate groups that are transferred by way of protein kinases. Phosphorylation of the hyd ...
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Guanosine Diphosphate
Guanosine diphosphate, abbreviated GDP, is a nucleoside diphosphate. It is an ester of pyrophosphoric acid with the nucleoside guanosine. GDP consists of a pyrophosphate group, a pentose sugar ribose, and the nucleobase guanine. GDP is the product of GTP dephosphorylation by GTPases, e.g., the G-proteins that are involved in signal transduction. GDP is converted into GTP with the help of pyruvate kinase and phosphoenolpyruvate. See also * DNA *Guanosine triphosphate *Nucleoside *Nucleotide *Oligonucleotide *RNA Ribonucleic acid (RNA) is a polymeric molecule essential in various biological roles in coding, decoding, regulation and expression of genes. RNA and deoxyribonucleic acid ( DNA) are nucleic acids. Along with lipids, proteins, and carbohydra ... References {{DEFAULTSORT:Guanosine phosphate2 Nucleotides Phosphate esters Purines Pyrophosphates ...
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Adenosine Diphosphate
Adenosine diphosphate (ADP), also known as adenosine pyrophosphate (APP), is an important organic compound in metabolism and is essential to the flow of energy in living cells. ADP consists of three important structural components: a sugar backbone attached to adenine and two phosphate groups bonded to the 5 carbon atom of ribose. The diphosphate group of ADP is attached to the 5’ carbon of the sugar backbone, while the adenine attaches to the 1’ carbon. ADP can be interconverted to adenosine triphosphate (ATP) and adenosine monophosphate (AMP). ATP contains one more phosphate group than does ADP. AMP contains one fewer phosphate group. Energy transfer used by all living things is a result of dephosphorylation of ATP by enzymes known as ATPases. The cleavage of a phosphate group from ATP results in the coupling of energy to metabolic reactions and a by-product of ADP. ATP is continually reformed from lower-energy species ADP and AMP. The biosynthesis of ATP is achieved through ...
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Guanosine Monophosphate
Guanosine monophosphate (GMP), also known as 5′-guanidylic acid or guanylic acid (conjugate base guanylate), is a nucleotide that is used as a monomer in RNA. It is an ester of phosphoric acid with the nucleoside guanosine. GMP consists of the phosphate group, the pentose sugar ribose, and the nucleobase guanine; hence it is a ribonucleoside monophosphate. Guanosine monophosphate is commercially produced by microbial fermentation. As an acyl substituent, it takes the form of the prefix guanylyl-. ''De novo'' synthesis GMP synthesis starts with D-ribose 5′-phosphate, a product of the pentose phosphate pathway. The synthesis proceeds by the gradual formation of the purine ring on carbon-1 of ribose, with CO2, glutamine, glycine, aspartate and one-carbon derivatives of tetrahydrofolate donating various elements towards the building of the ring As inhibitor of guanosine monophosphate synthesis in experimental models, the glutamine analogue DON can be used.''Ahluwalia GS et alMet ...
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Adenosine Monophosphate
Adenosine monophosphate (AMP), also known as 5'-adenylic acid, is a nucleotide. AMP consists of a phosphate group, the sugar ribose, and the nucleobase adenine; it is an ester of phosphoric acid and the nucleoside adenosine. As a substituent it takes the form of the prefix adenylyl-. AMP plays an important role in many cellular metabolic processes, being interconverted to Adenosine diphosphate, ADP and/or Adenosine triphosphate, ATP. AMP is also a component in the synthesis of RNA. AMP is present in all known forms of life. Production and degradation AMP does not have the high energy phosphoanhydride bond associated with ADP and ATP. AMP can be produced from Adenosine diphosphate, ADP: : 2 ADP → ATP + AMP Or AMP may be produced by the hydrolysis of one high energy phosphate bond of ADP: : ADP + H2O → AMP + phosphate, Pi AMP can also be formed by hydrolysis of Adenosine triphosphate, ATP into AMP and pyrophosphate: : ATP + H2O → AMP + pyrophosphate, PPi When RNA i ...
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Feedback Inhibition
An enzyme inhibitor is a molecule that binds to an enzyme and blocks its activity. Enzymes are proteins that speed up chemical reactions necessary for life, in which substrate molecules are converted into products. An enzyme facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the enzyme that accelerates the most difficult step of the reaction. An enzyme inhibitor stops ("inhibits") this process, either by binding to the enzyme's active site (thus preventing the substrate itself from binding) or by binding to another site on the enzyme such that the enzyme's catalysis of the reaction is blocked. Enzyme inhibitors may bind reversibly or irreversibly. Irreversible inhibitors form a chemical bond with the enzyme such that the enzyme is inhibited until the chemical bond is broken. By contrast, reversible inhibitors bind non-covalently and may spontaneously leave the enzyme, allowing the enzyme to resume its function ...
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