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.
An enzyme of the lyase class that catalyzes the conversion of GTP and oxaloacetate to GDP, phosphoenolpyruvate, and carbon dioxide. This reaction is part of gluconeogenesis in the liver. The enzyme occurs in both the mitochondria and cytosol of mammalian liver. (From Dorland, 27th ed) EC 4.1.1.32.
An enzyme with high affinity for carbon dioxide. It catalyzes irreversibly the formation of oxaloacetate from phosphoenolpyruvate and carbon dioxide. This fixation of carbon dioxide in several bacteria and some plants is the first step in the biosynthesis of glucose. EC 4.1.1.31.
An enzyme of the lyase class that catalyzes the conversion of ATP and oxaloacetate to ADP, phosphoenolpyruvate, and carbon dioxide. The enzyme is found in some bacteria, yeast, and Trypanosoma, and is important for the photosynthetic assimilation of carbon dioxide in some plants. EC 4.1.1.49.
Biosynthesis of GLUCOSE from nonhexose or non-carbohydrate precursors, such as LACTATE; PYRUVATE; ALANINE; and GLYCEROL.
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.-.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.

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)

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 ...
Staphylococcus aureus; pan ID: SAUPAN002709000; symbol: pgm; products: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, phosphoglyceromutase, putative 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; orthologs: COL: SACOL0841 (pgm), N315: SA0730 (pgm), NCTC8325: SAOUHSC_00798, Newman: NWMN_0744 (pgm)
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.
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.: ...
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 ...
3-Bisphosphoglycerate (1,3-BPG) 2,3-Bisphosphoglycerate (2,3-BPG) Bisphosphoglycerate mutase Bisphosphoglycerate phosphatase ...
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. ...
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 (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 ...
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 ...
... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 - phosphoglucomutase MeSH D08.811.399.520.750.700 - phosphoglycerate ... 2-acetolactate mutase MeSH D08.811.399.520.250 - chorismate mutase MeSH D08.811.399.520.250.500 - prephenate dehydratase MeSH ... mutase MeSH D08.811.399.894.200 - amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH D08.811.399.894. ... D08.811.399.520.250.750 - prephenate dehydrogenase MeSH D08.811.399.520.625 - methylmalonyl-coa mutase MeSH D08.811.399.520.750 ...
This step is the enzymatic transfer of a phosphate group from 1,3-bisphosphoglycerate to ADP by phosphoglycerate kinase, ... Phosphoglycerate mutase isomerises 3-phosphoglycerate into 2-phosphoglycerate. Enolase next converts 2-phosphoglycerate to ... The G3P is converted to 1,3-bisphosphoglycerate in the presence of enzyme glyceraldehyde-3-phosphate dehydrogenase (an oxido- ... 3-bisphosphoglycerate. The hydrogen is used to reduce two molecules of NAD+, a hydrogen carrier, to give NADH + H+ for each ...
3-Bisphosphoglycerate 2 × Phosphoglycerate kinase ADP ATP ADP ATP 2 × 3-Phosphoglycerate 2 × Phosphoglycerate mutase 2 × 2- ... As a consequence of bypassing this step, the molecule of ATP generated from 1-3 bisphosphoglycerate in the next reaction will ... This step is the enzymatic transfer of a phosphate group from 1,3-bisphosphoglycerate to ADP by phosphoglycerate kinase, ... Cofactors: Mg2+ Phosphoglycerate mutase isomerises 3-phosphoglycerate into 2-phosphoglycerate. Enolase next converts 2- ...
... phosphoacetylglucosamine mutase EC 5.4.2.4: bisphosphoglycerate mutase EC 5.4.2.5: phosphoglucomutase (glucose-cofactor) EC 5.4 ... 2-acetolactate mutase EC 5.4.99.4: 2-methyleneglutarate mutase EC 5.4.99.5: chorismate mutase EC 5.4.99.6: Now EC 5.4.4.2, ... phosphoenolpyruvate mutase EC 5.4.2.10: phosphoglucosamine mutase EC 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate- ... benzene mutase EC 5.4.4.2: isochorismate synthase EC 5.4.4.3: 3-(hydroxyamino)phenol mutase EC 5.4.4.4: geraniol isomerase EC ...
3-bisphosphoglycerate + ADP 1,3-bisphosphoglycerate + NAD(P)H + H+ ⇌ G3P + Pi + NAD(P)+ Triose-phosphate isomerase maintains ... Pi In gluconeogenesis 3-PG is produced by enolase and phosphoglycerate mutase acting in series PEP + H2O ⇌ 2-PG ⇌ 3-PG In the ...
3-bisphosphoglycerate phosphatase(2,3-DPG), another hydrolase which catalyzes the metabolic reaction of 2,3-bisphosphoglycerate ... In all animal tissues, 2,3-PGA is important as the cofactor of the glycolytic enzyme, phosphoglycerate mutase. More important, ...
Takahashi Y, Takahashi S, Yoshimi T, Miura T (June 1998). "Hypoxia-induced expression of phosphoglycerate mutase B in ... Phosphoglycerate kinase 1 is an enzyme involved in the conversion of 1,3-bisphosphoglycerate (1,3-BPG) to 3-phosphoglycerate (3 ... Phosphoglycerate mutase B (PGM-B) is one of the latter glycolytic enzymes responsible for the conversion of 3-phosphoglycerate ... phosphoglycerate mutase (PGM), enolase 1 (ENOA), pyruvate kinase (PK), pyruvate dehydrogenase kinase, isozyme 1 (PDK1) and ...
Phosphoglycerate mutase 2 (PGAM2), also known as muscle-specific phosphoglycerate mutase (PGAM-M), is a phosphoglycerate mutase ... 3-bisphosphoglycerate as a cofactor. Since both 3-PGA and 2-PGA are allosteric regulators of the pentose phosphate pathway (PPP ... Mutations in this gene cause muscle phosphoglycerate mutase deficiency, also known as glycogen storage disease X.[provided by ... DiMauro S, Miranda AF, Khan S, Gitlin K, Friedman R (June 1981). "Human muscle phosphoglycerate mutase deficiency: newly ...
3-bisphosphoglycerate 3-phosphatase EC 3.1.3.81: Transferred entry, now EC 3.6.1.75, diacylglycerol diphosphate phosphatase EC ... phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) EC 3.1.3.14: methylphosphothioglycerate phosphatase EC 3.1.3.15: ...
He described the role of the 2,3-bisphosphoglycerate for the anaerobic production of energy in the erythrocytes (Luebering- ... 9-19 Rapoport, S. and J. Luebering: An Optical Study Of Diphosphoglycerate Mutase (From the Children's Hospital Research ...
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 } ...
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 } ...
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 ...
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 ...
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 ...
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 ] ...
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 ...
2,3-bisphosphoglycerate-independent phosphoglycerate mutase (GpmI). P64270. 1.53 ↑. 10. Dihydrolipoyllysine-residue ... 3-bisphosphoglycerate-independent phosphoglycerate mutase (GpmI), fructose-bisphosphate aldolase class 1 (Fda), and ...
3-bisphosphoglycerate-independent phosphoglycerate mutase, PEG-2, putative glucose-6-phosphate 1-epimerase; PK2, plastidial ... phosphoglycerate mutase (PGM), glucose-6-phosphate 1-epimerase (PEG), and pyruvate kinase (PK) were highly expressed in the ...
2%2C3-bisphosphoglycerate-independent phosphoglycerate mutase. 164. SEQF2779,CP000925.1. ABY79392.1 jb [NA] [AA] 654/217. ...
2%2C3-bisphosphoglycerate-dependent phosphoglycerate mutase. 153. SEQF2367,AJTF01000013.1. SEQF2367_00155 jb [NA] [AA] 399/132 ...
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 ...
Bisphosphoglycerate mutase. $5.00. USD Add to cart. * Bleomycin hydrolase. $5.00. USD Add to cart ...
8. Bisphosphoglycerate mutase. Bisphosphoglycerate mutase is important in placental cells and erythrocyte-specific enzymes. ...
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 } ...
bisphosphoglycerate mutase [Source:HG.... BRWD3. 254065. BRWD3. bromodomain and WD repeat domain cont.... ...
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 ...
DVU2935 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase Details for DVU2935 - 2,3-bisphosphoglycerate-dependent ...
... 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; ...
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 ...
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 ...
Bisphosphoglycerate mutase (BPGM) deficiency ...
3-bisphosphoglycerate; PGK, phosphoglycerate kinase; PGM, phosphoglycerate mutase; ENO, enolase; PEP, phosphoenolpyruvate; PNO ...
Bisphosphoglycerate mutase. Zinc finger and BTB domain-containing protein 20. Mitoferrin-1 ...
2%2C3-bisphosphoglycerate-dependent phosphoglycerate mutase. 58. SEQF2964,KV801830.1. SEQF2964_00058 jb [NA] [AA] 489/162. ... phosphoglycerate mutase GpmB. 39. SEQF2964,KV801830.1. SEQF2964_00039 jb [NA] [AA] 1347/448. 38912-37566. Glutamate-1- ...
3-bisphosphoglycerate-dependent phosphoglycerate mutase (PGAM), glyceraldehyde 3-phosphate dehydrogenase (GAPDH), glucose-6- ...
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 ...
... 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" ...
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. Compositional properties of 2,3-bisphosphoglycerate-dependent ... phosphoglycerate mutase (bottom) versus UniprotKB/SwissProt (top). Green: Global amino acid composition; Magenta: Percentage of ...
2,3-bisphosphoglycerate-independent phosphoglycerate mutase [1] (data from MRSA252). NWMN_RS04915. NAD(+) kinase [1] (data from ...
Phosphofructokinase 2/Fructose 2,6-bisphosphatase - Bisphosphoglycerate mutase. Category: EC 4.1.1 ...
... 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- ...
  • 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)
  • Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities. (hmdb.ca)
  • 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)
  • Haggarty NW, Dunbar B, Fothergill LA: The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase. (hmdb.ca)
  • 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)
  • Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence. (hmdb.ca)
  • 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)
  • 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)
  • 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)
  • Compositional properties of 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (bottom) versus UniprotKB/SwissProt (top). (ucy.ac.cy)
  • 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)
  • 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)
  • Rapaport-Leubering cycle is mainly concerned with the synthesis of 2,3- bisphosphoglycerate in the RBC. (medetuit.com)
  • 6. In the sixth step of Glycolysis, glyceraldehyde 3-phosphate is dehydrogenated to 1,3-bisphosphoglycerate. (quizbiology.com)
  • Glyceraldehyde-3-phosphate is then oxidized by the enzyme glyceraldehyde 3-phosphate dehydrogenase to 1,3-bisphosphoglycerate (also called just Dysphoglycerate). (cerebromedico.com)
  • 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)
  • 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)
  • Molecular genetic studies in muscle phosphoglycerate mutase (PGAM-M) deficiency. (nih.gov)
  • Isolation and characterization of the gene encoding the muscle-specific isozyme of human phosphoglycerate mutase. (nih.gov)
  • 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)
  • Also exhibits mutase (EC 5.4.2.11) activity. (nih.gov)
  • 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)
  • 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)
  • 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)
  • The invention includes compounds and compositions for inhibiting phosphoglycerate mutase (PGM) activity. (nih.gov)
  • 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)