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Human Metabolome Database Version 2.5

 

Showing metabocard for 2,3-Diphosphoglyceric acid (HMDB01294)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-08-30 12:59:42
Accession Number HMDB01294
Secondary Accession Numbers Not Available
Common Name 2,3-Diphosphoglyceric acid
Description 2,3-Bisphosphoglycerate (2,3-BPG, also known as 2,3-diphosphoglycerate or 2,3-DPG) is a three carbon isomer of the glycolytic intermediate 1,3-bisphosphoglycerate and is present at high levels in the human red blood cell (RBC; erythrocyte)--at the same molar concentration as hemoglobin. It is notable because it binds to deoxygenated hemoglobin in RBCs. In doing so, it allosterically upregulates the ability of RBCs to release oxygen near tissues that need it most. Its function was discovered in 1967 by Reinhold Benesch and Ruth Benesch.
Synonyms
  1. (2R)-2,3-bis(phosphonooxy)-Propanoic acid
  2. (R)-2,3-bis(phosphonooxy)-Propanoate
  3. (R)-2,3-bis(phosphonooxy)-Propanoic acid
  4. 2,3-Bisphospho-D-glycerate
  5. 2,3-Bisphospho-D-glyceric acid
  6. 2,3-Bisphosphoglyceric acid
  7. 2,3-Diphospho-D-glycerate
  8. 2,3-Diphospho-D-glyceric acid
  9. 2,3-Diphospho-D-glyceric acid pentasodium salt
  10. 2,3-bis(phosphonooxy)-Propanoate
  11. 2,3-bis(phosphonooxy)-Propanoic acid
  12. 2,3-disphospho-D-glycerate
  13. D-Glyceric acid bis
  14. D-Glyceric acid bis(dihydrogen phosphate)
  15. Diphosphoglycerate
  16. Diphosphoglyceric acid
  17. Glycerate 2,3-diphosphate
  18. Glyceric acid bis(dihydrogen phosphate)
  19. Glyceric acid diphosphate
  20. (2R)-2,3-bis(phosphonooxy)-Propanoate
Chemical IUPAC Name 2,3-diphosphonooxypropanoic acid
Chemical Formula C3H8O10P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellaneous
Class
  • Acyl Phosphates
Sub Class
  • Glycerophosphates
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • phosphoric acid ester
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 266.037
Monoisotopic Molecular Weight 265.959259
Isomeric SMILES OC(=O)[C@@H](COP(O)(O)=O)OP(O)(O)=O
Canonical SMILES OC(=O)C(COP(O)(O)=O)OP(O)(O)=O
KEGG Compound ID C01159 Link Image
BioCyc ID 23-DIPHOSPHOGLYCERATE Link Image
BiGG ID 1315507 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01294 Link Image
Metagene Link HMDB01294 Link Image
METLIN ID 153 Link Image
PubChem Compound 186004 Link Image
PubChem Substance 763458 Link Image
ChEBI ID Not Available
CAS Registry Number 138-81-8
InChI Identifier InChI=1/C3H8O10P2/c4-3(5)2(13-15(9,10)11)1-12-14(6,7)8/h2H,1H2,(H,4,5)(H2,6,7,8)(H2,9,10,11)/t2-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 9.69 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -5
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.55 [Predicted by ALOGPS]; -4.2 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location
  • Blood
  • Cellular Cytoplasm
Tissue Location
Tissue References
Erythrocyte —
Myelin —
Nerve Cells —
Red Blood Cell —
Reticulocyte —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 530.0 +/- 800.0 uM
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Cellular Cytoplasm
Value 4500.0 (4000.0-5000.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Glycolysis SMP00040 Link Image map00010 Link Image
General References
  1. Mairbaurl H, Schobersberger W, Oelz O, Bartsch P, Eckardt KU, Bauer C: Unchanged in vivo P50 at high altitude despite decreased erythrocyte age and elevated 2,3-diphosphoglycerate. J Appl Physiol. 1990 Mar;68(3):1186-94. [PubMed Link Image]
  2. Luganova IS, Blinov MN, Abdulkadyrova AS: [Age composition of the erythrocyte population, ATP and 2,3-diphosphoglycerate composition in erythrocytes in different forms of hemolytic anemia] Vopr Med Khim. 1978 Jul-Aug;24(4):499-505. [PubMed Link Image]
  3. Miwa S, Fujii H, Matsumoto N, Nakatsuji T, Oda S, Asano H, Asano S: A case of red-cell adenosine deaminase overproduction associated with hereditary hemolytic anemia found in Japan. Am J Hematol. 1978;5(2):107-15. [PubMed Link Image]
  4. Sezdi M, Bayik M, Ulgen Y: Storage effects on the Cole-Cole parameters of erythrocyte suspensions. Physiol Meas. 2006 Jul;27(7):623-35. Epub 2006 Apr 28. [PubMed Link Image]
  5. Linko K, Hekali R: Influence of the Taurus radiowave blood warmer on human red cells. Hemolysis and erythrocyte ATP and 2,3 DPG concentrations following warming by radiowaves, microwaves and water bath. Acta Anaesthesiol Scand. 1980;24(1):46-52. [PubMed Link Image]
  6. Shanoian SA, Gel'shtein GG, Sharova IuA, Metina RA, Lifliandskii DB: [Study of 2,3-diphosphoglyceric acid levels in artificial blood circulation with the use of a perfusate composed of defrosted erythrocytes and donor blood] Probl Gematol Pereliv Krovi. 1976 Feb;21(2):41-3. [PubMed Link Image]
  7. Spodaryk K, Zoladz JA: The 2,3-DPG levels of human red blood cells during an incremental exercise test: relationship to the blood acid-base balance. Physiol Res. 1998;47(1):17-22. [PubMed Link Image]
  8. Springer RR, Clark DK, Lea AS, Solis RT: Effects of changes in arterial carbon dioxide tension on oxygen consumption during cardiopulmonary bypass. Chest. 1979 May;75(5):549-54. [PubMed Link Image]
  9. Coppola L, Giunta R, Verrazzo G, Luongo C, Sammartino A, Vicario C, Giugliano D: Influence of ozone on haemoglobin oxygen affinity in type-2 diabetic patients with peripheral vascular disease: in vitro studies. Diabete Metab. 1995 Oct;21(4):252-5. [PubMed Link Image]
  10. Nakano T, Fujioka H, Tamura S, Amuro Y, Nabeshima K, Hada T, Higashino K: Erythrocyte 2,3-diphosphoglycerate in liver diseases. Am J Gastroenterol. 1987 Dec;82(12):1283-6. [PubMed Link Image]
  11. diBella G, Scandariato G, Suriano O, Rizzo A: Oxygen affinity and Bohr effect responses to 2,3-diphosphoglycerate in equine and human blood. Res Vet Sci. 1996 May;60(3):272-5. [PubMed Link Image]
  12. Pas'ko SA, Volosheniuk TG: [Causes, sequelae and possible ways of preventing hypophosphatemia in patients with cerebral ischemia] Zh Nevropatol Psikhiatr Im S S Korsakova. 1990;90(10):25-7. [PubMed Link Image]
  13. Rosenmund A, Binswanger U, Straub PW: Oxidative injury to erythrocytes, cell rigidity, and splenic hemolysis in hemodialyzed uremic patients. Ann Intern Med. 1975 Apr;82(4):460-5. [PubMed Link Image]
  14. Antonowicz J, Andrzejak R, Smolik R: Influence of heavy metal mixtures on erythrocyte metabolism. Int Arch Occup Environ Health. 1990;62(3):195-8. [PubMed Link Image]
  15. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
  16. Krasomski G, Zachara B: [2,3-diphosphoglycerate level in the red blood cells, inorganic phosphorus in the blood serum and the acid-base equilibrium indicators in different periods of normal pregnancy] Ginekol Pol. 1981 Aug;52(8):687-92. [PubMed Link Image]
  17. Wallas CH: Elevated red blood cell 2,3-diphosphoglycerate levels in black blood donors. Transfusion. 1978 Jan-Feb;18(1):108-12. [PubMed Link Image]
  18. Hirszel P, Maher JF, Tempel GE, Mengel CE: Effect of hemodialysis on factors influencing oxygen transport. J Lab Clin Med. 1975 Jun;85(6):978-86. [PubMed Link Image]
  19. Lijnen P, Hespel P, Van Oppens S, Fiocchi R, Goossens W, Vanden Eynde E, Amery A: Erythrocyte 2,3-diphosphoglycerate and serum enzyme concentrations in trained and sedentary men. Med Sci Sports Exerc. 1986 Apr;18(2):174-9. [PubMed Link Image]
  20. Yoneda S, Kako T, Kohketsu M, Fujinami T: Changes in blood viscosity following nifedipine administration and its relation to the contents of adenosine triphosphate and 2,3-diphosphoglyceric acid in red blood cells in patients with angina pectoris. Arzneimittelforschung. 1989 Apr;39(4):504-6. [PubMed Link Image]
Metabolic Enzymes
  1. Bisphosphoglycerate mutase
  2. Phosphoglycerate mutase 2
  3. Phosphoglycerate mutase 1
  4. 2,3-bisphosphoglycerate mutase (2,3-bisphosphoglycerate mutase, isoform CRA_a)
  5. Phosphoglycerate mutase family member 4 (PGAM3)
Enzyme 1 [top]
Enzyme 1 ID 5498
Enzyme 1 Name Bisphosphoglycerate mutase
Enzyme 1 Synonyms
  1. 2,3-bisphosphoglycerate mutase, erythrocyte
  2. 2,3-bisphosphoglycerate synthase
  3. BPGM
  4. BPG-dependent PGAM
Enzyme 1 Gene Name BPGM
Enzyme 1 Protein Sequence >Bisphosphoglycerate mutase 
MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVL
NRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYN
VTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRG
KTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEA
IQAAIKKVEDQGKVKQAKK
Enzyme 1 Number of Residues 259
Enzyme 1 Molecular Weight 30006
Enzyme 1 Theoretical pI 6.52
Enzyme 1 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 1 General Function Carbohydrate transport and metabolism
Enzyme 1 Specific Function Plays a major role in regulating hemoglobin oxygen affinity as a consequence of controlling 2,3-BPG concentration. Can also catalyze the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 29481 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P07738 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PMGE_HUMAN Link Image
Enzyme 1 PDB ID 1T8P Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >780 bp 
ATGTCCAAGTACAAACTTATTATGTTAAGACATGGAGAGGGTGCTTGGAATAAGGAGAAC
CGTTTTTGTAGCTGGGTGGATCAGAAACTCAACAGCGAAGGAATGGAGGAAGCTCGGAAC
TGTGGGAAGCAACTCAAAGCGTTAAACTTTGAGTTTGATCTTGTATTCACATCTGTCCTT
AATCGGTCCATTCACACAGCCTGGCTGATCCTGGAAGAGCTAGGCCAGGAATGGGTGCCT
GTGGAAAGCTCCTGGCGTCTAAATGAGCGTCACTATGGGGCCTTGATCGGTCTCAACAGG
GAGCAGATGGCTTTGAATCATGGTGAAGAACAAGTGAGGCTCTGGAGAAGAAGCTACAAT
GTAACCCCGCCTCCCATTGAGGAGTCTCATCCTTACTACCAAGAAATCTACAACGACCGG
AGGTATAAAGTATGCGATGTGCCCTTGGATCAACTGCCACGGTCGGAAAGCTTAAAGGAT
GTTCTGGAGAGACTCCTTCCCTATTGGAATGAAAGGATTGCTCCCGAAGTATTACGTGGC
AAAACCATTCTGATATCTGCTCATGGAAATAGCAGTAGGGCACTCCTAAAACACCTGGAA
GGTATCTCAGATGAAGACATCATCAACATTACTCTTCCTACTGGAGTCCCCATTCTTCTG
GAATTGGATGAAAACCTGCGTGCTGTTGGGCCTCATCAGTTCCTGGGTGACCAAGAGGCG
ATCCAAGCAGCCATTAAGAAAGTAGAAGATCAAGGAAAAGTGAAACAAGCTAAAAAATAG
Enzyme 1 GenBank Gene ID X04327 Link Image
Enzyme 1 GeneCard ID BPGM Link Image
Enzyme 1 GenAtlas ID BPGM Link Image
Enzyme 1 HGNC ID HGNC:1093 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q31-q34
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Joulin V, Peduzzi J, Romeo PH, Rosa R, Valentin C, Dubart A, Lapeyre B, Blouquit Y, Garel MC, Goossens M, et al.: Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence. EMBO J. 1986 Sep;5(9):2275-83. [PubMed Link Image]
  2. 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. Biomed Biochim Acta. 1987;46(2-3):S126-30. [PubMed Link Image]
  3. Joulin V, Garel MC, Le Boulch P, Valentin C, Rosa R, Rosa J, Cohen-Solal M: Isolation and characterization of the human 2,3-bisphosphoglycerate mutase gene. J Biol Chem. 1988 Oct 25;263(30):15785-90. [PubMed Link Image]
  4. Stafforini DM, Rollins EN, Prescott SM, McIntyre TM: The platelet-activating factor acetylhydrolase from human erythrocytes. Purification and properties. J Biol Chem. 1993 Feb 25;268(6):3857-65. [PubMed Link Image]
  5. Craescu CT, Schaad O, Garel MC, Rosa R, Edelstein S: Structural modeling of the human erythrocyte bisphosphoglycerate mutase. Biochimie. 1992 Jun;74(6):519-26. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5499
Enzyme 2 Name Phosphoglycerate mutase 2
Enzyme 2 Synonyms
  1. Phosphoglycerate mutase isozyme M
  2. PGAM-M
  3. BPG-dependent PGAM 2
  4. Muscle-specific phosphoglycerate mutase
Enzyme 2 Gene Name PGAM2
Enzyme 2 Protein Sequence >Phosphoglycerate mutase 2 
MATHRLVMVRHGESTWNQENRFCGWFDAELSEKGTEEAKRGAKAIKDAKMEFDICYTSVL
KRAIRTLWAILDGTDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFD
IPPPPMDEKHPYYNSISKERRYAGLKPGELPTCESLKDTIARALPFWNEEIVPQIKAGKR
VLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELNKELKPTKPMQFLGDEETVR
KAMEAVAAQGKAK
Enzyme 2 Number of Residues 253
Enzyme 2 Molecular Weight 28767
Enzyme 2 Theoretical pI 9.32
Enzyme 2 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 2 General Function Carbohydrate transport and metabolism
Enzyme 2 Specific Function Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 189872 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P15259 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PGAM2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >762 bp 
ATGGCCACTCACCGCCTCGTGATGGTCCGGCACGGCGAGAGCACATGGAACCAGGAGAAC
CGTTTCTGTGGCTGGTTCGATGCAGAGCTGAGTGAAAAGGGGACCGAGGAGGCCAAGCGG
GGAGCCAAGGCCATCAAGGATGCCAAGATGGAGTTTGACATCTGCTACACGTCAGTGCTG
AAGCGGGCCATCCGCACCCTCTGGGCCATCCTGGACGGCACGGACCAGATGTGGCTGCCT
GTGGTGCGCACTTGGCGCCTCAATGAGCGGCATTACGGGGGCCTCACAGGCCTCAACAAG
GCAGAAACGGCCGCCAAGCACGGGGAGGAGCAGGTGAAGATCTGGAGGCGCTCCTTCGAC
ATCCCGCCGCCCCCGATGGACGAGAAGCACCCCTACTACAACTCCATTAGCAAGGAGCGT
CGGTACGCAGGCCTGAAGCCCGGGGAACTCCCCACCTGCGAGAGCCTCAAGGACACCATT
GCCCGGGCCCTGCCCTTCTGGAACGAGGAGATTGTTCCCCAGATCAAGGCCGGCAAGCGA
GTGCTCATTGCAGCCCACGGGAACAGCCTGCGGGGCATTGTCAAGCACCTGGAAGGGATG
TCAGACCAGGCGATCATGGAGCTGAACCTGCCCACGGGGATCCCCATTGTGTATGAGCTG
AACAAGGAGCTGAAGCCCACCAAGCCCATGCAGTTCCTGGGTGATGAGGAAACGGTGCGG
AAGGCCATGGAGGCTGTGGCTGCCCAGGGCAAGGCCAAGTGA
Enzyme 2 GenBank Gene ID M55674 Link Image
Enzyme 2 GeneCard ID PGAM2 Link Image
Enzyme 2 GenAtlas ID PGAM2 Link Image
Enzyme 2 HGNC ID HGNC:8889 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Castella-Escola J, Ojcius DM, LeBoulch P, Joulin V, Blouquit Y, Garel MC, Valentin C, Rosa R, Climent-Romeo F, Cohen-Solal M: Isolation and characterization of the gene encoding the muscle-specific isozyme of human phosphoglycerate mutase. Gene. 1990 Jul 16;91(2):225-32. [PubMed Link Image]
  2. Tsujino S, Sakoda S, Mizuno R, Kobayashi T, Suzuki T, Kishimoto S, Shanske S, DiMauro S, Schon EA: Structure of the gene encoding the muscle-specific subunit of human phosphoglycerate mutase. J Biol Chem. 1989 Sep 15;264(26):15334-7. [PubMed Link Image]
  3. Shanske S, Sakoda S, Hermodson MA, DiMauro S, Schon EA: Isolation of a cDNA encoding the muscle-specific subunit of human phosphoglycerate mutase. J Biol Chem. 1987 Oct 25;262(30):14612-7. [PubMed Link Image]
  4. Tsujino S, Shanske S, Sakoda S, Fenichel G, DiMauro S: The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency. Am J Hum Genet. 1993 Mar;52(3):472-7. [PubMed Link Image]
  5. Hadjigeorgiou GM, Kawashima N, Bruno C, Andreu AL, Sue CM, Rigden DJ, Kawashima A, Shanske S, DiMauro S: Manifesting heterozygotes in a Japanese family with a novel mutation in the muscle-specific phosphoglycerate mutase (PGAM-M) gene. Neuromuscul Disord. 1999 Oct;9(6-7):399-402. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5501
Enzyme 3 Name Phosphoglycerate mutase 1
Enzyme 3 Synonyms
  1. Phosphoglycerate mutase isozyme B
  2. PGAM-B
  3. BPG-dependent PGAM 1
Enzyme 3 Gene Name PGAM1
Enzyme 3 Protein Sequence >Phosphoglycerate mutase 1 
MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQ
KRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYD
VPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKR
VLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVR
KAMEAVAAQGKAKK
Enzyme 3 Number of Residues 254
Enzyme 3 Molecular Weight 28804
Enzyme 3 Theoretical pI 7.22
Enzyme 3 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 Specific Function Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 551174 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P18669 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PGAM1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >765 bp 
ATGGCCGCCTACAAACTGGTGCTGATCCGGCACGGCGAGAGCGCATGGAACCTGGAGAAC
CGCTTCAGCGGCTGGTACGACGCCGACCTGAGCCCGGCGGGCCACGAGGAGGCGAAGCGC
GGCGGGCAGGCGCTACGAGATGCTGGCTATGAGTTTGACATCTGCTTCACCTCAGTGCAG
AAGAGAGCGATCCGGACCCTCTGGACAGTGCTAGATGCCATTGATCAGATGTGGCTGCCA
GTGGTGAGGACTTGGCGCCTCAATGAGCGGCACTATGGGGGTCTAACCGGTCTCAATAAA
GCAGAAACTGCTGCAAAGCATGGTGAGGCCCAGGTGAAGATCTGGAGGCGCTCCTATGAT
GTCCCACCACCTCCGATGGAGCCCGACCATCCTTTCTACAGCAACATCAGTAAGGATCGC
AGGTATGCAGACCTCACAGAAGATCAGCTACCCTCCTGTGAGAGTCTGAAGGATACTATT
GCCAGAGCTCTGCCCTTCTGGAATGAAGAAATAGTTCCCCAGATCAAGGAGGGGAAACGT
GTACTGATTGCAGCCCATGGCAACAGCCTCCGGGGCATTGTCAAGCATCTGGAGGGTCTC
TCTGAAGAGGCTATCATGGAGCTGAACCTGCCGACTGGTATTCCCATTGTCTATGAATTG
GACAAGAACTTGAAGCCTATCAAGCCCATGCAGTTTCTGGGGGATGAAGAGACGGTGCGC
AAAGCCATGGAAGCTGTGGCTGCCCAGGGCAAGGCCAAGAAGTGA
Enzyme 3 GenBank Gene ID J04173 Link Image
Enzyme 3 GeneCard ID PGAM1 Link Image
Enzyme 3 GenAtlas ID PGAM1 Link Image
Enzyme 3 HGNC ID HGNC:8888 Link Image
Enzyme 3 Chromosome Location 10
Enzyme 3 Locus 10q25.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Sakoda S, Shanske S, DiMauro S, Schon EA: Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family. J Biol Chem. 1988 Nov 15;263(32):16899-905. [PubMed Link Image]
  2. Blouquit Y, Calvin MC, Rosa R, Prome D, Prome JC, Pratbernou F, Cohen-Solal M, Rosa J: Sequence of the human erythrocyte phosphoglycerate mutase by microsequencer and mass spectrometry. J Biol Chem. 1988 Nov 15;263(32):16906-10. [PubMed Link Image]
  3. Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis. 1997 Mar-Apr;18(3-4):588-98. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 14910
Enzyme 4 Name 2,3-bisphosphoglycerate mutase (2,3-bisphosphoglycerate mutase, isoform CRA_a)
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name BPGM
Enzyme 4 Protein Sequence >2,3-bisphosphoglycerate mutase (2,3-bisphosphoglycerate mutase, isoform CRA_a) 
MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVL
NRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYN
VTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRG
KTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEA
IQAAIKKVEDQGKVKQAKK
Enzyme 4 Number of Residues 259
Enzyme 4 Molecular Weight 30006
Enzyme 4 Theoretical pI 6.52
Enzyme 4 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 4 General Function Carbohydrate transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID A4D1N9 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A4D1N9_HUMAN Link Image
Enzyme 4 PDB ID 1T8P Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID CH236950 Link Image
Enzyme 4 GeneCard ID A4D1N9 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 14915
Enzyme 5 Name Phosphoglycerate mutase family member 4 (PGAM3)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name PGAM4
Enzyme 5 Protein Sequence >Phosphoglycerate mutase family member 4 (PGAM3) 
MAAYKLVLIRHGESTWNLENRFSCWYDADLSPAGHEEAKRGGQALRDAGYEFDICLTSVQ
KRVIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYD
VPPPPMEPDHPFYSNISKDRRYADLTEDQLPSYESPKDTIARALPFWNEEIVPQIKEGKR
VLIAAHGNSLQGIAKHVEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVC
KAIEAVAAQGKAKK
Enzyme 5 Number of Residues 254
Enzyme 5 Molecular Weight 28777
Enzyme 5 Theoretical pI 6.63
Enzyme 5 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 5 General Function Carbohydrate transport and metabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 82802763 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q5JPN2 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q5JPN2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >762 bp 
ATGGCCGCCTACAAACTGGTGCTGATCCGGCACGGCGAGAGCACATGGAACCTGGAGAAC
CGCTTCAGCTGCTGGTACGACGCCGATCTGAGCCCGGCGGGCCACGAGGAGGCGAAGCGC
GGCGGGCAGGCGCTACGAGATGCTGGCTATGAGTTTGACATCTGCCTCACCTCAGTGCAG
AAGAGAGTGATCCGGACCCTCTGGACAGTGCTAGATGCCATTGATCAGATGTGGCTGCCA
GTGGTGAGGACTTGGCGCCTCAATGAGCGGCACTATGGGGGTCTAACCGGTCTCAATAAA
GCAGAAACTGCTGCAAAGCATGGTGAGGCCCAGGTGAAGATCTGGAGGCGCTCCTATGAT
GTCCCACCACCTCCGATGGAGCCCGACCATCCTTTCTACAGCAACATCAGTAAGGATCGC
AGGTATGCAGACCTCACAGAAGATCAGCTACCCTCCTATGAGAGTCCGAAGGATACTATT
GCCAGAGCTCTGCCCTTCTGGAATGAAGAAATAGTTCCCCAGATCAAGGAGGGGAAACGT
GTACTGATTGCAGCCCATGGCAACAGCCTCCAGGGCATTGCCAAGCATGTGGAGGGTCTC
TCTGAAGAGGCTATCATGGAGCTGAACCTGCCGACTGGTATTCCCATCGTCTATGAATTG
GACAAGAACTTGAAGCCTATCAAGCCCATGCAGTTTCTGGGGGATGAAGAGACGGTGTGC
AAAGCCATAGAAGCTGTGGCTGCCCAGGGCAAGGCCAAGAAG
Enzyme 5 GenBank Gene ID DQ120647 Link Image
Enzyme 5 GeneCard ID Q5JPN2 Link Image
Enzyme 5 GenAtlas ID PGAM4 Link Image
Enzyme 5 HGNC ID HGNC:21731 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available