Creatine phosphate; phosphorylcreatine; creatine-P; phosphagen; fosfocreatine
3D model (JSmol)
|Molar mass||211.11 g·mol−1|
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
|what is ?)(|
Phosphocreatine, also known as creatine phosphate (CP) or PCr (Pcr), is a phosphorylated creatine molecule that serves as a rapidly mobilizable reserve of high-energy phosphates in skeletal muscle and the brain to recycle adenosine tri phosphate; which is the energy currency of the cell.
Two amino acids- arginine, and glycine are transformed into guanidinoacetate (also called glycocyamine or GAA) in the kidneys by the enzyme AGAT, which is then transported in the blood to the liver. A methyl group is added to GAA from the amino acid methionine by the enzyme GAMT, forming non phosphorylated creatine. This is then dumped into the blood by the liver where it travels mainly to the muscle cells (95% of the bodies creatine is in muscles), and to a lesser extent the brain, heart, and pancreas . Once inside the cells it is transformed into phosphocreatine by the enzyme complex creatine kinase which makes it able to donate it's phosphate group to recycle adenosine di phosphate (ADP), back into adenosine tri phosphate (ATP). As we only make 250g of ATP a day but recycle our entire bodyweight in ATP each day due to creatine phosphate; this process is extremely important, and is the basis of all vertebrates bio energetic system. After creatine phosphate has undergone a certain number of de phosphorylation, and re phosphorylation cycles recycling ATP, it is broken down into creatinine, which is then excreted in the urine. A 70kg adult male has around 120g of creatine in them, with 40% being the non phosphorylated form, and 60% as creatine phosphate. 1-2% of that amount is broken down, and excreted each day as creatinine.
It is used intravenously in hospitals in some parts of the world for cardiovascular problems under the name Neoton, and also used by some professional athletes, as it is not a controlled substance.
Phosphocreatine can anaerobically donate a phosphate group to ADP to form ATP during the first two to seven seconds following an intense muscular or neuronal effort. Conversely, excess ATP can be used during a period of low effort to convert creatine to phosphocreatine. The reversible phosphorylation of creatine (i.e., both the forward and backward reaction) is catalyzed by several creatine kinases. The presence of creatine kinase (CK-MB, MB for muscle/brain) in blood plasma is indicative of tissue damage and is used in the diagnosis of myocardial infarction. The cell's ability to generate phosphocreatine from excess ATP during rest, as well as its use of phosphocreatine for quick regeneration of ATP during intense activity, provides a spatial and temporal buffer of ATP concentration. In other words, phosphocreatine acts as high-energy reserve in a coupled reaction; the energy given off from donating the phosphate group is used to regenerate the other compound - in this case, ATP. Phosphocreatine plays a particularly important role in tissues that have high, fluctuating energy demands such as muscle and brain.
The discovery of phosphocreatine was reported by Grace and Philip Eggleton of the University of Cambridge and separately by Cyrus Fiske and Yellapragada Subbarow of the Harvard Medical School in 1927. A few years later David Nachmansohn, working under Meyerhof at the Kaiser Wilhelm Institute in Dahlem, Berlin, contributed to the understanding of the phosphocreatine's role in the cell.
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- Saks, Valdur (2007). Molecular system bioenergetics: energy for life. Weinheim: Wiley-VCH. p. 2. ISBN 978-3-527-31787-5.
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- Eggleton, Philip; Eggleton, Grace Palmer (1927). "The inorganic phosphate and a labile form of organic phosphate in the gastrocnemius of the frog". Biochemical Journal. 21 (1): 190–195. PMC . PMID 16743804.
- Fiske, Cyrus H.; Subbarao, Yellapragada (1927). "The nature of the 'inorganic phosphate' in voluntary muscle". Science. 65 (1686): 401–403. PMID 17807679. doi:10.1126/science.65.1686.401.