Ribose 5-phosphate
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Ribose 5-phosphate
Ribose 5-phosphate (R5P) is both a product and an intermediate of the pentose phosphate pathway. The last step of the Redox, oxidative reactions in the pentose phosphate pathway is the production of ribulose 5-phosphate. Depending on the body's state, ribulose 5-phosphate can reversibly Isomerization, isomerize to ribose 5-phosphate. Ribulose 5-phosphate can alternatively undergo a series of isomerizations as well as transaldolations and transketolations that result in the production of other pentose phosphates as well as fructose 6-phosphate and glyceraldehyde 3-phosphate (both intermediates in glycolysis). The enzyme ribose-phosphate diphosphokinase converts ribose-5-phosphate into phosphoribosyl pyrophosphate. Structure R5P consists of a five-carbon sugar, ribose, and a phosphate group at the five-position carbon. It can exist in open chain form or in furanose form. The furanose form is most commonly referred to as ribose 5-phosphoric acid. Biosynthesis The formation of ...
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Pentose Phosphate Pathway
The pentose phosphate pathway (also called the phosphogluconate pathway and the hexose monophosphate shunt and the HMP Shunt) is a metabolic pathway parallel to glycolysis. It generates NADPH and pentoses (5-carbon sugars) as well as ribose 5-phosphate, a precursor for the synthesis of nucleotides. While the pentose phosphate pathway does involve oxidation of glucose, its primary role is anabolic rather than catabolic. The pathway is especially important in red blood cells (erythrocytes). There are two distinct phases in the pathway. The first is the oxidative phase, in which NADPH is generated, and the second is the non-oxidative synthesis of 5-carbon sugars. For most organisms, the pentose phosphate pathway takes place in the cytosol; in plants, most steps take place in plastids. Like glycolysis, the pentose phosphate pathway appears to have a very ancient evolutionary origin. The reactions of this pathway are mostly enzyme-catalyzed in modern cells, however, they also occur ...
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Glucose 6-phosphate
Glucose 6-phosphate (G6P, sometimes called the Robison ester) is a glucose sugar phosphorylated at the hydroxy group on carbon 6. This dianion is very common in cells as the majority of glucose entering a cell will become phosphorylated in this way. Because of its prominent position in cellular chemistry, glucose 6-phosphate has many possible fates within the cell. It lies at the start of two major metabolic pathways: glycolysis and the pentose phosphate pathway. In addition to these two metabolic pathways, glucose 6-phosphate may also be converted to glycogen or starch for storage. This storage is in the liver and muscles in the form of glycogen for most multicellular animals, and in intracellular starch or glycogen granules for most other organisms. Production From glucose Within a cell, glucose 6-phosphate is produced by phosphorylation of glucose on the sixth carbon. This is catalyzed by the enzyme hexokinase in most cells, and, in higher animals, glucokinase in certain ...
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Pyruvate Kinase
Pyruvate kinase is the enzyme involved in the last step of glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), yielding one molecule of pyruvate and one molecule of ATP. Pyruvate kinase was inappropriately named (inconsistently with a conventional kinase) before it was recognized that it did not directly catalyze phosphorylation of pyruvate, which does not occur under physiological conditions. Pyruvate kinase is present in four distinct, tissue-specific isozymes in animals, each consisting of particular kinetic properties necessary to accommodate the variations in metabolic requirements of diverse tissues. Isozymes in vertebrates Four isozymes of pyruvate kinase expressed in vertebrates: L (liver), R (erythrocytes), M1 (muscle and brain) and M2 (early fetal tissue and most adult tissues). The L and R isozymes are expressed by the gene PKLR, whereas the M1 and M2 isozymes are expressed by the gene PKM2. The R ...
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Transaldolase
Transaldolase is an enzyme () of the non-oxidative phase of the pentose phosphate pathway. In humans, transaldolase is encoded by the ''TALDO1'' gene. The following chemical reaction is catalyzed by transaldolase: : sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate \rightleftharpoons erythrose 4-phosphate + fructose 6-phosphate Clinical significance The pentose phosphate pathway has two metabolic functions: (1) generation of nicotinamide adenine dinucleotide phosphate (reduced NADPH), for reductive biosynthesis, and (2) formation of ribose, which is an essential component of ATP, DNA, and RNA. Transaldolase links the pentose phosphate pathway to glycolysis. In patients with deficiency of transaldolase, there's an accumulation of erythritol (from erythrose 4-phosphate), D-arabitol, and ribitol. The deletion in 3 base pairs in the ''TALDO1'' gene results in the absence of serine at position 171 of the transaldolase protein, which is part of a highly conserved region, ...
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Transketolase
Transketolase (abbreviated as TK) is an enzyme that is encoded by the TKT gene. It participates in both the pentose phosphate pathway in all organisms and the Calvin cycle of photosynthesis. Transketolase catalyzes two important reactions, which operate in opposite directions in these two pathways. In the first reaction of the non-oxidative pentose phosphate pathway, the cofactor thiamine diphosphate accepts a 2-carbon fragment from a 5-carbon ketose ( D-xylulose-5-P), then transfers this fragment to a 5-carbon aldose (D-ribose-5-P) to form a 7-carbon ketose ( sedoheptulose-7-P). The abstraction of two carbons from D-xylulose-5-P yields the 3-carbon aldose glyceraldehyde-3-P. In the Calvin cycle, transketolase catalyzes the reverse reaction, the conversion of sedoheptulose-7-P and glyceraldehyde-3-P to pentoses, the aldose D-ribose-5-P and the ketose D-xylulose-5-P. The second reaction catalyzed by transketolase in the pentose phosphate pathway involves the same thiamine diphosph ...
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Glyceraldehyde 3-phosphate
Glyceraldehyde 3-phosphate, also known as triose phosphate or 3-phosphoglyceraldehyde and abbreviated as G3P, GA3P, GADP, GAP, TP, GALP or PGAL, is a metabolite that occurs as an intermediate in several central pathways of all organisms.Nelson, D. L.; Cox, M. M. "Lehninger, Principles of Biochemistry" 3rd Ed. Worth Publishing: New York, 2000. . With the chemical formula H(O)CCH(OH)CH2OPO32-, this anion is a monophosphate ester of glyceraldehyde. An intermediate in both glycolysis and gluconeogenesis Formation D-glyceraldehyde 3-phosphate is formed from the following three compounds in reversible reactions: *Fructose-1,6-bisphosphate ( F1,6BP), catalyzed by aldolase. ''The numbering of the carbon atoms indicates the fate of the carbons according to their position in fructose 6-phosphate.'' *Dihydroxyacetone phosphate ( DHAP), catalyzed by triose phosphate isomerase. *1,3-bisphosphoglycerate ( 1,3BPG), catalyzed by glyceraldehyde 3-phosphate dehydrogenase. As a substra ...
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Fructose 6-phosphate
Fructose 6-phosphate (sometimes called the Neuberg ester) is a derivative of fructose, which has been phosphorylated at the 6-hydroxy group. It is one of several possible fructosephosphates. The β-D-form of this compound is very common in cells. The great majority of glucose is converted to fructose 6-phosphate upon entering a cell. Fructose is predominantly converted to fructose 1-phosphate by fructokinase following cellular import. History The name ''Neuberg ester'' comes from the German biochemist Carl Neuberg. In 1918, he found that the compound (later identified as fructose 6-phosphate) was beproduced by mild acid hydrolysis of fructose 2,6-bisphosphate.Fruton, Joseph S. ''Proteins, Enzymes, Genes: The Interplay of Chemistry and Biology''. Yale University Press: New Haven, 1999. p 292 In glycolysis Fructose 6-phosphate lies within the glycolysis metabolic pathway and is produced by isomerisation of glucose 6-phosphate. It is in turn further phosphorylated to fructose-1 ...
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Glycolysis
Glycolysis is the metabolic pathway that converts glucose () into pyruvate (). The free energy released in this process is used to form the high-energy molecules adenosine triphosphate (ATP) and reduced nicotinamide adenine dinucleotide (NADH). Glycolysis is a sequence of ten reactions catalyzed by enzymes. Glycolysis is a metabolic pathway that does not require oxygen (In anaerobic conditions pyruvate is converted to lactic acid). The wide occurrence of glycolysis in other species indicates that it is an ancient metabolic pathway. Indeed, the reactions that make up glycolysis and its parallel pathway, the pentose phosphate pathway, occur in the oxygen-free conditions of the Archean oceans, also in the absence of enzymes, catalyzed by metal. In most organisms, glycolysis occurs in the liquid part of cells, the cytosol. The most common type of glycolysis is the ''Embden–Meyerhof–Parnas (EMP) pathway'', which was discovered by Gustav Embden, Otto Meyerhof, and Jakub Karol ...
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Enzyme Catalysis
Enzyme catalysis is the increase in the rate of a process by a biological molecule, an "enzyme". Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, called the active site. Most enzymes are made predominantly of proteins, either a single protein chain or many such chains in a multi-subunit complex. Enzymes often also incorporate non-protein components, such as metal ions or specialized organic molecules known as cofactor (e.g. adenosine triphosphate). Many cofactors are vitamins, and their role as vitamins is directly linked to their use in the catalysis of biological process within metabolism. Catalysis of biochemical reactions in the cell is vital since many but not all metabolically essential reactions have very low rates when uncatalysed. One driver of protein evolution is the optimization of such catalytic activities, although only the most crucial enzymes operate near catalytic e ...
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Ribose-5-phosphate Isomerase
Ribose-5-phosphate isomerase (Rpi) encoded by the RPIA gene is an enzyme () that catalyzes the conversion between ribose-5-phosphate (R5P) and ribulose-5-phosphate (Ru5P). It is a member of a larger class of isomerases which catalyze the interconversion of chemical isomers (in this case structural isomers of pentose). It plays a vital role in biochemical metabolism in both the pentose phosphate pathway and the Calvin cycle. The systematic name of this enzyme class is D-ribose-5-phosphate aldose-ketose-isomerase. Structure Gene RpiA in human beings is encoded on the second chromosome on the short arm (p arm) at position 11.2. Its encoding sequence is nearly 60,000 base pairs long. The only known naturally occurring genetic mutation results in ribose-5-phosphate isomerase deficiency, discussed below. The enzyme is thought to have been present for most of evolutionary history. Knock-out experiments conducted on the genes of various species meant to encode RpiA have indicated simi ...
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NADP+
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP or, in older notation, TPN (triphosphopyridine nucleotide), is a Cofactor (biochemistry), cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). It is used by all forms of cellular life. NADPH is the redox, reduced form of NADP. NADP differs from NAD+, NAD by the presence of an additional phosphate group on the 2' position of the ribose ring that carries the adenine Moiety (chemistry), moiety. This extra phosphate is added by NAD+ kinase, NAD+ kinase and removed by NADP+ phosphatase. Biosynthesis NADP In general, NADP+ is synthesized before NADPH is. Such a reaction usually starts with NAD+, NAD+ from either the de-novo or the salvage pathway, with NAD+ kinase, NAD+ kinase adding the extra phosphate group. ADP-ribosyl cyclase allows for synthesis from nicotinamide in the salvage pathway, and NADP+ phosphatase ...
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