An enzyme that catalyzes the transfer of phosphate from C-3 of 1,3-diphosphoglycerate to C-2 of 3-phosphoglycerate, forming 2,3-diphosphoglycerate. EC 5.4.2.4.
An enzyme that catalyzes the conversion of 2-phospho-D-glycerate to 3-phospho-D-glycerate. EC 5.4.2.1.
2,3-Diphosphoglycerate (2,3-DPG) is a physiological modulator of hemoglobin oxygen affinity, reducing its attraction to oxygen in red blood cells, which facilitates the release of oxygen to tissues with lower oxygen concentrations.
A highly anionic organic phosphate which is present in human red blood cells at about the same molar ratio as hemoglobin. It binds to deoxyhemoglobin but not the oxygenated form, therefore diminishing the oxygen affinity of hemoglobin. This is essential in enabling hemoglobin to unload oxygen in tissue capillaries. It is also an intermediate in the conversion of 3-phosphoglycerate to 2-phosphoglycerate by phosphoglycerate mutase (EC 5.4.2.1). (From Stryer Biochemistry, 4th ed, p160; Enzyme Nomenclature, 1992, p508)
A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.
Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.
An enzyme catalyzing the transfer of a phosphate group from 3-phospho-D-glycerate in the presence of ATP to yield 3-phospho-D-glyceroyl phosphate and ADP. EC 2.7.2.3.
Glyceric acids are compounds that contain a glycerol moiety with one or more carboxylic acid groups, which can exist in various forms such as glycerate, glycerophosphate, and glyceronitrate, playing crucial roles in metabolism and energy production.
A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.
Common name for the order Pleuronectiformes. A very distinctive group in that during development they become asymmetrical, i.e., one eye migrates to lie adjacent to the other. They swim on the eyeless side. FLOUNDER, sole, and turbot, along with several others, are included in this order.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A metabolic process that converts GLUCOSE into two molecules of PYRUVIC ACID through a series of enzymatic reactions. Energy generated by this process is conserved in two molecules of ATP. Glycolysis is the universal catabolic pathway for glucose, free glucose, or glucose derived from complex CARBOHYDRATES, such as GLYCOGEN and STARCH.
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.

Model of 2,3-bisphosphoglycerate metabolism in the human erythrocyte based on detailed enzyme kinetic equations: in vivo kinetic characterization of 2,3-bisphosphoglycerate synthase/phosphatase using 13C and 31P NMR. (1/55)

This is the first in a series of three papers [see also Mulquiney and Kuchel (1999) Biochem. J. 342, 579-594; Mulquiney and Kuchel (1999) Biochem. J. 342, 595-602] that present a detailed mathematical model of erythrocyte metabolism which explains the regulation and control of 2,3-bisphosphoglycerate (2,3-BPG) metabolism. 2,3-BPG is a modulator of haemoglobin oxygen affinity and hence plays an important role in blood oxygen transport and delivery. This paper presents an in vivo kinetic characterization of 2,3-BPG synthase/phosphatase (BPGS/P), the enzyme that catalyses both the synthesis and degradation of 2,3-BPG. Much previous work had indicated that the behaviour of this enzyme in vitro is markedly different from that in vivo. (13)C and (31)P NMR were used to monitor the time courses of selected metabolites when erythrocytes were incubated with or without [U-(13)C]glucose. Simulations of the experimental time courses were then made. By iteratively changing the parameters of the BPGS/P part of the model until a good match between the NMR-derived data and simulations were achieved, it was possible to characterize BPGS/P kinetically in vivo. This work revealed that: (1) the pH-dependence of the synthase activity results largely from a strong co-operative inhibition of the synthase activity by protons; (2) 3-phosphoglycerate and 2-phosphoglycerate are much weaker inhibitors of 2,3-BPG phosphatase in vivo than in vitro; (3) the K(m) of BPGS/P for 2,3-BPG is significantly higher than that measured in vitro; (4) the maximal activity of the phosphatase in vivo is approximately twice that in vitro, when P(i) is the sole activator (second substrate); and (5) 2-phosphoglycollate appears to play no role in the activation of the phosphatase in vivo. Using the newly determined kinetic parameters, the percentage of glycolytic carbon flux that passes through the 2, 3-BPG shunt in the normal in vivo steady state was estimated to be 19%.  (+info)

Phosphocreatine-dependent protein phosphorylation in rat skeletal muscle. (2/55)

Phosphocreatine (PCr) was found to alter the phosphorylation state of two proteins of apparent molecular masses 18 and 29 kDa in dialysed cell-free extracts of rat skeletal muscle in the presence of [gamma-32P]ATP. The 29 kDa protein was identified as phosphoglycerate mutase (PGM), phosphorylated at the active-site histidine residue by 2,3-bisphosphoglycerate (2,3-biPG). 2,3-biPG labelling from [gamma-32P]ATP occurred through the concerted action of phosphoglycerate kinase and 2,3-bisphosphoglycerate mutase. PCr-dependent labelling, which required creatine kinase, resulted from a shift in the phosphoglycerate kinase equilibrium towards 1,3-bisphosphoglycerate (1,3-biPG) synthesis, ultimately resulting in an increase in available [2-32P]2,3-biPG. The maximal catalytic activity of PGM was unaffected by PCr. The 18 kDa protein was transiently phosphorylated at a histidine residue, probably by 1,3-biPG. No proteins of this monomeric molecular mass are known to bind 1,3-biPG, suggesting that the 18 kDa protein is an undescribed phosphoenzyme intermediate. Previous observations of 2- and 3-phosphoglycerate-dependent protein phosphorylation in cytosolic extracts [Ueda & Plagens (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 1229-1233; Pek, Usami, Bilir, Fischer-Bovenkerk & Ueda (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 4294-4298], attributed to the action of novel kinases, are likely to represent phosphoenzyme intermediates labelled by bisphosphorylated metabolites in a similar manner.  (+info)

Immunocytochemical localization of glycolytic and fermentative enzymes in Zymomonas mobilis. (3/55)

Gold-labeled antibodies were used to examine the subcellular locations of 11 glycolytic and fermentative enzymes in Zymomonas mobilis. Glucose-fructose oxidoreductase was clearly localized in the periplasmic region. Phosphogluconate lactonase and alcohol dehydrogenase I were concentrated in the cytoplasm near the plasma membrane. The eight remaining enzymes were more evenly distributed within the cytoplasmic matrix. Selected enzyme pairs were labeled on opposite sides of the same thin section to examine the frequency of colocalization. Results from these experiments provide evidence that glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, and alcohol dehydrogenase I form an enzyme complex.  (+info)

A single MEF-2 site is a major positive regulatory element required for transcription of the muscle-specific subunit of the human phosphoglycerate mutase gene in skeletal and cardiac muscle cells. (4/55)

In order to analyze the transcriptional regulation of the muscle-specific subunit of the human phosphoglycerate mutase (PGAM-M) gene, chimeric genes composed of the upstream region of the PGAM-M gene and the bacterial chloramphenicol acetyltransferase (CAT) gene were constructed and transfected into C2C12 skeletal myocytes, primary cultured cardiac muscle cells, and C3H10T1/2 fibroblasts. The expression of chimeric reporter genes was restricted in skeletal and cardiac muscle cells. In C2C12 myotubes and primary cultured cardiac muscle cells, the segment between nucleotides -165 and +41 relative to the transcription initiation site was sufficient to confer maximal CAT activity. This region contains two E boxes and one MEF-2 motif. Deletion and substitution mutation analysis showed that a single MEF-2 motif but not the E boxes had a substantial effect on skeletal and cardiac muscle-specific enhancer activity and that the cardiac muscle-specific negative regulatory region was located between nucleotides -505 and -165. When the PGAM-M gene constructs were cotransfected with MyoD into C3H10T1/2, the profile of CAT activity was similar to that observed in C2C12 myotubes. Gel mobility shift analysis revealed that when the nuclear extracts from skeletal and cardiac muscle cells were used, the PGAM-M MEF-2 site generated the specific band that was inhibited by unlabeled PGAM-M MEF-2 and muscle creatine kinase MEF-2 oligomers but not by a mutant PGAM-M MEF-2 oligomer. These observations define the PGAM-M enhancer as the only cardiac- and skeletal-muscle-specific enhancer characterized thus far that is mainly activated through MEF-2.  (+info)

Development of a mutagenesis, expression and purification system for yeast phosphoglycerate mutase. Investigation of the role of active-site His181. (5/55)

A system has been developed to allow the convenient production, expression and purification of site-directed mutants of the enzyme phosphoglycerate mutase from Saccharomyces cerevisiae. This enzyme is well characterised; both the amino acid sequence and crystal structure have been determined and a reaction mechanism has been proposed. However, the molecular basis for catalysis remains poorly understood, with only circumstantial evidence for the roles of most of the active site residues other than His8, which is phosphorylated during the reaction cycle. A vector/host expression system has been designed which allows recombinant forms of phosphoglycerate mutase to be efficiently expressed in yeast with no background wild-type activity. A simple one-column purification protocol typically yields 30 mg pure enzyme/1 l of culture. The active-site residue, His181, which is thought to be involved in proton transfer during the catalytic cycle, has been mutated to an alanine. The resultant mutant has been purified and characterised. Kinetic analysis shows a large decrease (1.6 x 10(4)) in the catalytic efficiency, and an 11-fold increase in the Km for the cofactor 2,3-bisphosphoglycerate. These observations are consistent with an integral role for His181 in the reaction mechanism of phosphoglycerate mutase, probably as a general acid or base.  (+info)

Compound heterozygosity in a complete erythrocyte bisphosphoglycerate mutase deficiency. (6/55)

Erythrocyte bisphosphoglycerate mutase (BPGM) deficiency is a rare disease associated with a decrease in 2,3-diphosphoglycerate concentration. A complete BPGM deficiency was described in 1978 by Rosa et al (J Clin Invest 62:907, 1978) and was shown to be associated with 30% to 50% of an inactive enzyme detectable by specific antibodies and resulting from an 89 Arg-->Cys substitution. The propositus' three sisters exhibited the same phenotype, while his two children had an intermediate phenotype. Samples from the family were examined using polymerase chain reaction and allele-specific oligonucleotide hybridization and sequencing techniques. Amplification of erythrocyte total RNA from the propositus' sister around the 89 mutation indicated the presence of two forms of messenger RNAs, a major form with the 89 Arg-->Cys mutation and a minor form with a normal sequence. Sequence studies of the propositus' DNA samples indicated heterozygosity at locus 89 and another heterozygosity with the deletion of nucleotide C 205 or C 206. Therefore, the total BPGM deficiency results from a genetic compound with one allele coding for an inactive enzyme (mutation BPGM Creteil I) and the other bearing a frameshift mutation (mutation BPGM Creteil II). Examination of the propositus' two children indicated that they both inherited the BPGM Creteil I mutation.  (+info)

Study of a kindred with partial deficiency of red cell 2,3-diphosphoglycerate mutase (2,3-DPGM) and compensated hemolysis. (7/55)

A kindred with partial deficiency of red cell 2,3-diphosphoglycerate mutase (2,3-DPGM) was studied. The propositus presented with indirect hyperbilirubinemia, normal hemoglobin (15.8 g/dl), and elevated reticulocyte count (4.6%). The red cell 51Cr survival was decreased (tau1/2 16 days). Incubated osmotic fragility was normal; autohemolysis was increased and corrected with glucose and ATP. The P50 was 18.5 mm Hg (normal 25.5 +/- 3), but the stability, electrophoresis, and fingerprinting of hemoglobin were normal. The concentration of 2,3-diphosphoglycerate (2,3-DPG) was reduced to 43% of normal. Red cell 2,3-DPGM was decreased to 59% of normal; 2,3-DPG phosphatase was similarly decreased. All red cell glycolytic and hexose monophosphate shunt enzymes, glycolytic intermediates other than 2,3-DPG, and glucose consumption and lactate production were normal. Five family members showed similar hematologic findings. The deficiency appears to be secondary to decreased enzyme synthesis and to be inherited as an autosomal dominant trait in this family. Partial deficiency of 2,3-DPGM should now be considered in the differential diagnosis of compensated hemolysis associated with increased oxygen affinity.  (+info)

Red cell diphosphoglycerate mutase. Immunochemical studies in vertebrate red cells, including a human variant lacking 2,3-DPG. (8/55)

Diphosphoglycerate mutase (DPGM) was purified to homogeneity from human erythrocytes. The enzyme and Freund adjuvant were injected into chickens and yielded a monospecific precipitating antibody. Radial immunodiffusion with this antibody was used to measure the amount of DPGM in hemolysates from human adult and cord red cells. Dog, rabbit, rat, chicken, and goat red cells all had DPGM during the neonatal period, but goat adult red cells had no detectable enzyme. Single bands with no spurs were present on Ouchterlony plates in which human hemolysate was placed adjacent to hemolysates from the other species tested. The amount of human red cell DPGM did not differ between young and old cells separated by centrifugation. Red cells from a patient with a DPGM genetic variant who had erythrocytosis and no detectable enzyme activity contained a reduced amount of DPGM as determined by radial immunodiffusion. The abnormal DPGM differed from normal by immunoelectrophoresis and in stability as measured by the amount of crossreacting material in young versus old erythrocytes.  (+info)

Bisphosphoglycerate mutase (BPGM) is an enzyme that plays a crucial role in the regulation of oxygen transport in red blood cells. The main function of BPGM is to convert 1,3-bisphosphoglycerate (1,3-BPG) into 2,3-bisphosphoglycerate (2,3-BPG), also known as 2,3-diphosphoglycerate (2,3-DPG).

2,3-BPG is essential for modulating the affinity of hemoglobin for oxygen. By increasing the concentration of 2,3-BPG in red blood cells, BPGM reduces the ability of hemoglobin to bind to oxygen, allowing more oxygen to be released from hemoglobin and made available to tissues, particularly under low-oxygen conditions. This is especially important for individuals living at high altitudes or those with chronic lung diseases who may have impaired oxygen transport.

Defects in the BPGM gene can lead to a rare disorder called 2,3-bisphosphoglycerate deficiency, which results in an increased affinity of hemoglobin for oxygen and reduced oxygen delivery to tissues. This condition is characterized by symptoms such as shortness of breath, fatigue, and headaches, particularly during exercise or at high altitudes.

Phosphoglycerate Mutase (PGM) is an enzyme that plays a crucial role in the glycolytic pathway, which is a metabolic process that converts glucose into pyruvate, producing ATP and NADH as energy currency for the cell.

The enzyme catalyzes the interconversion of 3-phosphoglycerate (3-PG) and 2-phosphoglycerate (2-PG), which is the ninth step in glycolysis. Specifically, PGM transfers a phosphate group from the third carbon atom to the second carbon atom of 3-PG, resulting in the formation of 2-PG and inorganic phosphate.

There are two types of Phosphoglycerate Mutase isoenzymes in humans, including:

1. Phosphoglycerate Mutase 1 (PGAM1): This is a cytosolic enzyme that is widely expressed in various tissues, including skeletal muscle, heart, brain, and liver.
2. Phosphoglycerate Mutase 2 (PGAM2): This is a muscle-specific isoenzyme that is primarily found in cardiac and skeletal muscles.

Mutations in the PGAM1 gene have been associated with hemolytic anemia, neurodevelopmental disorders, and other metabolic abnormalities, while mutations in the PGAM2 gene have been linked to myopathies and other muscle-related disorders.

Diphosphoglycerates (also known as 2,3-diphosphoglycerates or 2,3-DPG) are organic molecules found in red blood cells. They play a crucial role in regulating the affinity of hemoglobin for oxygen. Hemoglobin is the protein in red blood cells that carries oxygen from the lungs to the body's tissues.

When the concentration of diphosphoglycerates in red blood cells increases, it reduces the ability of hemoglobin to bind with oxygen, which allows more oxygen to be released into the tissues. This is particularly important in conditions where there is low oxygen availability, such as at high altitudes or in diseases that cause poor oxygen delivery to the tissues, like heart failure and chronic obstructive pulmonary disease (COPD).

In summary, diphosphoglycerates are essential molecules that help regulate hemoglobin's affinity for oxygen, ensuring optimal oxygen delivery to the body's tissues.

2,3-Diphosphoglycerate (2,3-DPG) is a molecule found in red blood cells that plays a crucial role in regulating the affinity of hemoglobin for oxygen. It is a byproduct of the glycolytic pathway, which is a series of biochemical reactions that convert glucose into energy.

In the tissues where oxygen demand is high, such as muscles and organs, 2,3-DPG concentrations are typically elevated. This molecule binds to deoxygenated hemoglobin at specific sites on the beta chains, reducing its affinity for oxygen and promoting the release of oxygen to the tissues.

Conversely, in the lungs where oxygen is abundant, 2,3-DPG concentrations are lower, allowing hemoglobin to bind more readily to oxygen and load up with oxygen for delivery to the tissues. Therefore, 2,3-DPG helps optimize the matching of oxygen supply and demand in the body.

Phosphotransferases are a group of enzymes that catalyze the transfer of a phosphate group from a donor molecule to an acceptor molecule. This reaction is essential for various cellular processes, including energy metabolism, signal transduction, and biosynthesis.

The systematic name for this group of enzymes is phosphotransferase, which is derived from the general reaction they catalyze: D-donor + A-acceptor = D-donor minus phosphate + A-phosphate. The donor molecule can be a variety of compounds, such as ATP or a phosphorylated protein, while the acceptor molecule is typically a compound that becomes phosphorylated during the reaction.

Phosphotransferases are classified into several subgroups based on the type of donor and acceptor molecules they act upon. For example, kinases are a subgroup of phosphotransferases that transfer a phosphate group from ATP to a protein or other organic compound. Phosphatases, another subgroup, remove phosphate groups from molecules by transferring them to water.

Overall, phosphotransferases play a critical role in regulating many cellular functions and are important targets for drug development in various diseases, including cancer and neurological disorders.

Methylmalonyl-CoA mutase is a mitochondrial enzyme that plays a crucial role in the metabolism of certain amino acids and fatty acids. Specifically, it catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, which is an important step in the catabolic pathways of valine, isoleucine, threonine, methionine, odd-chain fatty acids, and cholesterol.

The enzyme requires a cofactor called adenosylcobalamin (vitamin B12) for its activity. In the absence of this cofactor or due to mutations in the gene encoding the enzyme, methylmalonyl-CoA mutase deficiency can occur, leading to the accumulation of methylmalonic acid and other toxic metabolites, which can cause a range of symptoms including vomiting, dehydration, lethargy, hypotonia, developmental delay, and metabolic acidosis. This condition is typically inherited in an autosomal recessive manner and can be diagnosed through biochemical tests and genetic analysis.

Erythrocytes, also known as red blood cells (RBCs), are the most common type of blood cell in circulating blood in mammals. They are responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs.

Erythrocytes are formed in the bone marrow and have a biconcave shape, which allows them to fold and bend easily as they pass through narrow blood vessels. They do not have a nucleus or mitochondria, which makes them more flexible but also limits their ability to reproduce or repair themselves.

In humans, erythrocytes are typically disc-shaped and measure about 7 micrometers in diameter. They contain the protein hemoglobin, which binds to oxygen and gives blood its red color. The lifespan of an erythrocyte is approximately 120 days, after which it is broken down in the liver and spleen.

Abnormalities in erythrocyte count or function can lead to various medical conditions, such as anemia, polycythemia, and sickle cell disease.

Phosphoglycerate Kinase (PGK) is an enzyme that plays a crucial role in the glycolytic pathway, which is a series of reactions that convert glucose into pyruvate, producing ATP and NADH as energy-rich compounds. PGK catalyzes the conversion of 1,3-bisphosphoglycerate (1,3-BPG) to 3-phosphoglycerate (3-PG), concomitantly transferring a phosphate group to ADP to form ATP. This reaction is the fourth step in the glycolytic pathway and is reversible under certain conditions.

In humans, there are two isoforms of PGK: PGK1 and PGK2. PGK1 is widely expressed in various tissues, while PGK2 is primarily found in sperm cells. Deficiencies or mutations in the PGK1 gene can lead to a rare metabolic disorder called Phosphoglycerate Kinase Deficiency (PGKD), which can present with hemolytic anemia and neurological symptoms.

I believe there might be a slight misunderstanding in your question. "Glyceric acid" is not a widely recognized or established term in medicine or biochemistry. However, glyceric acid can refer to a specific compound with the chemical formula C3H8O4, also known as 2,3-dihydroxypropanoid acid or glycerol-3-phosphate when phosphorylated.

Glyceric acid is an organic compound that plays a crucial role in cellular metabolism, particularly in energy production pathways such as glycolysis and gluconeogenesis. It can be formed from the reduction of dihydroxyacetone phosphate (a glycolytic intermediate) or through the oxidation of glycerol.

If you were referring to a different term or concept, please provide more context so I can give a more accurate answer.

Phosphoric monoester hydrolases are a class of enzymes that catalyze the hydrolysis of phosphoric monoesters into alcohol and phosphate. This class of enzymes includes several specific enzymes, such as phosphatases and nucleotidases, which play important roles in various biological processes, including metabolism, signal transduction, and regulation of cellular processes.

Phosphoric monoester hydrolases are classified under the EC number 3.1.3 by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB). The enzymes in this class share a common mechanism of action, which involves the nucleophilic attack on the phosphorus atom of the substrate by a serine or cysteine residue in the active site of the enzyme. This results in the formation of a covalent intermediate, which is then hydrolyzed to release the products.

Phosphoric monoester hydrolases are important therapeutic targets for the development of drugs that can modulate their activity. For example, inhibitors of phosphoric monoester hydrolases have been developed as potential treatments for various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

Flatfishes are a group of marine fish characterized by having both eyes on one side of their head, which is flattened laterally. This gives them a distinctive asymmetrical appearance. They belong to the order Pleuronectiformes and include various species such as halibut, flounder, sole, and plaice. Flatfishes start their life with eyes on both sides of their head, but during development, one eye migrates to the other side of the head, a process known as metamorphosis. They are bottom-dwelling predators that rely on their excellent camouflage abilities to ambush prey.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

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.

Glycolysis is a fundamental metabolic pathway that occurs in the cytoplasm of cells, consisting of a series of biochemical reactions. It's the process by which a six-carbon glucose molecule is broken down into two three-carbon pyruvate molecules. This process generates a net gain of two ATP molecules (the main energy currency in cells), two NADH molecules, and two water molecules.

Glycolysis can be divided into two stages: the preparatory phase (or 'energy investment' phase) and the payoff phase (or 'energy generation' phase). During the preparatory phase, glucose is phosphorylated twice to form glucose-6-phosphate and then converted to fructose-1,6-bisphosphate. These reactions consume two ATP molecules but set up the subsequent breakdown of fructose-1,6-bisphosphate into triose phosphates in the payoff phase. In this second stage, each triose phosphate is further oxidized and degraded to produce one pyruvate molecule, one NADH molecule, and one ATP molecule through substrate-level phosphorylation.

Glycolysis does not require oxygen to proceed; thus, it can occur under both aerobic (with oxygen) and anaerobic (without oxygen) conditions. In the absence of oxygen, the pyruvate produced during glycolysis is further metabolized through fermentation pathways such as lactic acid fermentation or alcohol fermentation to regenerate NAD+, which is necessary for glycolysis to continue.

In summary, glycolysis is a crucial process in cellular energy metabolism, allowing cells to convert glucose into ATP and other essential molecules while also serving as a starting point for various other biochemical pathways.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme that plays a crucial role in the metabolic pathway of glycolysis. Its primary function is to convert glyceraldehyde-3-phosphate (a triose sugar phosphate) into D-glycerate 1,3-bisphosphate, while also converting nicotinamide adenine dinucleotide (NAD+) into its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has also been implicated in various non-metabolic processes, including DNA replication, repair, and transcription regulation, due to its ability to interact with different proteins and nucleic acids.

2-3 Bisphosphoglycerate in the active site of Bisphosphoglycerate Mutase. Depicted and labeled are the residues that assist in ... Bisphosphoglycerate Mutase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) EC 5.4.2.4 (Articles with ... Bisphosphoglycerate mutase (EC 5.4.2.4, BPGM) is an enzyme expressed in erythrocytes and placental cells. It is responsible for ... Ravel P, Craescu CT, Arous N, Rosa J, Garel MC (May 1997). "Critical role of human bisphosphoglycerate mutase Cys22 in the ...
Rose, Z.B.; Dube, S. (1976). "Rates of phosphorylation and dephosphorylation of phosphoglycerate mutase and bisphosphoglycerate ... Cowgill, R.W.; Pizer, L.I. (1956). "Purification and Some Properties of Phosphorylglyceric Acid Mutase from Rabbit Skeletal ... This phosphate group relocation is catalyzed by phosphoglycerate mutase, an enzyme that also catalyzes the reverse reaction. ... In glycolysis, 3-phosphoglycerate is an intermediate following the dephosphorylation (reduction) of 1,3-bisphosphoglycerate.: ...
3-bisphosphoglycerate from 1,3-bisphosphoglycerate similar to the enzyme bisphosphoglycerate mutase[citation needed]. Kinetic ... This enzyme is not to be confused with Bisphosphoglycerate mutase which catalyzes the conversion of 1,3-bisphosphoglycerate to ... Kinetics and effects of salts on the mutase and bisphosphoglycerate phosphatase activities of the enzyme from chicken breast ... 2,3-bisphosphoglycerate is required a cofactor for dPGM. In contrast, the iPGM class is independent of 2,3-bisphosphoglycerate ...
Examples of mutases include bisphosphoglycerate mutase, which appears in red blood cells and phosphoglycerate mutase, which is ... Phosphoglucomutase Methylmalonyl-CoA mutase Phosphoglycerate mutase Nelson, David; Cox, Michael (2008). Lehninger Principles of ... A mutase is an enzyme of the isomerase class that catalyzes the movement of a functional group from one position to another ... In other words, mutases catalyze intramolecular group transfers. ...
Bisphosphoglycerate mutase - Homo sapiens (Human) UniProt-Information about bisphosphoglycerate mutase A live model of the ... Through the Luebering-Rapoport pathway bisphosphoglycerate mutase catalyzes the transfer of a phosphoryl group from C1 to C2 of ... 2,3-bisphosphoglycerate, the most concentrated organophosphate in the erythrocyte, forms 3-PG by the action of ... 3-bisphosphoglycerate (2,3-BPG), which regulates oxygen release from hemoglobin and delivery to tissues. 2,3-BPG, the reaction ...
Enzymes with single-substrate mechanisms include isomerases such as triosephosphateisomerase or bisphosphoglycerate mutase, ... Such cases exist: for example, a mutase such as phosphoglucomutase catalyses the transfer of a phospho group from one position ... Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3 ...
3-Bisphosphoglycerate (1,3-BPG) 2,3-Bisphosphoglycerate (2,3-BPG) Bisphosphoglycerate mutase Bisphosphoglycerate phosphatase ...
The phosphatase subunit of bisphosphoglycerate mutase, an enzyme found in red blood cells, shows an increase in activity by up ...
3-bisphosphoglycerate, bisphosphoglycerate synthase and phosphoglycerate mutase in rabbit erythroblasts and reticulocytes in ... 3-bisphosphoglycerate, bisphosphoglycerate synthase and phosphoglycerate mutase in rabbit erythroblasts and reticulocytes in ... where bisphosphoglycerate mutase catalyzes the transfer of a phosphoryl group from C1 to C2 of 1,3-BPG, giving 2,3-BPG. 2,3-BPG ... 3-BPG generated as the high-energy carboxylic acid-phosphate mixed anhydride bond is cleaved by bisphosphoglycerate mutase. The ...
3-bisphosphoglycerate independent phosphoglycerate mutase (iPGM), and pyruvate phosphate dikinase (PPDK). Glucose-6-phosphate ...
3-bisphosphoglycerate is generated as an intermediate. While rabbit muscle phosphoglucomutase has served as the prototype for ... Low ATP reservoir in muscles Glycogen storage disease Inborn errors of carbohydrate metabolism Metabolic myopathies Mutase ... is analogous to the interconversion of 2-phosphoglycerate and 3-phosphoglycerate catalyzed by phosphoglycerate mutase, in which ...
... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 - phosphoglucomutase MeSH D08.811.399.520.750.700 - phosphoglycerate ... 2-acetolactate mutase MeSH D08.811.399.520.250 - chorismate mutase MeSH D08.811.399.520.250.500 - prephenate dehydratase MeSH ... mutase MeSH D08.811.399.894.200 - amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH D08.811.399.894. ... D08.811.399.520.250.750 - prephenate dehydrogenase MeSH D08.811.399.520.625 - methylmalonyl-coa mutase MeSH D08.811.399.520.750 ...
This step is the enzymatic transfer of a phosphate group from 1,3-bisphosphoglycerate to ADP by phosphoglycerate kinase, ... Phosphoglycerate mutase isomerises 3-phosphoglycerate into 2-phosphoglycerate. Enolase next converts 2-phosphoglycerate to ... The G3P is converted to 1,3-bisphosphoglycerate in the presence of enzyme glyceraldehyde-3-phosphate dehydrogenase (an oxido- ... 3-bisphosphoglycerate. The hydrogen is used to reduce two molecules of NAD+, a hydrogen carrier, to give NADH + H+ for each ...
3-Bisphosphoglycerate 2 × Phosphoglycerate kinase ADP ATP ADP ATP 2 × 3-Phosphoglycerate 2 × Phosphoglycerate mutase 2 × 2- ... As a consequence of bypassing this step, the molecule of ATP generated from 1-3 bisphosphoglycerate in the next reaction will ... This step is the enzymatic transfer of a phosphate group from 1,3-bisphosphoglycerate to ADP by phosphoglycerate kinase, ... Cofactors: Mg2+ Phosphoglycerate mutase isomerises 3-phosphoglycerate into 2-phosphoglycerate. Enolase next converts 2- ...
... phosphoacetylglucosamine mutase EC 5.4.2.4: bisphosphoglycerate mutase EC 5.4.2.5: phosphoglucomutase (glucose-cofactor) EC 5.4 ... 2-acetolactate mutase EC 5.4.99.4: 2-methyleneglutarate mutase EC 5.4.99.5: chorismate mutase EC 5.4.99.6: Now EC 5.4.4.2, ... phosphoenolpyruvate mutase EC 5.4.2.10: phosphoglucosamine mutase EC 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate- ... benzene mutase EC 5.4.4.2: isochorismate synthase EC 5.4.4.3: 3-(hydroxyamino)phenol mutase EC 5.4.4.4: geraniol isomerase EC ...
3-bisphosphoglycerate + ADP 1,3-bisphosphoglycerate + NAD(P)H + H+ ⇌ G3P + Pi + NAD(P)+ Triose-phosphate isomerase maintains ... Pi In gluconeogenesis 3-PG is produced by enolase and phosphoglycerate mutase acting in series PEP + H2O ⇌ 2-PG ⇌ 3-PG In the ...
3-bisphosphoglycerate phosphatase(2,3-DPG), another hydrolase which catalyzes the metabolic reaction of 2,3-bisphosphoglycerate ... In all animal tissues, 2,3-PGA is important as the cofactor of the glycolytic enzyme, phosphoglycerate mutase. More important, ...
Takahashi Y, Takahashi S, Yoshimi T, Miura T (June 1998). "Hypoxia-induced expression of phosphoglycerate mutase B in ... Phosphoglycerate kinase 1 is an enzyme involved in the conversion of 1,3-bisphosphoglycerate (1,3-BPG) to 3-phosphoglycerate (3 ... Phosphoglycerate mutase B (PGM-B) is one of the latter glycolytic enzymes responsible for the conversion of 3-phosphoglycerate ... phosphoglycerate mutase (PGM), enolase 1 (ENOA), pyruvate kinase (PK), pyruvate dehydrogenase kinase, isozyme 1 (PDK1) and ...
Phosphoglycerate mutase 2 (PGAM2), also known as muscle-specific phosphoglycerate mutase (PGAM-M), is a phosphoglycerate mutase ... 3-bisphosphoglycerate as a cofactor. Since both 3-PGA and 2-PGA are allosteric regulators of the pentose phosphate pathway (PPP ... Mutations in this gene cause muscle phosphoglycerate mutase deficiency, also known as glycogen storage disease X.[provided by ... DiMauro S, Miranda AF, Khan S, Gitlin K, Friedman R (June 1981). "Human muscle phosphoglycerate mutase deficiency: newly ...
3-bisphosphoglycerate 3-phosphatase EC 3.1.3.81: Transferred entry, now EC 3.6.1.75, diacylglycerol diphosphate phosphatase EC ... phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) EC 3.1.3.14: methylphosphothioglycerate phosphatase EC 3.1.3.15: ...
He described the role of the 2,3-bisphosphoglycerate for the anaerobic production of energy in the erythrocytes (Luebering- ... 9-19 Rapoport, S. and J. Luebering: An Optical Study Of Diphosphoglycerate Mutase (From the Children's Hospital Research ...
2-3 Bisphosphoglycerate in the active site of Bisphosphoglycerate Mutase. Depicted and labeled are the residues that assist in ... Bisphosphoglycerate Mutase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) EC 5.4.2.4 (Articles with ... Bisphosphoglycerate mutase (EC 5.4.2.4, BPGM) is an enzyme expressed in erythrocytes and placental cells. It is responsible for ... Ravel P, Craescu CT, Arous N, Rosa J, Garel MC (May 1997). "Critical role of human bisphosphoglycerate mutase Cys22 in the ...
Bisphosphoglycerate Mutase Deficiency Protects against Cerebral Malaria and Severe Malaria-Induced Anemia. In: Cell Reports. ... Bisphosphoglycerate Mutase Deficiency Protects against Cerebral Malaria and Severe Malaria-Induced Anemia. Cell Reports. 2020 ... In RBCs, bisphosphoglycerate mutase (BPGM) acts as a key allosteric regulator of hemoglobin/oxyhemoglobin. We demonstrate here ... In RBCs, bisphosphoglycerate mutase (BPGM) acts as a key allosteric regulator of hemoglobin/oxyhemoglobin. We demonstrate here ...
2,3-bisphosphoglycerate-independent phosphoglycerate mutase (GpmI). P64270. 1.53 ↑. 10. Dihydrolipoyllysine-residue ... 3-bisphosphoglycerate-independent phosphoglycerate mutase (GpmI), fructose-bisphosphate aldolase class 1 (Fda), and ...
Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate. Nat Chem Biol. 2017 Oct;13(10):1081-1087. doi: ...
d1eqja2 c.76.1.3 (A:3-76,A:311-510) 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, catalytic domain {Bacillus ... Family c.76.1.3: 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, catalytic domain [64162] (1 protein). ... Protein 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, catalytic domain [64163] (1 species). ... PDB Description: crystal structure of phosphoglycerate mutase from bacillus stearothermophilus complexed with 2- ...
3-bisphosphoglycerate-dependent phosphoglycerate mutase) and in the synthesis of biomolecules (i.e. aspartate aminotransferase ...
Phosphoglycerate/bisphosphoglycerate mutase familyprotein. 3e-34. At1g22170. phosphoglycerate/bisphosphoglycerate mutase family ... phosphoglycerate/bisphosphoglycerate mutase family protein. O.I.. C.G.. S.X.. Please select. ... phosphoglycerate/bisphosphoglycerate mutase family protein. O.I.. C.G.. S.X.. Please select. ... PGM (PHOSPHOGLYCERATE/BISPHOSPHOGLYCERATE MUTASE). O.I.. C.G.. S.X.. Please select. ...
Search results query: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. Help Hide raw data panel #pdbid,chain, ...
5.4.2.4 bisphosphoglycerate mutase - MK BRENDA: BR20; BS1170 KEGG: R01662 MetaCyc: BISPHOSPHOGLYCERATE-MUTASE-RXN ...
Phosphoglycerate mutase (InterPro:IPR013078), Phosphoglycerate/bisphosphoglycerate mutase (InterPro:IPR001345); BEST ... phosphoglycerate/bisphosphoglycerate mutase family protein; FUNCTIONS IN: catalytic activity; INVOLVED IN: metabolic process; ... phosphoglycerate/bisphosphoglycerate mutase family protein (TAIR:AT5G04120.1); Has 9399 Blast hits to 9238 proteins in 1349 ...
Phosphoglycerate/bisphosphoglycerate mutase family protein.. LOC_Os06g01950. Os06g0109200. HyperTree MR List. Protein of ...
Phosphoglycerate/bisphosphoglycerate mutase, active site IPR001345 - 0.0. - Sma3. IPR012287 - 0.0. - Sma3. IPR014778 - 0.0. - ...
Bisphosphoglycerate mutase (pmge), bisphosphoglycerate mutase (BPGM), 2,3-bisphosphoglycerate mutase (Bpgm), ... bisphosphoglycerate mutase (Bpgm), 2,3-bisphosphoglycerate mutase (bpgm), bisphosphoglycerate mutase S homeolog (bpgm.S), Ab2- ...
Phosphoglycerate mutase (InterPro:IPR013078), Phosphoglycerate/bisphosphoglycerate mutase (InterPro:IPR001345); BEST ... phosphoglycerate/bisphosphoglycerate mutase family protein; FUNCTIONS IN: catalytic activity; INVOLVED IN: metabolic process; ... phosphoglycerate/bisphosphoglycerate mutase family protein (TAIR:AT5G04120.1); Has 9399 Blast hits to 9238 proteins in 1349 ...
2,3-bisphosphoglycerate-independent phosphoglycerate mutase. NP_391271.1. BBF10K_001006. gapA. glyceraldehyde-3-phosphate ... phosphoglucosamine mutase. NP_388058.1. BBF10K_000809. glmS. glutamine--fructose-6-phosphateaminotransferase. NP_388059.1. ...
3-bisphosphoglycerate-mutase; eno (CD3170), enolase; pykF (CD3394), pyruvate kinase; fumB (CD1004), fumarate hydratase subunit ...
2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 (NCBI) 1 MMP0112 MMP0112 2,3-bisphosphoglycerate-independent ...
2,3-bisphosphoglycerate-independent phosphoglycerate mutase [1] (data from MRSA252). SACOL_RS07705. DNA-binding protein HU [1] ...
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, putative [Source:UniProtKB/TrEMBL;Acc:D0MYI9] ...
Heterozygosity for bisphosphoglycerate mutase deficiency expressing clinically as congenital erythrocytosis: A case series and ... Hb or bisphosphoglycerate mutase (BPGM) variants) or affecting oxygen-sensing pathway proteins. Here, we describe five adults ... Functional analyses showed partial BPGM deficiency, reduced 2,3-bisphosphoglycerate levels and/or increased Hb-oxygen affinity ...
2,3-bisphosphoglycerate-independent phosphoglycerate mutase [Source:UniProtKB/Swiss-Prot;Acc:G5EFZ1]. ...
bisphosphoglycerate/phosphoglycerate mutase [EC:5.4.2.4 5.4.2.11]. K02231 adenosylcobinamide kinase / adenosylcobinamide- ...
2C3-bisphosphoglycerate-independent phosphoglycerate mutase [Ensembl]. Metalloenzyme superfamily, BPG-independent PGAM N- ... ","phosphoglycero mutase III, cofactor-independent [Ensembl]. Metalloenzyme superfamily, BPG-independent PGAM N-terminus (iPGM_ ... ","3-hydroxylaminophenol mutase [Ensembl]. Glutamine synthetase [Interproscan].","protein_coding" "AKP14726","metZ","Neisseria ... ","phosphoglycerate mutase [Ensembl]. Histidine phosphatase superfamily (branch 1) [Interproscan].","protein_coding" "AEA92914 ...
3-bisphosphoglycerate-independent phosphoglycerate mutase (Phosphoglyceromutase) (BPG-independent PGAM) (iPGM) [Ensembl]. BPG- ...
Enzymes with single-substrate mechanisms include isomerases such as triosephosphateisomerase or bisphosphoglycerate mutase, ... Such cases exist: for example, a mutase such as phosphoglucomutase catalyses the transfer of a phospho group from one position ... "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase" ...
mutase 2. Alpha-enolase. Bisphosphoglycerate. mutase. Bisphosphoglycerate. mutase. Phosphoglycerate. mutase 1. ...
For example, bisphosphoglycerate mutase is given an orthology K01837, three EC numbers 5.4.2.1, 5.4.2.4 and 3.1.3.13, three R ... There is another known enzyme named phosphoglycerate mutase, which has narrower substrate specificity (only catalyzing R01518 ...
3-bisphosphoglycerate-independent phosphoglycerate mutase OS=Mesembryanthemum crystallinum","protein_coding" "Cre06.g274994"," ... ","Chorismate mutase","protein_coding" "Sro543_g163470.1","Contig1245.g11633","Seminavis robusta","Peptide chain release factor ...
  • BPGM also has a mutase and a phosphatase function, but these are much less active, in contrast to its glycolytic cousin, phosphoglycerate mutase (PGM), which favors these two functions, but can also catalyze the synthesis of 2,3-BPG to a lesser extent. (wikipedia.org)
  • 3-phosphoglycerate is converted to 2-phosphoglycerate by the enzyme phosphoglycerate mutase. (dp.ua)
  • Bisphosphoglycerate mutase (EC 5.4.2.4, BPGM) is an enzyme expressed in erythrocytes and placental cells. (wikipedia.org)
  • In RBCs, bisphosphoglycerate mutase (BPGM) acts as a key allosteric regulator of hemoglobin/oxyhemoglobin. (princeton.edu)
  • Because the main function of bisphosphoglycerate mutase is the synthesis of 2,3-BPG, this enzyme is found only in erythrocytes and placental cells. (wikipedia.org)
  • Such cases exist: for example, a mutase such as phosphoglucomutase catalyses the transfer of a phospho group from one position to another, and isomerase is a more general term for an enzyme that catalyses any one-substrate one-product reaction, such as triosephosphate isomerase . (wikipedia.org)
  • Glyceraldehyde 3-phosphate is oxidised to 1,3 bisphosphoglycerate by the enzyme glyceraldehyde 3-phosphate dehydrogenase(G-3-P dehydrogenase). (dp.ua)
  • 1,3 Bisphosphoglycerate is converted to 3-phosphoglycerate by the enzyme phosphoglycerate kinase. (dp.ua)
  • 2-3 Bisphosphoglycerate in the active site of Bisphosphoglycerate Mutase. (wikipedia.org)

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