Bisphosphoglycerate Mutase: 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.Phosphoglycerate Mutase: An enzyme that catalyzes the conversion of 2-phospho-D-glycerate to 3-phospho-D-glycerate. EC 5.4.2.1.Diphosphoglyceric Acids2,3-Diphosphoglycerate: 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)Phosphotransferases: 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.Methylmalonyl-CoA Mutase: 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.Erythrocytes: Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.Phosphoglycerate Kinase: 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 AcidsPhosphoric Monoester Hydrolases: A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.Flatfishes: 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.Molecular Sequence Data: 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.Amino Acid Sequence: 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.Glycolysis: 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.Glyceraldehyde-3-Phosphate Dehydrogenases: 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.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Placenta: A highly vascularized mammalian fetal-maternal organ and major site of transport of oxygen, nutrients, and fetal waste products. It includes a fetal portion (CHORIONIC VILLI) derived from TROPHOBLASTS and a maternal portion (DECIDUA) derived from the uterine ENDOMETRIUM. The placenta produces an array of steroid, protein and peptide hormones (PLACENTAL HORMONES).Trophoblasts: Cells lining the outside of the BLASTOCYST. After binding to the ENDOMETRIUM, trophoblasts develop into two distinct layers, an inner layer of mononuclear cytotrophoblasts and an outer layer of continuous multinuclear cytoplasm, the syncytiotrophoblasts, which form the early fetal-maternal interface (PLACENTA).Chorionic Villi: The threadlike, vascular projections of the chorion. Chorionic villi may be free or embedded within the DECIDUA forming the site for exchange of substances between fetal and maternal blood (PLACENTA).Geobacillus stearothermophilus: A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Thymol: A phenol obtained from thyme oil or other volatile oils used as a stabilizer in pharmaceutical preparations, and as an antiseptic (antibacterial or antifungal) agent. It was formerly used as a vermifuge.Hot Temperature: Presence of warmth or heat or a temperature notably higher than an accustomed norm.Listeria monocytogenes: A species of gram-positive, rod-shaped bacteria widely distributed in nature. It has been isolated from sewage, soil, silage, and from feces of healthy animals and man. Infection with this bacterium leads to encephalitis, meningitis, endocarditis, and abortion.Monoterpenes: Compounds with a core of 10 carbons generally formed via the mevalonate pathway from the combination of 3,3-dimethylallyl pyrophosphate and isopentenyl pyrophosphate. They are cyclized and oxidized in a variety of ways. Due to the low molecular weight many of them exist in the form of essential oils (OILS, VOLATILE).Oils, Volatile: Oils which evaporate readily. The volatile oils occur in aromatic plants, to which they give odor and other characteristics. Most volatile oils consist of a mixture of two or more TERPENES or of a mixture of an eleoptene (the more volatile constituent of a volatile oil) with a stearopten (the more solid constituent). The synonym essential oils refers to the essence of a plant, as its perfume or scent, and not to its indispensability.Refrigeration: The mechanical process of cooling.Listeria: A genus of bacteria which may be found in the feces of animals and man, on vegetation, and in silage. Its species are parasitic on cold-blooded and warm-blooded animals, including man.Plasmodium vivax: A protozoan parasite that causes vivax malaria (MALARIA, VIVAX). This species is found almost everywhere malaria is endemic and is the only one that has a range extending into the temperate regions.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.Malaria, Vivax: Malaria caused by PLASMODIUM VIVAX. This form of malaria is less severe than MALARIA, FALCIPARUM, but there is a higher probability for relapses to occur. Febrile paroxysms often occur every other day.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.BooksPublishing: "The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.MEDLINE: The premier bibliographic database of the NATIONAL LIBRARY OF MEDICINE. MEDLINE® (MEDLARS Online) is the primary subset of PUBMED and can be searched on NLM's Web site in PubMed or the NLM Gateway. MEDLINE references are indexed with MEDICAL SUBJECT HEADINGS (MeSH).Polyphosphates: Linear polymers in which orthophosphate residues are linked with energy-rich phosphoanhydride bonds. They are found in plants, animals, and microorganisms.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Dinucleoside Phosphates: A group of compounds which consist of a nucleotide molecule to which an additional nucleoside is attached through the phosphate molecule(s). The nucleotide can contain any number of phosphates.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Rutamycin: A macrolide antibiotic of the oligomycin group, obtained from Streptomyces rutgersensis. It is used in cytochemistry as a tool to inhibit various ATPases and to uncouple oxidative phosphorylation from electron transport and also clinically as an antifungal agent.Phosphates: Inorganic salts of phosphoric acid.Two-Dimensional Difference Gel Electrophoresis: Methods of comparing two or more samples on the same two-dimensional gel electrophoresis gel.Droughts: Prolonged dry periods in natural climate cycle. They are slow-onset phenomena caused by rainfall deficit combined with other predisposing factors.Proteome: The protein complement of an organism coded for by its genome.Electrophoresis, Gel, Two-Dimensional: Electrophoresis in which a second perpendicular electrophoretic transport is performed on the separate components resulting from the first electrophoresis. This technique is usually performed on polyacrylamide gels.Proteomics: The systematic study of the complete complement of proteins (PROTEOME) of organisms.Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization: A mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis.Water: A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Camels: Hoofed mammals with four legs, a big-lipped snout, and a humped back belonging to the family Camelidae.Fibroblast Growth Factor 2: A single-chain polypeptide growth factor that plays a significant role in the process of WOUND HEALING and is a potent inducer of PHYSIOLOGIC ANGIOGENESIS. Several different forms of the human protein exist ranging from 18-24 kDa in size due to the use of alternative start sites within the fgf-2 gene. It has a 55 percent amino acid residue identity to FIBROBLAST GROWTH FACTOR 1 and has potent heparin-binding activity. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages. It was originally named basic fibroblast growth factor based upon its chemical properties and to distinguish it from acidic fibroblast growth factor (FIBROBLAST GROWTH FACTOR 1).Fibroblast Growth Factors: A family of small polypeptide growth factors that share several common features including a strong affinity for HEPARIN, and a central barrel-shaped core region of 140 amino acids that is highly homologous between family members. Although originally studied as proteins that stimulate the growth of fibroblasts this distinction is no longer a requirement for membership in the fibroblast growth factor family.Receptors, Fibroblast Growth Factor: Specific molecular sites or structures on cell membranes that react with FIBROBLAST GROWTH FACTORS (both the basic and acidic forms), their analogs, or their antagonists to elicit or to inhibit the specific response of the cell to these factors. These receptors frequently possess tyrosine kinase activity.Fibroblast Growth Factor 1: A 17-kDa single-chain polypeptide growth factor that plays a significant role in the process of WOUND HEALING and is a potent inducer of PHYSIOLOGIC ANGIOGENESIS. It binds to HEPARIN, which potentiates its biological activity and protects it from proteolysis. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages, and also has chemotactic and mitogenic activities. It was originally named acidic fibroblast growth factor based upon its chemical properties and to distinguish it from basic fibroblast growth factor (FIBROBLAST GROWTH FACTOR 2).Receptor, Fibroblast Growth Factor, Type 1: A fibroblast growth factor receptor with specificity for FIBROBLAST GROWTH FACTORS; HEPARAN SULFATE PROTEOGLYCAN; and NEURONAL CELL ADHESION MOLECULES. Several variants of the receptor exist due to multiple ALTERNATIVE SPLICING of its mRNA. Fibroblast growth factor receptor 1 is a tyrosine kinase that transmits signals through the MAP KINASE SIGNALING SYSTEM.Receptor, Fibroblast Growth Factor, Type 2: A fibroblast growth factor receptor that is found in two isoforms. One receptor isoform is found in the MESENCHYME and is activated by FIBROBLAST GROWTH FACTOR 2. A second isoform of fibroblast growth factor receptor 2 is found mainly in EPITHELIAL CELLS and is activated by FIBROBLAST GROWTH FACTOR 7 and FIBROBLAST GROWTH FACTOR 10. Mutation of the gene for fibroblast growth factor receptor 2 can result in craniosynostotic syndromes (e.g., APERT SYNDROME; and CROUZON SYNDROME).

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)

2,3-Bisphosphoglycerate mutase (2,3-BPGM), an erythroid-expressed enzyme, synthesises 2,3-bisphosphoglycerate (2,3-BPG), the allosteric modulator of haemoglobin. This ligand has a higher affinity for adult haemoglobin than for fetal haemoglobin and differential binding of it facilitates transfer of oxygen between adult and fetal blood by lowering the affinity of adult haemoglobin for oxygen. This paper reports the discovery that 2,3-BPGM is synthesised in non-erythroid cells of the human placenta. Western blot analysis of placental extracts revealed high levels of 2,3-BPGM in the human placenta. Immunohistochemical staining and in situ hybridisation experiments indicated that abundant 2,3-BPGM is present in the syncytiotrophoblast layer of the placental villi at the feto-maternal interface. A cytochemical staining technique showed that the placental 2,3-BPGM is active, indicating that 2,3-BPG is synthesised in the outermost cells of the placenta. These observations demonstrate an unexpected and abundant
Kit Component:- KN302227G1, Bpgm gRNA vector 1 in pCas-Guide vector- KN302227G2, Bpgm gRNA vector 2 in pCas-Guide vector- KN302227D, donor vector…
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Here again is a potential limiting factor for this pathway. The continuation of the reaction depends upon the availability of the oxidized form of the electron carrier, NAD+. Thus, NADH must be continuously oxidized back into NAD+ in order to keep this step going. If NAD+ is not available, the second half of glycolysis slows down or stops. If oxygen is available in the system, the NADH will be oxidized readily, though indirectly, and the high-energy electrons from the hydrogen released in this process will be used to produce ATP. In an environment without oxygen, an alternate pathway (fermentation) can provide the oxidation of NADH to NAD+.. Step 7. In the seventh step, catalyzed by phosphoglycerate kinase (an enzyme named for the reverse reaction), 1,3-bisphosphoglycerate donates a high-energy phosphate to ADP, forming one molecule of ATP. (This is an example of substrate-level phosphorylation.) A carbonyl group on the 1,3-bisphosphoglycerate is oxidized to a carboxyl group, and ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
2019年10月10日,上海交通大學醫學院藥理學與化學生物學系沈瑛副研究員課題組聯合復旦大學藥學院周璐副教授和上海中醫藥大學陳紅專教授在Cell Metabolism 雜志發表長文"A novel allosteric inhibitor of phosphoglycerate mutase 1 suppresses growth and metastasis of non-small cell lung cancer",率先報道磷酸甘油酸變位酶1(phosphoglycerate mutase 1, PGAM1)新型別構抑制劑對非小細胞肺癌的增殖、耐藥和轉移等生物學活性的多重抑制作用,揭示通過別構調節PGAM1同時干預PGAM1的代謝酶活性和非代謝酶依賴的蛋白-蛋白相互作用的抗腫瘤藥理學新機制。 ...
HEADER ISOMERASE 19-JUL-00 1E59 TITLE E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE COMPLEXED TITLE 2 WITH VANADATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHOSPHOGLYCERATE MUTASE; COMPND 3 CHAIN: A; COMPND 4 EC: 5.4.2.1; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 83333; SOURCE 4 STRAIN: K12; SOURCE 5 GENE: PGM1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3A KEYWDS INHIBITOR, VANDATE, GLYCOLYSIS AND GLUCONEOGENESIS, KEYWDS 2 PHOSPHOGLYCERATE MUTASE, ISOMERASE EXPDTA X-RAY DIFFRACTION AUTHOR C.S.BOND,W.N.HUNTER REVDAT 3 24-FEB-09 1E59 1 VERSN REVDAT 2 15-MAR-02 1E59 1 JRNL REVDAT 1 05-FEB-02 1E59 0 JRNL AUTH C.S.BOND,M.WHITE,W.N.HUNTER JRNL TITL MECHANISTIC IMPLICATIONS FOR ESCHERICHIA COLI JRNL TITL 2 COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE BASED JRNL TITL 3 ON THE HIGH-RESOLUTION CRYSTAL ...
GT:ID BAD56223.1 GT:GENE BAD56223.1 GT:PRODUCT putative phosphoglycerate mutase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 1542838..1543497 GB:FROM 1542838 GB:TO 1543497 GB:DIRECTION + GB:PRODUCT putative phosphoglycerate mutase GB:PROTEIN_ID BAD56223.1 LENGTH 219 SQ:AASEQ MSKYAGVRTLILLRHGQTEWNATDRMQGQIDTDLTELGRRQAKEAARELVSRNAIAIVSSDLRRAHDTALALAEHTDVPVALDPRLRETHLGDWQGLTHLEVDADYPGARVAWRLDATYRPPGGESKLEVGARALPVVRELYNERQDWPGRTIILVAHGGLIAALTAALLELPPQNWPALGGLANTSWVQLSSHGPGIDQPGWRLDVWNAAAKVAPDVL GT:EXON 1,1-219:0, BL:SWS:NREP 1 BL:SWS:REP 8-,136,GPMA_NITWN,4e-19,42.6,129/207, PROS 12-,21,PS00175,PG_MUTASE,PDOC00158, SEG 157-,172,ahggliaaltaallel, BL:PDB:NREP 1 BL:PDB:REP 9-,156,1h2eA,2e-22,40.0,145/207, RP:PDB:NREP 1 RP:PDB:REP 8-,209,1ebbA,8e-30,32.0,194/202, RP:PFM:NREP 1 RP:PFM:REP 10-,156,PF00300,2e-23,45.8,144/158,PGAM, HM:PFM:NREP 1 HM:PFM:REP 9-,165,PF00300,3.7e-45,40.0,155/158,PGAM, RP:SCP:NREP 1 RP:SCP:REP 8-,209,1ebbA,3e-30,32.0,194/202,c.60.1.1, HM:SCP:REP ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
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1E59: Mechanistic Implications for Escherichia Coli Cofactor-Dependent Phosphoglycerate Mutase Based on the High-Resolution Crystal Structure of a Vanadate Complex.
cjk:jk1912 K01834 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11] , (GenBank) gpmA; phosphoglycerate mutase (A) MSEQNNSHGNLILLRHGQSEWNASNQFTGWVDVRLTEKGRAEAVRGGEMIKEAGLEPTIL YTSLLRRAITTANIALDAADRHWIPVVRDWRLNERHYGALQGLNKAETKDKYGEEQFMAW RRSYDTPPPAIDADNEYAQTNDPRYADLSEIPATECLLDVVKRFIPYYEEEIEPRVKNGE TVLVAAHGNSLRALVKHLDKISDEDIAGLNIPTGIPLVYNIDADGKVLNPGGDYLDPEAA AAGAAAVAAQGQAK ...
At least five mutations in the PGAM2 gene have been found to cause phosphoglycerate mutase deficiency. The most common of these mutations, written as Trp78Ter or W78X, replaces the protein building block (amino acid) tryptophan with a premature stop signal in the instructions for making phosphoglycerate mutase. This mutation results in the production of an abnormally short, nonfunctional version of the enzyme. Other mutations change single amino acids in phosphoglycerate mutase.. Mutations in the PGAM2 gene greatly reduce the activity of phosphoglycerate mutase, which disrupts energy production in skeletal muscle cells. This defect underlies the muscle cramping, muscle breakdown, and related signs and symptoms that occur following strenuous exercise in affected individuals. ...
Definition of Phosphoglyceromutase with photos and pictures, translations, sample usage, and additional links for more information.
The protein encoded by this gene is a mutase that catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2015 ...
gpmA; highly similar to 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase from Klebsiella pneumoniae subsp. pneumoniae strain ATCC 700721 - MGH 78578 (sp,A6T6I3); K01834 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11] ...
Glyceraldehyde-3-phosphate dehydrogenase (NADP+)(phosphorylating); Involved in the photosynthetic carbon assimilation. Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phos [...] (337 aa ...
K01834 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11] , (GenBank) gpmA; 2,3-bisphosphoglycerate-dependent phosphoglycerate ...
Phosphoglycerate mutase deficiency is a disorder that primarily affects muscles used for movement (skeletal muscles). Beginning in childhood or adolescence, affected individuals experience muscle aches or cramping following strenuous physical activity. Some people with this condition also have recurrent episodes of myoglobinuria. Myoglobinuria occurs when muscle tissue breaks down abnormally and releases a protein called myoglobin, which is processed by the kidneys and released in the urine. If untreated, myoglobinuria can lead to kidney failure.. In some cases of phosphoglycerate mutase deficiency, microscopic tube-shaped structures called tubular aggregates are seen in muscle fibers. It is unclear how tubular aggregates are associated with the signs and symptoms of the disorder. ...
Proliferating cells, including cancer cells, obtain serine both exogenously and via the metabolism of glucose. By catalyzing the first, rate-limiting step in the synthesis of serine from glucose, phosphoglycerate dehydrogenase (PHGDH) controls flux through the biosynthetic pathway for this important amino acid and represents a putative target in oncology. To discover inhibitors of PHGDH, a coupled biochemical assay was developed and optimized to enable high-throughput screening for inhibitors of human PHGDH. Feedback inhibition was minimized by coupling PHGDH activity to two downstream enzymes (PSAT1 and PSPH), providing a marked improvement in enzymatic turnover. Further coupling of NADH to a diaphorase/resazurin system enabled a red-shifted detection readout, minimizing interference due to compound autofluorescence. With this protocol, over 400,000 small molecules were screened for PHGDH inhibition, and following hit validation and triage work, a piperazine-1-thiourea was identified. Following ...
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The cellular environment presents a protein with many small molecules with which it may interact. Many novel interactions between proteins and non-substrate metabolites are being uncovered through proteome-wide screens. The homodimeric Escherichia coli cofactor-dependant phosphoglycerate mutase (dPGM) was identified as an ATP binding protein in a proteome-wide screen, but dPGM does not use ATP for catalysis. This dissertation elucidates the effect of ATP and other non-substrate metabolites on dPGM. Initial investigations revealed a partially unfolded, monomeric intermediate of dPGM that forms during equilibrium unfolding. ATP binding was found to occur at the active site of dPGM and to be energetically coupled with dimerization; ligand binding events reduce the population of intermediate. An investigation into the structure of the dPGM intermediate revealed a cooperative folding unit that couples the active site and dimer interface of dPGM. By coupling the two binding sites, the cooperative unit is
• The carbon dioxide gas is temporarily converted to carbonic acid in red blood cells by the enzyme carbonic anhydrase, and then further converted to hydrogen and bicarbonate ions. • The result of increased carbon dioxide is decreased pH causing the Bohr effect. • Elevated carbon dioxide levels enhance unbinding of oxygen from oxyhemoglobin thereby making oxygen available for actively metabolizing cells. • By contrast, decreased carbon dioxide, as in the alveolar spaces, increases affinity of hemoglobin for oxygen and promotes oxygen loading and transport. • To a limited degree, changes in temperature affect the association and dissociation of O2 with hemoglobin. • The oxygen carrying ability of hemoglobin is unaffected by normal temperatures. • Near metabolically active cells, blood temperature rises, increasing the thermal motion of molecules which promotes the unloading of O2 to continue fueling aerobic metabolism in the tissue cells. • When temperature lowers,
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase from Burkholderia pseudomallei: We present here an ensemble of structures solved by the Seattle Structural Genomics Center for Infectious Disease (SSGCID) of 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, or PGAM, from Burkholderia pseudomallei, a pathogen which causes the serious skin infection melioidosis.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
1. We have purified membrane-associated Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphatases from bovine testis and human erythrocytes by chromatography on several media, including a novel 2,3-bisphosphoglycerate affinity column. 2. The enzymes have apparent molecular masses of 42 kDa (testis) and 70 kDa (erythrocyte), as determined by SDS/PAGE, and affinities for Ins(1,4,5)P3 of 14 microM and 22 microM respectively. 3. The two enzymes hydrolyse both Ins(1,4,5)P3 and Ins(1,3,4,5)P4 and are therefore type I Ins(1,4,5)P3 5-phosphatases [nomenclature of Hansen, Johanson, Williamson and Williamson (1987) J. Biol. Chem. 262, 17319-17326]. 4. On chromatofocusing, the partially purified testicular enzyme migrates as two peaks of activity, with pI values of about 5.8 and 5.5. The erythrocyte enzyme exhibits only the latter peak. 5. The testis 5-phosphatase is labile at 37 degrees C, but its activity can be maintained in the presence of 50 mM phorbol dibutyrate (PdBu). After PdBu treatment, a third form of the ...
Pgam2 - Pgam2 (Myc-DDK-tagged ORF) - Rat phosphoglycerate mutase 2 (muscle) (Pgam2), (10 ug) available for purchase from OriGene - Your Gene Company.
Nonalcoholic fatty liver organ disease (NAFLD) is normally a significant health burden in the ageing society with an urging medical need for a better understanding of the underlying mechanisms. and middle\aged mice developed fatty liver, but not adolescent mice. Extra MK-4827 fat accumulation was negatively correlated with an age\related reduction in mitochondrial mass and aggravated by a reduced capacity of fatty acid oxidation in high extra fat\fed mice. Irrespective of age, high fat diet improved ROS production in hepatic mitochondria associated with a balanced nuclear element erythroid\derived 2 like 2 (NFE2L2) dependent antioxidative response, most likely triggered by reduced tethering of NFE2L2 to mitochondrial phosphoglycerate mutase 5. Age indirectly affected mitochondrial function by reducing mitochondrial mass, therefore exacerbating diet\induced extra fat build up. Therefore, consideration of age in metabolic studies must be emphasized. Keywords: Age, diet\induced obesity, fatty acid ...
This gene encodes a protein that contains a ubiquitin associated domain at the N-terminus, an SH3 domain, and a C-terminal domain with similarities to the catalytic motif of phosphoglycerate mutase. The encoded protein was found to inhibit endocytosis of epidermal growth factor receptor (EGFR) and platelet-derived growth factor receptor. Sequence Note: The RefSeq transcript and protein were derived from transcript and genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments ...
Mouse polyclonal Methylmalonyl Coenzyme A mutase antibody validated for WB, IHC, ICC/IF and tested in Human and Rat. Referenced in 2 publications and 1…
In order for Candida species to adhere and colonize human host cells they must express cell wall proteins (CWP) and adapt to reactive oxygen species (ROS) generated by phagocytic cells of the human host during the respiratory burst. However, how these pathogens change the expression of CWP in response to oxidative stress (OSR) is not known. Here, fifteen moonlight-like CWP were identified that expressed differentially in four species of Candida after they were exposed to H2O2 or menadione (O2(-)). These proteins included: (i) glycolytic enzymes, such as glyceraldehyde-3-phosphate dehydrogenase (Gapdh), fructose-bisphosphate aldolase (Fba1), phosphoglycerate mutase (Gpm1), phosphoglycerate kinase (Pgk), pyruvate kinase (Pk) and enolase (Eno1); (ii) the heat shock proteins Ssb1 and Ssa2; (iii) OSR proteins such as peroxyredoxin (Tsa1), the stress protein Ddr48 (Ddr48) and glutathione reductase (Glr1); (iv) other metabolic enzymes such as ketol-acid reductoisomerase (Ilv5) and pyruvate ...
Recombinant Phosphoglycerate Kinase 2 (PGK2) Protein (His tag). Species: Human. Source: Escherichia coli (E. coli). Order product ABIN1981682.
Now the enzyme that catalyse these ten reactions are: hexokinase phosphoglucose isomerase phosphofructokinase aldolase triose phosphate isomerase glyceraldehyde-3-phosphate dehydrogenase phosphoglycerate kinase phosphoglycerate mutase enolase pyruvate kinase Done. BOOM!!!!!!!!!!!!!!!!!!! :D
Methylmalonyl Coenzyme A mutase Lysates available through Novus Biologicals. Browse our Methylmalonyl Coenzyme A mutase Lysate catalog backed by our Guarantee+.
Incubation of human erythrocytes in medium containing inosine (10 mM), pyruvate (10 mM), phosphate (50 mM) and NaCl (75 mM) at pH 6.6 leads to a more than 1000-fold increase in the concentration of 5-phosphoribosyl 1-pyrophosphate (PRPP), as identified and quantified by 31P-n.m.r. spectroscopy. The accumulation is highly pH-dependent, with a maximum at extracellular pH 6.60, and the maximum value of 1.3-1.6 mmol/l of erythrocytes is attained within 1 h at 37 degrees C. PRPP was accumulated despite high concentrations of 2,3-bisphosphoglycerate (2,3-BPG), an inhibitor of PRPP synthetase. The concentration of PRPP correlated with the intracellular concentration of inorganic phosphate (Pi). Substitution of either adenosine or adenosine plus inosine for inosine in the medium did not lead to 31P-n.m.r.-detectable accumulation of PRPP. These results show that neither 2,3-BPG nor PRPP itself inhibits the synthesis of PRPP in the human erythrocyte. Adenosine, however, prevents the inosine-stimulated ...
Cancer of the gingivo-buccal complex (GBC) is a major cancer in Indian men. This study reports the identification of tumor antigens, which elicit an antibody response in cancer of GBC using immunoproteomics. Proteins from KB cells separated by 2-D PAGE, were immunoblotted with IgG from sera of 28 cancer patients, 12 patients with leukoplakia, and 28 healthy individuals. Antigens detected by the IgGs from the patients sera were different among different individuals with presence of any single antigen ranging from 7 to 79%. Several of these antigens have been identified by MS and confirmed by immunostaining. They are three forms of α-enolase, peroxiredoxin-VI, annexin-II, HSP70, pyruvate kinase, α-tubulin, β-tubulin, ATP-synthase, phosphoglycerate mutase (PGM), aldose reductase, triosephosphate isomerase, and cyclophilin-A. Except, HSP70, these antigens are being reported in cancer of GBC for the first time. Pyruvate kinase and aldose reductase have not been reported to elicit autoantibody ...
Phosphoglycerate Phosphokinase antibody LS-C147605 is a biotin-conjugated rabbit polyclonal antibody to yeast Phosphoglycerate Phosphokinase. Validated for ELISA, IF, IHC and WB.
The Phosphoglycerate Kinase 1 is a glycolytic enzyme that catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. The encoded protein may also act as a cofactor for polymerase alpha. This gene lies on the X-chromosome, while a related pseudogene also has been found on the X-chromosome and another on chromosome 19.PGK1 is distinguished from testicular PGK2, which maps to chromosome 6p21. The deduced protein contains 417 amino acid residues. Southern blot analysis of human genomic DNAs showed a complex pattern of hybridizing fragments, 2 of which were non-X in origin. The results were interpreted as reflecting the existence of a small family of dispersed PGK or PGK-like genes.
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, ... Escherichia coli Aspartate Transcarbamoylase versus Yeast Chorismate Mutase". Microbiol. Mol. Biol. Rev. 65 (3): 404-21, table ...
... bisphosphoglycerate synthase and phosphoglycerate mutase in rabbit erythroblasts and reticulocytes in vivo". Unitat de ... González-Cinca N, Pérez de la Ossa P, Carreras J, Climent F."Effects of thyroid hormone and hypoxia on 2,3-bisphosphoglycerate ...
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, a metabolite in glycolysis 2,3-Bisphosphoglycerate regulates hemoglobin Bisphosphoglycerate mutase, an ... which has an FAA location identifier of BPG Bisphosphoglycerate, a molecule with two biologically important isomers: 1, ... enzyme which converts the former into the latter Bisphosphoglycerate phosphatase, an enzyme which acts on the latter Blocks Per ...
... 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 EC ... 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 ... isobutyryl-CoA mutase EC 5.4.99.14: 4-carboxymethyl-4-methylbutenolide mutase EC 5.4.99.15: (1→4)-a-D-glucan 1-a-D- ...
... may refer to: 1,3-Bisphosphoglycerate 2,3-Bisphosphoglycerate Bisphosphoglycerate mutase ...
Examples of this are bisphosphoglycerate mutase, which appears in red blood cells and phosphoglycerate mutase, which acts in ... A mutase is an enzyme of the isomerase class that catalyzes the shifting of a functional group from one position to another ... Phosphoglucomutase Methylmalonyl-CoA mutase Wikipedia:MeSH_D08#MeSH_D08.811.399.520_---_intramolecular_transferases_.28EC_5.4. ... In particular it moves phosphate groups within a single molecule, for instance: phosphoglycerate mutase. ...
3-bisphosphoglycerate from 1,3-bisphosphoglycerate similar to the enzyme bisphosphoglycerate mutase. Kinetic and structural ... 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 ...
... (BPGM) is an enzyme unique to erythrocytes and placental cells. It is responsible for the catalytic ... Bisphosphoglycerate Mutase at the US National Library of Medicine Medical Subject Headings (MeSH) EC 5.4.2.4. ... Ravel P, Craescu CT, Arous N, Rosa J, Garel MC (May 1997). "Critical role of human bisphosphoglycerate mutase Cys22 in the ... Because the main function of bisphosphoglycerate mutase is the synthesis of 2,3-BPG, this enzyme is found only in erythrocytes ...
For example, the secondary structure of the chorismate mutase of yeast is very similar to that of E. coli. Chorimate mutase in ... In enzymology, chorismate mutase (EC 5.4.99.5) is an enzyme that catalyzes the chemical reaction for the conversion of ... Chorismate mutase is found at a branch point in the pathway. The enzyme channels the substrate, chorismate to the biosynthesis ... The presence of chorismate mutase increases the rate of the reaction a million fold.[6] In the absence of enzyme catalysis this ...
Bisphosphoglycerate mutase. *v. *t. *e. Common for blood tests (CPT 82000-84999) ...
Bisphosphoglycerate mutase. *v. *t. *e. Hydrolase: esterases (EC 3.1). 3.1.1: Carboxylic. ester hydrolases. *Cholinesterase * ...
Bisphosphoglycerate mutase. This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.. *v ...
Bisphosphoglycerate mutase. Retrieved from "https://en.wikipedia.org/w/index.php?title=Cori_cycle&oldid=861368539" ...
Bisphosphoglycerate mutase. *BK channel. *Bombesin-like peptides. *Bombinin. *Bone morphogenetic protein receptor ...
3-bisphosphoglycerate is generated as an intermediate. While rabbit muscle phosphoglucomutase has served as the prototype for ... PGM5 mutase Beta-phosphoglucomutase Jagannathan, V; Luck, JM (1949). "Phosphoglucomutase; mechanism of action". Journal of ... 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 --- ... 2-acetolactate mutase MeSH D08.811.399.520.250 --- chorismate mutase MeSH D08.811.399.520.250.500 --- prephenate dehydratase ... phosphoglycerate mutase MeSH D08.811.399.894.200 --- amino acid isomerases MeSH D08.811.399.894.200.200 --- alanine racemase ... MeSH D08.811.399.520.250.750 --- prephenate dehydrogenase MeSH D08.811.399.520.625 --- methylmalonyl-coa mutase MeSH D08.811. ...
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- ...
... (acetyl coenzyme A) is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid metabolism.[1] Its main function is to deliver the acetyl group to the citric acid cycle (Krebs cycle) to be oxidized for energy production. Coenzyme A (CoASH or CoA) consists of a β-mercaptoethylamine group linked to the vitamin pantothenic acid through an amide linkage [2] and 3'-phosphorylated ADP. The acetyl group (indicated in blue in the structural diagram on the right) of acetyl-CoA is linked to the sulfhydryl substituent of the β-mercaptoethylamine group. This thioester linkage is a "high energy" bond, which is particularly reactive. Hydrolysis of the thioester bond is exergonic (−31.5 kJ/mol). CoA is acetylated to acetyl-CoA by the breakdown of carbohydrates through glycolysis and by the breakdown of fatty acids through β-oxidation. Acetyl-CoA then enters the citric acid cycle, where the acetyl group is oxidized to carbon dioxide and water, and the energy ...
... (3PG) is the conjugate acid of glycerate 3-phosphate (GP). The glycerate is a biochemically significant metabolic intermediate in both glycolysis and the Calvin cycle. This anion is often termed PGA when referring to the Calvin cycle. In the Calvin cycle, 3-phosphoglycerate is the product of the spontaneous scission of an unstable 6-carbon intermediate formed upon CO2 fixation. Thus, two equivalents of 3-phosphoglycerate are produced for each molecule of CO2 that is fixed.[1][2] ...
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1,3-Bisphosphoglycerate 1,3BPG Glycerate-1,3-bisphosphate,. glycerate-1,3-diphosphate,. 1,3-diphosphoglycerate PGAP, BPG, DPG ... Phosphoglycerate mutase isomerises 3-phosphoglycerate into 2-phosphoglycerate. 2-phosphoglycerate (2PG) enolase (ENO). a lyase ... 1,3-bisphosphoglycerate (1,3BPG) phosphoglycerate kinase (PGK). a transferase 3-phosphoglycerate (3PG) ... Glyceraldehyde-3-phosphate2− + Pi2− + NAD+ → 1,3-Bisphosphoglycerate4− + NADH + H+. 6.30 -1.29 ...
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, ...
1,3-Bisphosphoglycerate NAD+ + Pi NADH + H+ + 2 2 Phosphoglycerate kinase 3-Phosphoglycerate Phosphoglycerate mutase 2- ...
3-bisphosphoglycerate (2,3-BPG), the allosteric modulator of haemoglobin. This ligand has a higher affinity for adult ... 3-Bisphosphoglycerate mutase (2,3-BPGM), an erythroid-expressed enzyme, synthesises 2, ... 2,3-Bisphosphoglycerate mutase (2,3-BPGM), an erythroid-expressed enzyme, synthesises 2,3-bisphosphoglycerate (2,3-BPG), the ... Bisphosphoglycerate Mutase, Blotting, Western, Female, Humans, Immunohistochemistry, In Situ Hybridization, Placenta, RNA, ...
Insights Into the Catalytic Mechanism of Cofactor-Independent Phosphoglycerate Mutase from X-Ray Crystallography, Simulated ... 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE A 511 Geobacillus stearothermophilus EC#: 5.4.2.12 IUBMB Mutation: ... 1.4A CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED WITH 2-PHOSPHOGLYCERATE. *DOI: ...
Mechanistic Implications for Escherichia Coli Cofactor-Dependent Phosphoglycerate Mutase Based on the High-Resolution Crystal ... 2 3 Bisphosphoglycerate Dependent Phosphoglycerate Mutase Activity * Gluconeogenesis * Glycolytic Process * Metabolic Process ... Phosphoglycerate mutase-like Phosphoglycerate mutase-like Cofactor-dependent phosphoglycerate mutase Phosphoglycerate mutase ...
Short name: PG/BPGM_mutase_AS Description. Phosphoglycerate mutase (EC:5.4.2.1) (PGAM) and bisphosphoglycerate mutase (EC:5.4. ... Molecular cloning and nucleotide sequence of murine 2,3-bisphosphoglycerate mutase cDNA.. Biochem. Biophys. Res. Commun. 156 ... Intermediates in the phosphoglycerate mutase and bisphosphoglycerate synthase reactions.. Meth. Enzymol. 87 42-51 1982 ... Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae.. FEBS Lett. 229 383-7 1988 ...
Species: Phosphoglycerate/bisphosphoglycerate mutase, active site (IPR001345). Key Species. Key species. Number of proteins. ...
3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM). When BPGM is knocked out, 1,3-BPG can directly ... Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate.. Oslund RC1, Su X2, Haugbro M1, Kee JM1, ... Phosphoglycerate mutase 1 (PGAM1) catalyzes the isomerization of 3-PG into the downstream glycolytic intermediate 2- ... We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the ...
Bisphosphoglycerate mutase (BPGM) is an enzyme unique to erythrocytes and placental cells. It is responsible for the catalytic ... Bisphosphoglycerate Mutase at the US National Library of Medicine Medical Subject Headings (MeSH) EC 5.4.2.4. ... Ravel P, Craescu CT, Arous N, Rosa J, Garel MC (May 1997). "Critical role of human bisphosphoglycerate mutase Cys22 in the ... Because the main function of bisphosphoglycerate mutase is the synthesis of 2,3-BPG, this enzyme is found only in erythrocytes ...
3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity. ... 2,3-bisphosphoglycerate mutase, erythrocyte. 2,3-bisphosphoglycerate synthase (EC:5.4.2.111 Publication. Manual assertion based ... "Crystal structure of human bisphosphoglycerate mutase.". Wang Y., Wei Z., Bian Q., Cheng Z., Wan M., Liu L., Gong W.. J. Biol. ... Bisphosphoglycerate mutaseAdd BLAST. 258. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical ...
Human bisphosphoglycerate mutase complexed with 2,3-bisphosphoglycerate (15 days). *DOI: 10.2210/pdb2HHJ/pdb ... A series of high resolution crystal structures of human bisphosphoglycerate mutase co-crystallized with 2,3-bisphosphoglycerate ... Bisphosphoglycerate mutase. A, B. 267. Homo sapiens. Mutation(s): 0 Gene Names: BPGM. EC: 5.4.2.4 (PDB Primary Data), 5.4.2.1 ( ... Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.. Wang, Y., Liu, L., Wei, Z., Cheng, Z., ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Bisphosphoglycerate mutase (transcript variant 2). Not available. Recombinant protein of human 2,3-bisphosphoglycerate mutase ( ... Bisphosphoglycerate mutase (transcript variant 1). Not available. Recombinant protein of human 2,3-bisphosphoglycerate mutase ( ... Alternative names for Bisphosphoglycerate mutase antibody. BPGM, 2,3-bisphosphoglycerate mutase, erythrocyte, 2,3- ... Rabbit Polyclonal antibody to BPGM (2,3-bisphosphoglycerate mutase). Rabbit. IgG. Aff - Purified. Hu, Ms. ICC/IF, WB. 0.1 ml / ...
3-bisphosphoglycerate mutase deficiency in individuals with lifelong, unexplained erythrocytosis Identifying mutation carriers ... 3-bisphosphoglycerate mutase (BPGM) that catalyzes the conversion of 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate (2,3- ... Diagnosis of 2,3-bisphosphoglycerate mutase deficiency in individuals with lifelong, unexplained erythrocytosis ... can detect mutations in BPGM that are associated with unexplained lifelong erythrocytosis due to bisphosphoglycerate mutase ...
3-Bisphosphoglycerate Mutase, Full Gene Sequencing Analysis Useful For. Diagnosis of 2,3-bisphosphoglycerate mutase deficiency ...
3-Bisphosphoglycerate-independent phosphoglycerate mutase gi/441475375. 141. Metabolic processes. 24a. Translation elongation ... 3-bisphosphoglycerate-independent phosphoglycerate mutase, lactate dehydrogenase, triosephosphate isomerase, rod shape- ...
3-bisphosphoglycerate-dependent phosphoglycerate mutase. Neisseria gonorrhoeae NG-k5105 ... 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase UniProtKBInterProInteractive Modelling. 227 aa; Sequence (Fasta) ... Crystal structure of 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase from Neisseria gonor…. homo-4-mer 4×TLA;. 5um0. ...
2,3-bisphosphoglycerate-independent phosphoglycerate mutase. 61.0. 5.42. 6. 14. 10. gi,347602486. Chaperone protein ClpC1, ...
3-DPG mutase (DPGM) was measured in different mammals presenting large differences in 2,3-DPG concentration between fetal, ... Bisphosphoglycerate Mutase / blood*. Diphosphoglyceric Acids / biosynthesis*. Fetus. Guinea Pigs. Hemoglobins / analysis. ... To investigate a possible mechanism involved in the regulation of 2,3-diphosphoglycerate (2,3-DPG) synthesis, 2,3-DPG mutase ( ...
bisphosphoglycerate mutase;. diphosphoglycerate mutase;. glycerate phosphomutase;. bisphosphoglycerate synthase;. ... 2,3-diphosphoglycerate mutase;. phosphoglyceromutase;. 2,3-diphosphoglycerate synthase;. DPGM;. 2,3-bisphosphoglycerate mutase; ... The latter is rephosphorylated by the enzyme to yield 2,3-bisphosphoglycerate, but this reaction is slowed by dissociation of 3 ... This enzyme also catalyses, slowly, the reaction of EC 5.4.2.11 [phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)] ...
3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a ... Phosphoglycerate mutase 1Add BLAST. 254. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view ... phosphoglycerate mutase activity Source: RGD ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the ... "Nuclear location of phosphoglycerate mutase BB isozyme in rat tissues.". Egea G., Urena J.M., Grana X., Marsal J., Carreras J. ...
bisphosphoglycerate mutase activity Source: UniProtKB-EC. *phosphoglycerate mutase activity Source: Ensembl. *protein kinase ... Phosphoglycerate mutaseUniRule annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system ... Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.UniRule annotation. ,p>Information which has been ... tr,Q3U7Z6,Q3U7Z6_MOUSE Phosphoglycerate mutase OS=Mus musculus GN=Pgam1 PE=1 SV=1 ...
3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a ... 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Source: GO_Central. *bisphosphoglycerate mutase activity ... Phosphoglycerate mutase 2Add BLAST. 253. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view ... Phosphoglycerate mutase 2 (EC:5.4.2.11By similarity. ,p>Manually curated information which has been propagated from a related ...
Phosphoglycerate Mutase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human ... Gene Ontology (GO) annotations related to this gene include protein kinase binding and bisphosphoglycerate mutase activity. An ... PGAM1 (Phosphoglycerate Mutase 1) is a Protein Coding gene. Diseases associated with PGAM1 include Phosphoglycerate Mutase ... The protein encoded by this gene is a mutase that catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2- ...
BPGM; bisphosphoglycerate mutase [KO:K01837] [EC:5.4.2.11 5.4.2.4]. 9562 MINPP1; multiple inositol-polyphosphate phosphatase 1 ... PGAM2; phosphoglycerate mutase 2 [KO:K01834] [EC:5.4.2.11]. 441531 PGAM4; phosphoglycerate mutase family member 4 [KO:K01834] [ ... PGAM1; phosphoglycerate mutase 1 [KO:K01834] [EC:5.4.2.11]. 5224 ...
3-bisphosphoglycerate-dependent phosphoglycerate mutase (PVX_091640, PF11_0208); triosephosphate isomerase (PVX_118495, PF14_ ...
IPR001345 Phosphoglycerate/bisphosphoglycerate mutase, active site. IPR027417 P-loop containing nucleoside triphosphate ...
  • The structures of chorismate mutases vary in different organisms, but the majority belong to the AroQ family and are characterized by an intertwined homodimer of 3-helical subunits. (wikipedia.org)