Glucose 1-phosphate
 Anionic form of α-D-glucose 1-phosphate
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 Neutral form of α-D-glucose 1-phosphate
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| Names | |
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| IUPAC name
D-Glucopyranosyl dihydrogen phosphate
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| Systematic IUPAC name
(2Ξ,3R,4S,5S,6R)-3,4,5-Trihydroxy-6-(hydroxymethyl)oxan-2-yl dihydrogen phosphate | |
| Other names
Cori ester
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| Identifiers | |
3D model (JSmol)
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| ChEBI | |
| ChemSpider | |
| ECHA InfoCard | 100.000.396 |
| KEGG | |
| MeSH | glucose-1-phosphate |
PubChem CID
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| UNII | |
CompTox Dashboard (EPA)
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| Properties | |
| C6H13O9P | |
| Molar mass | 260.135 g·mol−1 |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Glucose 1-phosphate (also called Cori ester) is a glucose molecule with a phosphate group on the 1'-carbon. It can exist in either the α- or β-anomeric form.
Reactions of α-glucose 1-phosphate
[edit]Catabolic
[edit]In glycogenolysis, it is the direct product of the reaction in which glycogen phosphorylase cleaves off a molecule of glucose from a greater glycogen structure. A deficiency of muscle glycogen phosphorylase is known as glycogen storage disease type V (McArdle Disease).
To be utilized in cellular catabolism it must first be converted to glucose 6-phosphate by the enzyme phosphoglucomutase in a free equilibrium.[1][2][3] One reason that cells form glucose 1-phosphate instead of glucose during glycogen breakdown is that the very polar phosphorylated glucose cannot leave the cell membrane and so is marked for intracellular catabolism. Phosphoglucomutase-1 deficiency is known as glycogen storage disease type 14 (GSD XIV).[4]
Anabolic
[edit]In glycogenesis, free glucose 1-phosphate can also react with UTP to form UDP-glucose,[5] by using the enzyme UDP-glucose pyrophosphorylase. It can then return to the greater glycogen structure via glycogen synthase.[5]
β-Glucose 1-phosphate
[edit]β-Glucose 1-phosphate is found in some microbes. It is produced by inverting α-glucan phosphorylases including maltose phosphorylase, kojibiose phosphorylase and trehalose phosphorylase and is then converted into glucose 6-phosphate by β-phosphoglucomutase.
See also
[edit]References
[edit]- ^ Pelley, John W. (2012-01-01), Pelley, John W. (ed.), "8 - Gluconeogenesis and Glycogen Metabolism", Elsevier's Integrated Review Biochemistry (Second Edition), Philadelphia: W.B. Saunders, pp. 67–73, doi:10.1016/b978-0-323-07446-9.00008-8, ISBN 978-0-323-07446-9, retrieved 2020-12-16
- ^ Isselbacher, Kurt J. (1965-01-01), Bergmeyer, Hans-Ulrich (ed.), "Galactose-1-phosphate Uridyl Transferase", Methods of Enzymatic Analysis, Academic Press, pp. 863–866, doi:10.1016/b978-0-12-395630-9.50153-5, ISBN 978-0-12-395630-9, retrieved 2020-12-16
- ^ Bergmeyer, Hans-Ulrich; Klotzsch, Helmut (1965-01-01), Bergmeyer, Hans-Ulrich (ed.), "d-Glucose-1-phosphate", Methods of Enzymatic Analysis, Academic Press, pp. 131–133, doi:10.1016/b978-0-12-395630-9.50024-4, ISBN 978-0-12-395630-9, retrieved 2020-12-16
- ^ Orphanet: Glycogen storage disease due to phosphoglucomutase deficiency
- ^ a b Blanco, Antonio; Blanco, Gustavo (2017-01-01), Blanco, Antonio; Blanco, Gustavo (eds.), "Chapter 19 - Integration and Regulation of Metabolism", Medical Biochemistry, Academic Press, pp. 425–445, doi:10.1016/b978-0-12-803550-4.00019-7, ISBN 978-0-12-803550-4, retrieved 2020-12-16