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2,3-bisphosphoglycerate mutase

Bisphosphoglycerate Mutase, BPGM, 2,3-bisphosphoglycerate mutase
2,3-diphosphoglycerate (2,3-DPG) is a small molecule found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. This gene encodes a multifunctional enzyme that catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. The enzyme also has phosphoglycerate phosphomutase activity. Deficiency of this enzyme increases the affinity of cells for oxygen. Mutations in this gene result in hemolytic anemia. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Sep 2009] (from NCBI)
Top mentioned proteins: ACID, CAN, fibrillin-1, HAD, AGE
Papers on Bisphosphoglycerate Mutase
Microarray and Co-expression Network Analysis of Genes Associated with Acute Doxorubicin Cardiomyopathy in Mice.
Li et al., Beijing, China. In Cardiovasc Toxicol, Oct 2015
Several key genes, including 2,3-bisphosphoglycerate mutase (Bpgm), hexokinase 2, pyruvate dehydrogenase kinase, isoenzyme 4 and fructose-2,6-bisphosphate 2-phosphatase, are closely related to glucose metabolism.
Relationship between chronic disturbance of 2,3-diphosphoglycerate metabolism in erythrocytes and Alzheimer disease.
Kaminsky et al., San Antonio, United States. In Cns Neurol Disord Drug Targets, Sep 2015
Glycolytic enzymes hexokinase, phosphofructokinase, bisphosphoglycerate mutase and bisphosphoglycerate phosphatase displayed lower activities in age-matched controls, and higher activities in AD patients, as compared to those in young adult control subjects.
Associations between Serum Sex Hormone Concentrations and Whole Blood Gene Expression Profiles in the General Population.
Wallaschofski et al., Greifswald, Germany. In Plos One, 2014
RESULTS: In men, positive correlations were detected between AD and DDIT4 mRNA levels, as well as between SHBG and the mRNA levels of RPIA, RIOK3, GYPB, BPGM, and RAB2B.
Hereditary erythrocytosis, thrombocytosis and neutrophilia.
Gotlib et al., Stanford, United States. In Best Pract Res Clin Haematol, 2014
Secondary congenital erythrocytosis may be characterized by normal or high serum EPO levels, and is related to high oxygen affinity haemoglobin variants, mutation of the enzyme biphosphoglycerate mutase (BPGM), or defects in components of the oxygen-sensing pathway.
Insights into the phosphatase and the synthase activities of human bisphosphoglycerate mutase: a quantum mechanics/molecular mechanics simulation.
Zhang et al., Changchun, China. In Phys Chem Chem Phys, 2014
Bisphosphoglycerate mutase (BPGM) is a multi-activity enzyme.
Genetic basis of congenital erythrocytosis: mutation update and online databases.
ECE-Consortium et al., Coimbra, Portugal. In Hum Mutat, 2014
These include hemoglobin variants with increased affinity for oxygen (HBB, HBA mutations), decreased production of 2,3-bisphosphoglycerate due to BPGM mutations, or mutations in the genes involved in the hypoxia sensing pathway (VHL, EPAS1, and EGLN1).
Proteomic analysis on the alteration of protein expression in the early-stage placental villous tissue of electromagnetic fields associated with cell phone exposure.
Huang et al., Hangzhou, China. In Reprod Sci, 2013
Twelve proteins were identified- procollagen-proline, eukaryotic translation elongation factor 1 delta, chain D crystal structure of human vitamin D-binding protein, thioredoxin-like 3, capping protein, isocitrate dehydrogenase 3 alpha, calumenin, Catechol-O-methyltransferase protein, proteinase inhibitor 6 (PI-6; SerpinB6) protein, 3,2-trans-enoyl-CoA isomerase protein, chain B human erythrocyte 2,3-bisphosphoglycerate mutase, and nucleoprotein.
[Differential expression of genes that encode glycolysis enzymes in kidney and lung cancer in humans].
Kudryavtseva et al., In Genetika, 2013
Quantitative analysis of mRNA level demonstrated that only a part ofgenes that encode glycolysis enzymes maintain relatively stable mRNA level, including the HK1, ADPGK, GPI, PGK1, and PKM2 genes in kidney papillary cancer and the ADPGK, ALDOA, GAPDH, PGK1, BPGM, ENO1, and PKM2 genes in planocellular lung cancer.
Age-related defects in erythrocyte 2,3-diphosphoglycerate metabolism in dementia.
Aliev et al., Pushchino, Russia. In Aging Dis, 2012
AD is characterized by higher activities of hexokinase, phosphofructokinase, and bisphosphoglycerate mutase and bisphosphoglycerate phosphatase in RBCs.
Usefulness of material recovered from distal embolic protection devices after carotid angioplasty for proteomic studies.
Castillo et al., Santiago de Compostela, Spain. In J Vasc Interv Radiol, 2012
Annexin A5 (ANXA5), haptoglobin precursor, purine nucleoside phosphorylase, transgelin-2 (TAGLN2), and bisphosphoglycerate mutase were upregulated in debris from patients with high systemic inflammation, and proteasome subunit 8 beta type and glutathione-S-transferase kappa 1 (GSTK1) levels were higher in debris from patients with low levels of systemic inflammation.
Differentially displayed genes with oxygen depletion stress and transcriptional responses in the marine mussel, Mytilus galloprovincialis.
Yum et al., South Korea. In Comp Biochem Physiol Part D Genomics Proteomics, 2011
The observed differences in the DD-PCR of 10 genes (encoding elongation factor 1 alpha, heat shock protein 90, calcium/calmodulin-dependent protein kinase II, GTPase-activating protein, 18S ribosomal RNA, cytochrome oxidase subunit 1, ATP synthase, chitinase, phosphoglycerate/bisphosphoglycerate mutase family protein, and the nicotinic acetylcholine receptor) were confirmed by quantitative RT-PCR and their transcriptional changes in the mussels exposed to hypoxic conditions for 24-72 h were investigated.
Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding.
Nairn et al., Glasgow, United Kingdom. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010
1.94 A resolution X-ray structure of bisphosphoglycerate mutase is presented, focusing on the dynamic nature of key ligand-binding residues and their interaction with the inhibitor citrate
Role of band 3 in regulating metabolic flux of red blood cells.
Low et al., Madison, United States. In Proc Natl Acad Sci U S A, 2009
Moreover, these metabolic alterations were not attributable to modulation of bisphosphoglycerate mutase, direct inhibition of GEs by pervanadate, or oxidation, which are the major side effects of pervanadate treatment.
Placental expression of 2,3 bisphosphoglycerate mutase in IGF-II knock out mouse: correlation of circulating maternal 2,3 bisphosphoglycerate and fetal growth.
Vatish et al., Coventry, United Kingdom. In Placenta, 2009
Bisphosphoglycerate mutase (BPGM) catalyses the formation of 2,3 bisphosphoglycerate (BPG) a ligand of haemoglobin.
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.
Gong et al., Beijing, China. In J Biol Chem, 2007
analysis of histidine phosphorylation in human bisphosphoglycerate mutase
Crystal structure of human bisphosphoglycerate mutase.
Gong et al., Beijing, China. In J Biol Chem, 2004
bisphosphoglycerate mutase crystallographic structure
The phosphoglycerate mutases.
Watson et al., Edinburgh, United Kingdom. In Adv Enzymol Relat Areas Mol Biol, 1988
Cofactor-dependent monophosphoglycerate mutase and bisphosphoglycerate mutase are undoubtedly very closely related.
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