An enzyme that catalyzes the transfer of phosphate from C-3 of 1,3-diphosphoglycerate to C-2 of 3-phosphoglycerate, forming 2,3-diphosphoglycerate. EC 5.4.2.4.
An enzyme that catalyzes the conversion of 2-phospho-D-glycerate to 3-phospho-D-glycerate. EC 5.4.2.1.
A highly anionic organic phosphate which is present in human red blood cells at about the same molar ratio as hemoglobin. It binds to deoxyhemoglobin but not the oxygenated form, therefore diminishing the oxygen affinity of hemoglobin. This is essential in enabling hemoglobin to unload oxygen in tissue capillaries. It is also an intermediate in the conversion of 3-phosphoglycerate to 2-phosphoglycerate by phosphoglycerate mutase (EC 5.4.2.1). (From Stryer Biochemistry, 4th ed, p160; Enzyme Nomenclature, 1992, p508)
A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.
Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.
An enzyme catalyzing the transfer of a phosphate group from 3-phospho-D-glycerate in the presence of ATP to yield 3-phospho-D-glyceroyl phosphate and ADP. EC 2.7.2.3.
A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.
Common name for the order Pleuronectiformes. A very distinctive group in that during development they become asymmetrical, i.e., one eye migrates to lie adjacent to the other. They swim on the eyeless side. FLOUNDER, sole, and turbot, along with several others, are included in this order.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A metabolic process that converts GLUCOSE into two molecules of PYRUVIC ACID through a series of enzymatic reactions. Energy generated by this process is conserved in two molecules of ATP. Glycolysis is the universal catabolic pathway for glucose, free glucose, or glucose derived from complex CARBOHYDRATES, such as GLYCOGEN and STARCH.
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.
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.
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).
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).
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).
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.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
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.
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 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.
The mechanical process of cooling.
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.
Potentially pathogenic bacteria found in nasal membranes, skin, hair follicles, and perineum of warm-blooded animals. They may cause a wide range of infections and intoxications.
The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.
Infections with bacteria of the genus STAPHYLOCOCCUS.
The portion of an interactive computer program that issues messages to and receives commands from a user.
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.
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 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.
A publication issued at stated, more or less regular, intervals.
"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.
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).
Linear polymers in which orthophosphate residues are linked with energy-rich phosphoanhydride bonds. They are found in plants, animals, and microorganisms.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
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.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
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.
Inorganic salts of phosphoric acid.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

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 ...
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.
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 ...
Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown t
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 ...
SWISS-MODEL Repository entry for P65708 (GPMA_STAAM), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. Staphylococcus aureus (strain Mu50 / ATCC 700699)
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 first substrate-level phosphorylation occurs after the conversion of 3-phosphoglyceraldehyde and Pi and NAD+ to 1,3-bisphosphoglycerate via glyceraldehyde 3-phosphate dehydrogenase. 1,3-bisphosphoglycerate is then dephosphorylated via phosphoglycerate kinase, producing 3-phosphoglycerate and ATP through a substrate-level phosphorylation. The second substrate-level phosphorylation occurs by dephosphorylating phosphoenolpyruvate, catalyzed by pyruvate kinase, producing pyruvate and ATP. During the preparatory phase, each 6-carbon glucose molecule is broken into two 3-carbon molecules. Thus, in glycolysis dephosphorylation results in the production of 4 ATP. However, the prior preparatory phase consumes 2 ATP, so the net yield in glycolysis is 2 ATP. 2 molecules of NADH are also produced and can be used in oxidative phosphorylation to generate more ATP. ...
• 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 ...
Burkholderia phymatum STM815 is a β-rhizobial strain that can effectively nodulate several species of the large legume genus Mimosa. Two Tn5-induced mutants of this strain, KM16-22 and KM51, failed to form root nodules on Mimosa pudica, but still caused root hair deformation, which is one of the early steps of rhizobial infection. Both mutants grew well in a complex medium. However, KM16-22 could not grow on minimal medium unless a sugar and a metabolic intermediate such as pyruvate were provided, and KM51 also could not grow on minimal medium unless a sugar was added. The Tn5-interrupted genes of the mutants showed strong homologies to pgm, which encodes 2,3-biphosphoglycerate-dependent phosphoglycerate mutase (dPGM), and fbp, which encodes fructose 1,6-bisphosphatase (FBPase). Both enzymes are known to be involved in obligate steps in carbohydrate metabolism. Enzyme assays confirmed that KM16-22 and KM51 had indeed lost dPGM and FBPase activity, respectively, whilst the activities of these enzymes
The recombinant expression of Sa-iPGM was performed by growing transformed cells in Luria-Bertani broth at 37°C containing ampicillin (100 µg ml−1) and kanamycin (25 µg ml−1). Recombinant cell mass was induced with 100 µM IPTG when the OD600 reached 0.6 and was grown for 4 h at the same temperature. Harvested cells from 2 l culture were resuspended and lysed by ultrasonication in buffer A (10 mM Tris-HCl pH 8.0, 10 mM imidazole, 300 mM NaCl) containing leupeptin, pepstatin, aprotinin (0.1 µM each) and 0.2 µM phenylmethylsulfonyl chloride (PMSF) as protease inhibitors. The lysate was centrifuged at 22 000g at 4°C for 40 min. The supernatant was loaded onto Ni-NTA Sepharose High Performance affinity matrix (GE Healthcare Biosciences) pre-equilibrated with buffer A. The column was then washed extensively with buffer A to remove bound contaminants. Recombinant His6-tagged Sa-iPGM was finally eluted with buffer B (10 mM Tris-HCl pH 8.0, 300 mM NaCl, 50 mM imidazole). The eluted protein was ...
SWISS-MODEL Repository entry for A1VYF1 (GPMI_CAMJJ), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. Campylobacter jejuni subsp jejuni serotype O:23/36 (strain 81-176)
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+.
TY - JOUR. T1 - Phosphoglycerate kinase. T2 - Structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea: Phosphoglycerate Kinase. AU - Rojas-Pirela, Maura. AU - Andrade-Alviárez, Diego. AU - ROJAS DURAN, MARIA VERONICA. AU - Kemmerling, Ulrike. AU - Cáceres, Ana J.. AU - Michels, Paul A.. AU - Concepción, Juan Luis. AU - Quiñones, Wilfredo. N1 - Publisher Copyright: © 2020 The Authors. Copyright: Copyright 2020 Elsevier B.V., All rights reserved.. PY - 2020/11/1. Y1 - 2020/11/1. N2 - Phosphoglycerate kinase (PGK) is a glycolytic enzyme that is well conserved among the three domains of life. PGK is usually a monomeric enzyme of about 45 kDa that catalyses one of the two ATP-producing reactions in the glycolytic pathway, through the conversion of 1,3-bisphosphoglycerate (1,3BPGA) to 3-phosphoglycerate (3PGA). It also participates in gluconeogenesis, catalysing the opposite reaction to produce 1,3BPGA and ADP. Like most other glycolytic enzymes, PGK has also been ...
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.
Metabolic analysis of TM7 was performed by pooling sequence data from TM7a and TM7b, along with data from a third TM7 cell (TM7c). TM7c assembled into 474 kb and 632 genes but was not used as an independent reference because a sample-handling error during sequencing caused commingling with genomic DNA from TM7a. We binned the metagenome on the basis of similarities between the three TM7 samples and phylogenetic markers by selecting contigs that have phylogenetically unique marker genes. On the basis of the presence of recognizable signature genes, the oral TM7 cells are predicted to be capable of a range of common metabolic processes, such as glycolysis (3-phosphoglycerate kinase, phosphoglycerate mutase triosephosphate isomerase, and pyruvate kinase), the tricarboxylic acid cycle (succinyl-CoA synthetase), nucleotide biosynthesis (dihydroorotate dehydrogenase, uridylate kinase, guanylate kinase, aerobic-type ribonucleoside diphosphate reductase, and thymidylate synthase), and some amino acid ...
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, ... 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 ...
The phosphatase subunit of bisphosphoglycerate mutase, an enzyme found in red blood cells, shows an increase in activity by up ...
3-bisphosphoglycerate, bisphosphoglycerate synthase and phosphoglycerate mutase in rabbit erythroblasts and reticulocytes in ... 3-bisphosphoglycerate, bisphosphoglycerate synthase and phosphoglycerate mutase in rabbit erythroblasts and reticulocytes in ... where bisphosphoglycerate mutase catalyzes the transfer of a phosphoryl group from C1 to C2 of 1,3-BPG, giving 2,3-BPG. 2,3-BPG ... 3-BPG generated as the high-energy carboxylic acid-phosphate mixed anhydride bond is cleaved by bisphosphoglycerate mutase. The ...
3-bisphosphoglycerate independent phosphoglycerate mutase (iPGM), and pyruvate phosphate dikinase (PPDK). Glucose-6-phosphate ...
... 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 ... phosphoglucosamine mutase EC 5.4.2.11: phosphoglycerate mutase EC 5.4.2.12: phosphoglycerate mutase EC 5.4.3.1: deleted EC 5.4. ... 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 ...
... may refer to: 1,3-Bisphosphoglycerate 2,3-Bisphosphoglycerate Bisphosphoglycerate mutase ... Bisphosphoglycerate phosphatase This set index page lists chemical compounds articles associated with the same name. If an ...
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 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[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 ...
2-3 Bisphosphoglycerate in the active site of Bisphosphoglycerate Mutase. Depicted and labeled are the residues that assist in ... 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 ...
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; mechanism of action". The Journal ... is analogous to the interconversion of 2-phosphoglycerate and 3-phosphoglycerate catalyzed by phosphoglycerate mutase, in which ...
... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 - phosphoglucomutase MeSH D08.811.399.520.750.700 - phosphoglycerate ... 2-acetolactate mutase MeSH D08.811.399.520.250 - chorismate mutase MeSH D08.811.399.520.250.500 - prephenate dehydratase MeSH ... mutase MeSH D08.811.399.894.200 - amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH D08.811.399.894. ... D08.811.399.520.250.750 - prephenate dehydrogenase MeSH D08.811.399.520.625 - methylmalonyl-coa mutase MeSH D08.811.399.520.750 ...
... 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 ...
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 int 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 ...
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 ...
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. 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 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- ...
The two G3P now each are catalyzed by glyceraldehyde-3-phosphate dehydrogenase to produce two 1,3-bisphosphoglycerate. The two ... then react with phosphoglycerate kinase to produce two 3-phosphoglycerate which then reacts with phosphoglycerate mutase to get ...
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, ...
... (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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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 ...
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-PG + ATP ⇌ 1,3-bisphosphoglycerate + ADP. 1,3-bisphosphoglycerate + NAD(P)H + H+ ⇌ G3P + Pi + NAD(P)+. Triose-phosphate ... In gluconeogenesis 3-PG is produced by enolase and phosphoglycerate mutase acting in series ...
1,3-Bisphosphoglycerate NAD+ + Pi NADH + H+ + 2 2 Phosphoglycerate kinase 3-Phosphoglycerate Phosphoglycerate mutase 2- ...
1,3-Bisphosphoglycerate. NAD+ + Pi. NADH + H+. +. 2. 2. Phosphoglycerate kinase. 3-Phosphoglycerate. Phosphoglycerate mutase. 2 ...
2-3 Bisphosphoglycerate in the active site of Bisphosphoglycerate Mutase. Depicted and labeled are the residues that assist in ... 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 ...
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 ...
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 ...
Bisphosphoglycerate mutase is a trifunctional enzyme of which the main function is to synthesize 2,3-bisphosphoglycerate, the ... Bisphosphoglycerate mutase is a trifunctional enzyme of which the main function is to synthesize 2,3-bisphosphoglycerate, the ... Bisphosphoglycerate mutase. A, B. 267. Homo sapiens. Mutation(s): 0 Gene Names: BPGM. EC: 5.4.2.4 (PDB Primary Data), 5.4.2.11 ... Crystal structure of human bisphosphoglycerate mutase. Wang, Y., Wei, Z., Bian, Q., Cheng, Z., Wan, M., Liu, L., Gong, W.. ( ...
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., ...
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 (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, ...
bisphosphoglycerate mutase. CA1. carbonic anhydrase. DHAP. dihydroxyacetone phosphate. ENO1. Alpha-enolase. ESI. electrospray ... Additionally, the concentration of bisphosphoglycerate mutase (BPGM), a key enzyme for regulating the oxygen loading capacity ... This could prevent potential ATP loss by the diversion of 1,3-bisphosphoglyverate to produce 2,3-bisphosphoglycerate. ... 3-bisphosphoglycerate, DHAP, and FDP were all found to be over 50% heritable (Fig. 3). It is also noteworthy that one of the ...
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. ...
3-bisphosphoglycerate-dependent phosphoglycerate mutase. Staphylococcus aureus (strain Mu50 / ATCC 700699) ... 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase UniProtKBInterProInteractive Modelling. 228 aa; Sequence (Fasta) 18 ...
2,3-bisphosphoglycerate-independent phosphoglycerate mutase. 61.0. 5.42. 6. 14. 10. gi,347602486. Chaperone protein ClpC1, ...
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-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 ( ...
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 ...
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 controls serine pathway flux via 3-phosphoglycerate *Rob C Oslund ... Rights & permissionsfor article Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate . Opens in a new ...
Compound: Bisphosphoglycerate mutase. Species: Homo sapiens [TaxId:9606]. Gene: BPGM. Database cross-references and differences ... Compound: Bisphosphoglycerate mutase. Species: Homo sapiens [TaxId:9606]. Gene: BPGM. Database cross-references and differences ... Description: The Structure of Human Bisphosphoglycerate Mutase to 1.94A. Class: isomerase. Keywords: homodimer, synthase, ... phosphatase, mutase, ISOMERASE. Deposited on 2010-06-10, released 2010-11-10. The last revision prior to the SCOPe 2.07 freeze ...
3-bisphosphoglycerate-dependent phosphoglycerate mutase; eno, enolase; pyk, pyruvate kinase; pdhA, pyruvate dehydrogenase ( ... For example, vitamin B12 is a necessary cofactor for methylmalonyl-CoA mutase (mcm), which is present in "Pyropristinus" and ...
3-bisphosphoglycerate; BPGM, bisphosphoglycerate mutase; dPGM, cofactor-dependent phosphoglycerate mutase; EPP, ecdysteroid ... phosphoglycerate mutase 5; SH3, Src homology 3; TFIIC, transcription factor IIC; TIGAR, TP53 (tumour protein 53)-induced ... cofactor-dependent phosphoglycerate mutase). The superfamily contains two branches sharing very limited sequence similarity: ... Abbreviations: AP, acid phosphatase; 1,3-BPG, 1,3-bisphosphoglycerate; 2,3-BPG, 2, ...
15 Thus, in human bisphosphoglycerate mutase (PDB entry: 2A9J), the 3-phosphoglycerate has phosphoryl oxygen coordination from ... For example, in β-phosphoglucose mutase (PDB entry: 2WF8), a BeF3 is coordinated to Asp8, while a catalytic magnesium bridges ...
2,3-bisphosphoglycerate mutase. NM_199186. NM_001724. Gene Info. CEBPG. CCAAT/enhancer binding protein (C/EBP), gamma. NM_ ...
MF] bisphosphoglycerate 2-phosphatase activity *[MF] bisphosphoglycerate mutase activity *[MF] phosphoglycerate mutase activity ...
  • Bisphosphoglycerate mutase (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 glycolitic 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)
  • Phosphoglycerate mutase ( EC:5.4.2.1 ) (PGAM) and bisphosphoglycerate mutase ( EC:5.4.2.4 ) (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate [ PMID: 2847721 , PMID: 2831102 , PMID: 10958932 ]. (ebi.ac.uk)
  • We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM). (nih.gov)
  • The BPGM gene encodes the enzyme 2,3-bisphosphoglycerate mutase (BPGM) that catalyzes the conversion of 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate (2,3-BPG), also known as 2,3-diphosphoglycerate (2,3-DPG), through the Luebering-Rapoport pathway. (mayocliniclabs.com)
  • This test can detect mutations in BPGM that are associated with unexplained lifelong erythrocytosis due to bisphosphoglycerate mutase deficiency. (mayocliniclabs.com)
  • Mechanistically, erythrocyte ADORA2B-mediated activation of AMP-activated protein kinase (AMPK) and bisphosphoglycerate mutase (BPGM) promotes hypoxic and metabolic reprogramming to enhance production of 2,3-bisphosphoglycerate (2,3-BPG), an erythrocyte-specific metabolite triggering O 2 delivery. (plos.org)
  • BPGM also has a mutase and a phosphatase function, but these are much less active. (arp1.com)
  • BPGM (2,3-bisphosphoglycerate mutase) is a 259 amino acid protein that belongs to the phosphoglycerate mutase family and exists as a homodimer that plays a crucial role in the regulation of hemoglobin oxygen. (scrazzl.com)
  • 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. (ssgcid.org)
  • The phosphoglycerate mutase family encompasses enzymes that catalyse the interconversion of 3-phosphoglycerate and 2-phosphoglycerate and most organisms utilize PGAM to accomplish this reaction in glycolysis, the metabolic pathway which converts glucose into energy. (ssgcid.org)
  • The structure 3fdz , bound with 3-phosphoglycerate, phosphohistidine and 2,3-bisphosphoglycerate has captured the presence of two distinct stages of the PGAM catalytic cycle. (ssgcid.org)
  • The ensemble of six X-ray crystal structures of B. pseudomallei PGAM presented here provides for the first time a comprehensive view of a phosphoglycerate mutase enzyme complete with bound ligands encompassing substrate, intermediate, transition-state mimic and fragment-bound structures. (ssgcid.org)
  • Within the glycolytic pathway, the phosphoglycerate mutase enzyme (PGAM, also called PGM), catalyzes the conversion of 3-phosphoglycerate (3PG) to 2PG ( Fig. 1 A ). Two isoforms of PGAM have been reported: PGAM1 and PGAM2. (rupress.org)
  • Intermediates in the phosphoglycerate mutase and bisphosphoglycerate synthase reactions. (ebi.ac.uk)
  • There are a total of three reactions dPGM can catalyze: a mutase reaction resulting in the conversion of 3PG to 2PG and vice versa, a phosphatase reaction creating phosphoglycerate from 2,3-bisphosphoglycerate, and a synthase reaction producing 2,3-bisphosphoglycerate from 1,3-bisphosphoglycerate similar to the enzyme bisphosphoglycerate mutase[citation needed]. (wikipedia.org)
  • 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)
  • Bisphosphoglycerate mutase is a trifunctional enzyme of which the main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin. (rcsb.org)
  • The overall structure of the enzyme resembles that of the cofactor-dependent phosphoglycerate mutase except the regions of 13-21, 98-117, 127-151, and the C-terminal tail. (rcsb.org)
  • Bisphosphoglycerate mutase is an erythrocyte-specific enzyme catalyzing a series of intermolecular phosphoryl group transfer reactions. (rcsb.org)
  • The latter is rephosphorylated by the enzyme to yield 2,3-bisphosphoglycerate, but this reaction is slowed by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. (genome.jp)
  • This enzyme is not to be confused with Bisphosphoglycerate mutase which catalyzes the conversion of 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate. (wikipedia.org)
  • Phosphoglycerate mutase (PGM) is any enzyme that catalyzes step 8 of glycolysis. (wikipedia.org)
  • When 3-phosphoglycerate enters the active site, the phosphohistidine complex is positioned as to facilitate transfer of phosphate from enzyme to substrate C-2 creating a 2,3-bisphosphoglycerate intermediate. (wikipedia.org)
  • 3PG + P-Enzyme → 2,3BPG + Enzyme → 2PG + P-Enzyme 3-phosphoglycerate intermediate 2-phosphoglycerate ΔG°′=+1.1kcal/mol 3PG 2,3BPG 2PG Phosphoglycerate mutase exists primarily as a dimer of two either identical or closely related subunits of about 32kDa. (wikipedia.org)
  • An unbiased screen for genes that can immortalize mouse embryonic fibroblasts identified the glycolytic enzyme phosphoglycerate mutase (PGM). (aacrjournals.org)
  • Although the superfamily is overwhelmingly composed of phosphatases, the earliest known and arguably best-studied member is dPGM (cofactor-dependent phosphoglycerate mutase). (biochemj.org)
  • Kinetic and structural studies have provided evidence that indicate dPGM and bisphosphoglycerate mutase are paralogous structures. (wikipedia.org)
  • 2,3-bisphosphoglycerate is required a cofactor for dPGM. (wikipedia.org)
  • Anionic molecules such as vanadate, acetate, chloride ion, phosphate, 2-phosphoglycolate, and N-[tris(hydroxymethyl)methyl-2-amino]ethanesulfonate are known inhibitors of the mutase activity of dPGM. (wikipedia.org)
  • Phosphoglycerate mutase 1 (PGAM1) catalyzes the isomerization of 3-PG into the downstream glycolytic intermediate 2-phosphoglycerate (2-PG). (nih.gov)
  • PGAM1 (Phosphoglycerate Mutase 1) is a Protein Coding gene. (genecards.org)
  • Diseases associated with PGAM1 include Phosphoglycerate Mutase Deficiency and Corticobasal Degeneration . (genecards.org)
  • Orthologous to several human genes including PGAM1 (phosphoglycerate mutase 1). (zfin.org)
  • Phosphoglycerate mutase 1 (PGAM1) functions in glycolysis. (rupress.org)
  • The larger clade-1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. (embl.de)
  • Also exhibits mutase (EC 5.4.2.11 ) activity. (uniprot.org)
  • 54 The following summary is from Orphanet, a European reference portal for information on rare diseases and orphan drugs.Orpha Number: 97234Disease definitionMuscle phosphoglycerate mutase deficiency (PGAMD) is a metabolic myopathy characterised by exercise-induced cramp, myoglobinuria, and presence of tubular aggregates in the muscle biopsy. (malacards.org)
  • Phosphoglycerate Mutase Deficiency, also known as myopathy due to phosphoglycerate mutase deficiency , is related to glycogen storage disease x and myopathy , and has symptoms including myalgia An important gene associated with Phosphoglycerate Mutase Deficiency is PGAM2 (Phosphoglycerate Mutase 2), and among its related pathways/superpathways are Glycosaminoglycan metabolism and Glucose metabolism . (malacards.org)
  • 26 Phosphoglycerate mutase deficiency is a disorder that primarily affects muscles used for movement (skeletal muscles). (malacards.org)
  • Vanadate inhibits 2,3-diphosphoglycerate dependent phosphoglycerate mutases but does not affect the 2,3-bisphosphoglycerate indepent phosphoglycerate mutases. (springer.com)
  • Gene Ontology (GO) annotations related to this gene include protein kinase binding and bisphosphoglycerate mutase activity . (genecards.org)
  • Molecular cloning and nucleotide sequence of murine 2,3-bisphosphoglycerate mutase cDNA. (ebi.ac.uk)
  • cDNA encoding type B subunit of rat phosphoglycerate mutase: its isolation and nucleotide sequence. (semanticscholar.org)
  • In addition to being heritable, proteins and metabolites involved in glycolysis and redox metabolism are highly correlated, suggesting that crucial energy metabolism pathways are inherited en bloc at distinct levels. (mcponline.org)
  • 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. (genecards.org)
  • Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). (uniprot.org)
  • Amino acid residues involved in the catalytic site of human erythrocyte bisphosphoglycerate mutase. (wikipedia.org)
  • In contrast, the iPGM class is independent of 2,3-bisphosphoglycerate and catalyzes the intramolecular transfer of the phosphate group on monophosphoglycerates using a phosphoserineintermediate. (wikipedia.org)
  • The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. (embl.de)
  • The purification and properties of diphosphoglycerate mutase from human erythrocytes. (genome.jp)
  • Relationship of 2,3-diphosphoglycerate and 2,3-diphosphoglycerate mutase in various mammals. (biomedsearch.com)
  • The cells were fractionated according to the degree of differentiation of erythroblasts as evaluated from the hemoglobin content as well as the relative activities of the two enzymes, 3-phosphoglycerate kinase and bisphospho-glycerate mutase. (authormapper.com)
  • Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate. (nih.gov)
  • They catalyze the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. (wikipedia.org)
  • The catalyzed mutase reaction involves two separate phosphoryl groups and the ending phosphate on the 2-carbon is not the same phosphate removed from the 3-carbon. (wikipedia.org)
  • In addition, the side chain of Glu-13 would affect the Glu-89 protonation ability responsible for the low mutase activity. (rcsb.org)
  • Predicted to have bisphosphoglycerate mutase activity and phosphoglycerate mutase activity. (zfin.org)
  • Molecular function: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity. (expasy.org)
  • A series of high resolution crystal structures of human bisphosphoglycerate mutase co-crystallized with 2,3-bisphosphoglycerate, representing different time points in the phosphoryl transfer reaction, were solved. (rcsb.org)
  • These structures were published in the journal Acta Crystallographica Section F. Reference: "An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. (ssgcid.org)
  • It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. (wikipedia.org)
  • Belongs to the BPG-independent phosphoglycerate mutase family. (expasy.org)
  • Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. (genecards.org)
  • Phosphoglycerate mutase has a small positive Gibbs free energy and this reaction proceeds easily in both directions. (wikipedia.org)
  • Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae. (ebi.ac.uk)
  • The protein crystals were obtained and diffract to 2.5 A and produced the first crystal structure of bisphosphoglycerate mutase. (rcsb.org)
  • Development of a mutagenesis, expression and purification system for yeast phosphoglycerate mutase. (semanticscholar.org)
  • The conformational changes in the backbone and the side chains of some residues reveal the structural basis for the different activities between phosphoglycerate mutase and bisphosphoglycerate mutase. (rcsb.org)