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| Phosphocreatine | |
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| IUPAC name | 2-[Methyl-(N'-phosphonocarbamimidoyl) amino]acetic acid |
| Other names | Creatine phosphate Phosphorylcreatine Creatine-P |
| Identifiers | |
| Abbreviations | PCr |
| CAS number | [67-07-2] |
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| Properties | |
| Molecular formula | C4H10N3O5P |
| Molar mass | 211.113 g/mol |
| Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa) Infobox references |
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Phosphocreatine, also known as creatine phosphate or Pcr, is a phosphorylated creatine molecule that is an important energy store in skeletal muscle. It is used to anaerobically generate ATP from ADP, forming creatine for the 2 to 7 seconds following an intense effort. It does that by donating a phosphate group and this reaction is catalyzed by creatine kinase (presence of creatine kinase in plasma is indicative of tissue damage and is used in the diagnosis of myocardial infarction). This reaction is reversible and it therefore acts as a spatial and temporal buffer of ATP concentration. In other words, phosphocreatine is part of a coupled reaction; the energy given off from one reaction is used to regenerate the other compound - be it ATP. Phosphocreatine plays a particularly important role in tissues that have high, fluctuating energy demands such as muscle and brain.
Creatine phosphate is a high-energy phosphate-storage compound (phosphagen) found in muscles; formed from parts of three amino acids: Arg, Gly, and Met; biosynthesis: formation of quanidinoacetate from Arg and Gly (in kidney) followed by methylation (S-adenosyl methionine, SAM is required) to creatine (in liver), and phosphorylation by creatine kinase (ATP is required) to creatine phosphate (in muscle); catabolism: dehydratation to creatinine. is synthesized in the liver, and transported to the muscle cells, via the bloodstream, for storage.
History
Phosphocreatine was discovered by David Nachmansohn.
References
Schlattner, U., Tokarska-Schlattner, M., Wallimann, T. (2005). Mitochondrial creatine kinase in human health and disease. Biochemica et Biophysica Acta .27. (Published ahead of print).
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