Bisphosphoglycerate Mutase
Phosphoglycerate Mutase
2,3-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
Methylmalonyl-CoA Mutase
Erythrocytes
Phosphoglycerate Kinase
Phosphoric Monoester Hydrolases
Flatfishes
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
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
Phosphoenolpyruvate Carboxykinase (GTP)
Phosphoenolpyruvate Carboxylase
Phosphoenolpyruvate Carboxykinase (ATP)
Gluconeogenesis
Phosphoenolpyruvate Sugar Phosphotransferase System
The bacterial sugar phosphotransferase system (PTS) that catalyzes the transfer of the phosphoryl group from phosphoenolpyruvate to its sugar substrates (the PTS sugars) concomitant with the translocation of these sugars across the bacterial membrane. The phosphorylation of a given sugar requires four proteins, two general proteins, Enzyme I and HPr and a pair of sugar-specific proteins designated as the Enzyme II complex. The PTS has also been implicated in the induction of synthesis of some catabolic enzyme systems required for the utilization of sugars that are not substrates of the PTS as well as the regulation of the activity of ADENYLYL CYCLASES. EC 2.7.1.-.
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)Novel placental expression of 2,3-bisphosphoglycerate mutase. - Nuffield Department of Obstetrics and Gynaecology
Bisphosphoglycerate mutase antibody | acris-antibodies.com
Species: Phosphoglycerate/bisphosphoglycerate mutase, active site (IPR001345) | InterPro | EMBL-EBI
Phosphoglycerate/bisphosphoglycerate mutase, active site (IPR001345) | InterPro | EMBL-EBI
Glycolysis- Online Textbook Chapters - Alyvea.com
Reactome | BPGM dimer isomerises 1,3BPG to 2,3BPG
三浶快三公夦粽凅讠刓
PDB: 1E59
SAUPAN002709000 - AureoWiki
GTOP nfar0:BAD56223.1
Pgam1 - Phosphoglycerate mutase - Mus musculus (Mouse) - Pgam1 gene & protein
RCSB PDB - 5PGM: SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE
RCSB PDB
- 1E59: E.coli cofactor-dependent phosphoglycerate mutase complexed with vanadate Macromolecule Annotations...
Sequence Similarity Search - BLAST
Native Bakers yeast (S. cerevisiae) Glyceraldehyde-3-phosphate Dehydrogenase(EC 1.2.1.12) - Creative Enzymes
PGAM2 gene - Genetics Home Reference - NIH
Phosphoglyceromutase: Definition with Phosphoglyceromutase Pictures and Photos
Phosphoglycerate mutase 1
GFIT result for T02514
slr0582 protein (Synechocystis sp. PCC6803) - STRING database
SSDB Motif Search Result: pub:SAR11 0193
P65708 | SWISS-MODEL Repository
Phosphoglycerate mutase deficiency - Genetics Home Reference
Discovery and optimization of piperazine-1-thiourea-based human phosphoglycerate dehydrogenase inhibitors.
1H, 15N, 13C backbone resonance assignments of human phosphoglycerate kinase in a transition state analogue complex with ADP, 3...
Investigation of an energetic coupling between ligand binding and prot by Nathan W. Gardner
Substrate-level phosphorylation - Wikipedia
Hemoglobins affinity with oxygen - carbon dioxide, temperature and bisphosphoglycerate (BPG)
PGAM | SSGCID
AWRI796 2821 - Phosphoglycerate mutase - Saccharomyces cerevisiae (strain AWRI796) (Bakers yeast) - AWRI796 2821 gene & protein
Bovine testis and human erythrocytes contain different subtypes of membrane-associated Ins(1,4,5)P3/Ins(1,3,4,5)P4 5...
OriGene - Pgam2 (NM 017328) Human ORF cDNA Clone
August | 2017 | Discovery of potent and selective covalent inhibitors of JNK
TumorPortal
Effect of phosphoglycerate mutase and fructose 1,6-bisphosphatase deficiency on symbiotic Burkholderia phymatum | Microbiology...
IUCr) Expression, purification, crystallization and preliminary X-ray diffraction studies of phosphoglycerate mutase from...
A1VYF1 | SWISS-MODEL Repository
Anti-Methylmalonyl Coenzyme A mutase antibody (ab67869)
Most recent papers with the keyword Bisphosphates IV | Read by QxMD
Phosphoglycerate Kinase 2 (PGK2) (AA 1-417) (Active) protein (His tag)</span...
Glycolysis Made Easy | BioChemWiz - Nari R.
Methylmalonyl Coenzyme A mutase Lysates: Novus Biologicals
Phosphoglycerate kinase: Structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea:...
Inosine/pyruvate/phosphate medium but not adenosine/pyruvate/phosphate medium introduces millimolar amounts of 5-phosphoribosyl...
Tumor antigens eliciting autoantibody response in cancer of gingivo-buccal complex - Shukla - 2007 - PROTEOMICS - Clinical...
Anti-Phosphoglycerate Phosphokinase Antibody | Rabbit anti-Yeast | LSBio
Dissecting biological dark matter with single-cell genetic analysis of rare and uncultivated TM7 microbes from the human...
G304 | Phosphoglycerate Kinase 1 (PGK1)- Cloud-Clone Corp.
3-Phosphoglyceric acid
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.: ...
Luebering-Rapoport pathway
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 ...
Enzyme kinetics
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 ...
2-Phosphoglycolate
The phosphatase subunit of bisphosphoglycerate mutase, an enzyme found in red blood cells, shows an increase in activity by up ...
2,3-Bisphosphoglyceric acid
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 ...
Monocercomonoides
3-bisphosphoglycerate independent phosphoglycerate mutase (iPGM), and pyruvate phosphate dikinase (PPDK). Glucose-6-phosphate ...
Bisphosphoglycerate
3-Bisphosphoglycerate (1,3-BPG) 2,3-Bisphosphoglycerate (2,3-BPG) Bisphosphoglycerate mutase Bisphosphoglycerate phosphatase ...
Mutase
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. ...
Phosphoglycerate mutase
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 ...
Bisphosphoglycerate mutase
2-3 Bisphosphoglycerate in the active site of Bisphosphoglycerate Mutase. Depicted and labeled are the residues that assist in ... Bisphosphoglycerate mutase (EC 5.4.2.4, BPGM) is an enzyme unique to erythrocytes and placental cells. It is responsible for ... Bisphosphoglycerate Mutase at the US National Library of Medicine Medical Subject Headings (MeSH) EC 5.4.2.4 (Genes on human ... Ravel P, Craescu CT, Arous N, Rosa J, Garel MC (May 1997). "Critical role of human bisphosphoglycerate mutase Cys22 in the ...
Phosphoglucomutase
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 (June 1949). "Phosphoglucomutase: II Mechanism of Action". The ... is analogous to the interconversion of 2-phosphoglycerate and 3-phosphoglycerate catalyzed by phosphoglycerate mutase, in which ...
List of MeSH codes (D08)
... 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 ...
Entner-Doudoroff pathway
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 ...
Glycolysis
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- ...
List of EC numbers (EC 5)
... 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 ...
Fructose-bisphosphate aldolase
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 ...
Phosphoglycolate phosphatase
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, ...
Tumor hypoxia
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 ...
PGAM2
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 ...
List of EC numbers (EC 3)
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: ...
Samuel Mitja Rapoport
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 ...
Code System Concept
Bisphosphoglycerate mutase (substance) {2168009 , SNOMED-CT } Chorismate mutase (substance) {4067000 , SNOMED-CT } Cycloartenol ... Substance with mutase mechanism of action (substance). Code System Preferred Concept Name. Substance with mutase mechanism of ... 2-acetolactate mutase (substance) {37850005 , SNOMED-CT } 2-methyleneglutarate mutase (substance) {15399005 , SNOMED-CT } Beta- ... Methylaspartate mutase (substance) {83682009 , SNOMED-CT } Methylmalonyl-coenzyme A mutase (substance) {56024005 , SNOMED-CT } ...
Code System Concept
Bisphosphoglycerate mutase (substance). Code System Preferred Concept Name. Bisphosphoglycerate mutase (substance). Concept ... Enzyme (substance) {90668006 , SNOMED-CT } Substance with mutase mechanism of action (substance) {130945002 , SNOMED-CT } ...
Pediatric Polycythemia Vera Differential Diagnoses
Defects in bisphosphoglycerate mutase and phosphofructokinase result in decreased 2,3 BPG. BPG is necessary for hemoglobin to ... Rather, the phenotype at birth suggests the diagnoses such as high-affinity hemoglobin mutations, low 2,3 bisphosphoglycerate ...
Code System Concept
Bisphosphoglycerate mutase (substance) {2168009 , SNOMED-CT } Branched chain ketoacid decarboxylase (substance) {259466000 , ... 2-acetolactate mutase (substance) {37850005 , SNOMED-CT } 2-aminohexano-6-lactam racemase (substance) {130874005 , SNOMED-CT } ... Isobutyryl-coenzyme A mutase (substance) {130897008 , SNOMED-CT } Isochorismate synthase (substance) {1105007 , SNOMED-CT } ... Chorismate mutase (substance) {4067000 , SNOMED-CT } Chorismate synthase (substance) {22224001 , SNOMED-CT } Citramalate lyase ...
Bisphosphoglycerate mutase - Wikipedia
2-3 Bisphosphoglycerate in the active site of Bisphosphoglycerate Mutase. Depicted and labeled are the residues that assist in ... Bisphosphoglycerate mutase (EC 5.4.2.4, BPGM) is an enzyme unique to erythrocytes and placental cells. It is responsible for ... Bisphosphoglycerate Mutase at the US National Library of Medicine Medical Subject Headings (MeSH) EC 5.4.2.4 (Genes on human ... Ravel P, Craescu CT, Arous N, Rosa J, Garel MC (May 1997). "Critical role of human bisphosphoglycerate mutase Cys22 in the ...
Human Metabolome Database: Showing Protein Bisphosphoglycerate mutase (HMDBP00266)
Showing Protein Bisphosphoglycerate mutase (HMDBP00266). IdentificationBiological propertiesGene propertiesProtein properties ... Craescu CT, Schaad O, Garel MC, Rosa R, Edelstein S: Structural modeling of the human erythrocyte bisphosphoglycerate mutase. ... 3-bisphosphoglycerate mutase cDNA and revised amino acid sequence. Biomed Biochim Acta. 1987;46(2-3):S126-30. [PubMed:3036106 ... 3-bisphosphoglycerate mutase cDNA: revised amino acid sequence. EMBO J. 1986 Sep;5(9):2275-83. [PubMed:3023066 ] ...
Pediatric Polycythemia Vera Differential Diagnoses
Genes | Free Full-Text | Impacts of the Type I Toxin-Antitoxin System, SprG1/SprF1, on Staphylococcus aureus Gene Expression
Molecular mechanism of the extended oil accumulation phase contributing to the high seed oil content for the genotype of tung...
HOMD :: SEQF2779
HOMD :: SEQF2367
Protein View HIP000024198
EC 3.1.3.13 bisphosphoglycerate phosphatase EC 5.4.2.1 phosphoglycerate mutase EC 5.4.2.4 bisphosphoglycerate mutase ... Phosphoglycerate mutase 1; EC=3.1.3.13; EC=5.4.2.1; EC=5.4.2.4; BPG-dependent PGAM 1; Phosphoglycerate mutase isozyme B; PGAM-B ... Phosphoglycerate mutase 1; EC=3.1.3.13; EC=5.4.2.1; EC=5.4.2.4; BPG-dependent PGAM 1; Phosphoglycerate mutase isozyme B; PGAM-B ...
PeptiQuant? Plus Custom Proteomics Kits - MRM Proteomics
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Code System Concept
GSE411 UNSTIM VS 400MIN IL6 STIM SOCS3 KO MACROPHAGE DN
Phosphoglycerate Mutase 1 Predicts the Poor Prognosis of Oral Squamous Cell Carcinoma and is Associated with Cell Migration
Durany N, Joseph J, Campo E, Molina R, Carreras J. Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase ... Jiang X, Sun Q, Li H, Li K, Ren X. The role of phosphoglycerate mutase 1 in tumor aerobic glycolysis and its potential ... Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth. Cancer Cell. 2012;22:585-600 ... Phosphoglycerate mutase 1 promotes cancer cell migration independent of its metabolic activity. Oncogene. 2017;36:2900-9 ...
Desulfovibrio vulgaris Hildenborough Module 148 Residual: 0.45 | Syntrophy Portal
Evaluation of rate law approximations in bottom-up kinetic models of metabolism | BMC Systems Biology | Full Text
... bisphosphoglycerate phosphatase; DPGM, bisphosphoglycerate mutase; ENO, enolase; F6P, D-Fructose 6-phosphate; FDP, D-Fructose 1 ... Model of 2,3-bisphosphoglycerate metabolism in the human erythrocyte based on detailed enzyme kinetic equations: equations and ... phosphoglycerate mutase; Pi, orthophosphate; PK, pyruvate kinase; PRPP, 5-Phospho-alpha-D-ribose 1-diphosphate; PYR, pyruvate; ...
Glycolysis - Wikipedia
1,3-Bisphosphoglycerate (1,3BPG) Phosphoglycerate kinase (PGK). a transferase 3-Phosphoglycerate (3PG) ... phosphoglycerate mutase (8), phosphopyruvate hydratase (enolase) (9), pyruvate kinase (10), and lactate dehydrogenase (11). The ... 1,3-Bisphosphoglycerate 1,3BPG Glycerate-1,3-bisphosphate,. glycerate-1,3-diphosphate,. 1,3-diphosphoglycerate PGAP; BPG; DPG ... Glyceraldehyde-3-phosphate2− + Pi2− + NAD+ → 1,3-Bisphosphoglycerate4− + NADH + H+ 6.30 −1.29 ...
DEPOD - human DEPhOsphorylation Database
Bisphosphoglycerate mutase;BPGM;5.4.2.4;2,3-bisphosphoglycerate mutase, erythrocyte;2,3-bisphosphoglycerate synthase;5.4.2.11;2 ... Superfamily: histidine phosphatase (HP) Family: PGAM , Historic class: Phosphoglycerate mutase , CATH ID: 3.40.50.1240 , ... 3-bisphosphoglycerate (2,3-BPG) Also exhibits mutase (EC 54211)activity ...
De novo assembly and comparative transcriptome analysis of Euglena gracilis in response to anaerobic conditions | BMC Genomics ...
Pharos : Target Details - ZHX2
HOMD :: SEQF2964
Comparative transcriptome analysis revealing the potential mechanism of seed germination stimulated by exogenous gibberellin in...
PlantPromoterDB promoter information of AT3G50520.1
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 ...
KEGG pathway • massdatabase
... bisphosphoglycerate mutase [KO:K01837] [EC:5.4.2.4 5.4.2.11]" #, [129] "9562" #, [130] "MINPP1; multiple inositol-polyphosphate ... phosphoglycerate mutase 1 [KO:K01834] [EC:5.4.2.11]" #, [41] "5224" #, [42] "PGAM2; phosphoglycerate mutase 2 [KO:K01834] [EC: ... 5.4.2.11]" #, [43] "441531" #, [44] "PGAM4; phosphoglycerate mutase family member 4 [KO:K01834] [EC:5.4.2.11]" #, [45] "2027" ...
UniprotKB/SwissProt 2014 05: 251 aa from B2S2B5:1..251
NWMN RS04865 - AureoWiki
Phosphoenolpyruvate carboxykinase
Looking for Hypothetical Proteins in Clusters of Related Features - BV-BRC Documentation
... bisphosphoglycerate-independent phosphoglycerate mutase (EC 5.4.2.12)::Murein hydrolase activator EnvC::Rhodanese-related ... Chorismate mutase I (EC 5.4.99.5)::Prephenate dehydratase (EC 4.2.1.51)::2-keto-3-deoxy-D-arabino-heptulosonate-7-phosphate ... Phosphoglycerate mutase (EC 5.4.2.11)::UDP-glucose 4-epimerase (EC 5.1.3.2)::Inosine/xanthosine triphosphatase (EC 3.6.1.-):: ... Phosphoglucosamine mutase (EC 5.4.2.10)::Penicillin-binding protein 2 (PBP-2)::Rod shape-determining protein RodA::D-alanyl-D- ...
BPGM2
- Bisphosphoglycerate mutase (EC 5.4.2.4, BPGM) is an enzyme unique to erythrocytes and placental cells. (wikipedia.org)
- 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)
Phosphatase1
- Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities. (hmdb.ca)
Catalytic2
- It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. (wikipedia.org)
- Amino acid residues involved in the catalytic site of human erythrocyte bisphosphoglycerate mutase. (wikipedia.org)
Diphosphoglycerate1
- Haggarty NW, Dunbar B, Fothergill LA: The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase. (hmdb.ca)
Enzyme3
- 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)
- In this study, we investigated the role of the metabolic enzyme phosphoglycerate mutase 1 (PGAM1) in OSCC. (jcancer.org)
- Phosphoglycerate mutase 1 (PGAM1) is an essential metabolic enzyme in glycolysis that catalyzes the conversion of 3-phosphoglycerate (3-PG) into 2-phosphoglycerate (2-PG) [ 6 ]. (jcancer.org)
Human erythrocyte1
- Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence. (hmdb.ca)
Amino1
- Cohen-Solal M, Joulin V, Romeo PH, Rosa R, Valentin C, Garel MC, Rosa J: Molecular cloning of the human 2,3-bisphosphoglycerate mutase cDNA and revised amino acid sequence. (hmdb.ca)
Fold2
- Phosphoglycerate kinase 1 was overexpressed additional than 18 fold which catalysed the conversion of 1,three bisphosphoglycerate to 3 phosphoglyc erate coupled using the generation of ATP. (camkkinases.com)
- Most intrigu ingly, we uncovered that phosphoglycerate mutase 1 was shown an upregulation up to six fold. (camkkinases.com)
Role1
- Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). (hmdb.ca)
Properties1
- Compositional properties of 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (bottom) versus UniprotKB/SwissProt (top). (ucy.ac.cy)
Levels1
- Rather, the phenotype at birth suggests the diagnoses such as high-affinity hemoglobin mutations, low 2,3 bisphosphoglycerate levels (BPG), primary familial and congenital polycythemia (PFCP), Chuvash polycythemia or rare mutations of HIF2a, or proline dehydrogenase type 2 genes. (medscape.com)
Phosphoglycerate4
- Phosphoglycerate mutase 1 (PGAM1) catalyzes the isomerization of 3-PG into the downstream glycolytic intermediate 2-phosphoglycerate (2-PG). (princeton.edu)
- Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases. (expasy.org)
- Compositional properties of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (bottom) versus UniprotKB/SwissProt (top). (ucy.ac.cy)
- 7. In step 7 of Glycolysis, 1,3-bisphosphoglycerate is hydrolysed to 3-phosphoglycerate by forming ATP. (quizbiology.com)
Source:HGN1
- bisphosphoglycerate mutase [Source:HGN. (gsea-msigdb.org)
Cycle1
- Rapaport-Leubering cycle is mainly concerned with the synthesis of 2,3- bisphosphoglycerate in the RBC. (medetuit.com)
Step1
- 6. In the sixth step of Glycolysis, glyceraldehyde 3-phosphate is dehydrogenated to 1,3-bisphosphoglycerate. (quizbiology.com)
Glyceraldehyde 3-phosphate d1
- Glyceraldehyde-3-phosphate is then oxidized by the enzyme glyceraldehyde 3-phosphate dehydrogenase to 1,3-bisphosphoglycerate (also called just Dysphoglycerate). (cerebromedico.com)
Glycolytic enzyme2
- The glycolytic enzyme phosphoglycerate mutase (PGAM) is a dimer, and mature human skeletal muscle contains almost exclusively the MM form of the enzyme, PGAM-M. In 1981, we identified a patient with PGAM-M deficiency, and three additional patients have since been described. (nih.gov)
- The co-factor independent phosphoglycerate mutase (iPGM) is an essential glycolytic enzyme and validated target in several infectious organisms structurally distinct from its human isozyme. (nih.gov)
IPGM1
- The search for the homologues of this domain in the non-redundant sequence database using PSI-BLAST, resulted in identification of distant relationship between this family and the alkaline phosphatase-like superfamily, which includes families of aryl sulfatase, N-acetylgalactosomine-4-sulfatase, alkaline phosphatase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGM). (smokeybandittransam.com)
PGAM1
- Molecular genetic studies in muscle phosphoglycerate mutase (PGAM-M) deficiency. (nih.gov)
Isozyme1
- Isolation and characterization of the gene encoding the muscle-specific isozyme of human phosphoglycerate mutase. (nih.gov)
Dehydrogenase1
- Rather, the phenotype at birth suggests the diagnoses such as high-affinity hemoglobin mutations, low 2,3 bisphosphoglycerate levels (BPG), primary familial and congenital polycythemia (PFCP), Chuvash polycythemia or rare mutations of HIF2a, or proline dehydrogenase type 2 genes. (medscape.com)
2.111
- Also exhibits mutase (EC 5.4.2.11) activity. (nih.gov)
Reaction3
- this reaction does not require the cofactor 2,3-bisphosphoglycerate. (ntu.edu.sg)
- A redox reaction converts glyceraldehyde-3-phosphate into bisphosphoglycerate, which releases an H+ ion from NAD+ to NADH. (badscienceblogs.net)
- Interconversion of 3- and 2-phosphoglycerate with 2, 3-bisphosphoglycerate as the primer of the reaction. (icr.ac.uk)
Hemoglobin1
- Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). (nih.gov)
Converts2
- Phosphoglycerate kinase simultaneously converts ADP to ATP by converting 1,3-bisphosphoglycerate to 3-phosphoglycerate via phosphoglycerate kinase. (badscienceblogs.net)
- 3-phosphoglycerate converts to 2-phosphoglycerate via Phospoglycerate mutase. (badscienceblogs.net)
Activity1
- The invention includes compounds and compositions for inhibiting phosphoglycerate mutase (PGM) activity. (nih.gov)
Human1
- Using solid phase peptide synthesis, the ipglycermides and analogs were prepared in milligram quantity and evaluated in functional target-based assays on a panel of phosphoglycerate mutase enzymes from target and anti-target (i.e., human dPGM) species. (nih.gov)