Adenosine thiamine triphosphate
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| IUPAC name
3-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-(2-(((((((((2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methoxy)(hydroxy)phosphoryl)oxy)(hydroxy)phosphoryl)oxy)(hydroxy)phosphoryl)oxy)ethyl)-4-methylthiazol-3-ium | |
| Other names
P1,P3-(Adenosine-5'-thiamine) triphosphate | |
| Identifiers | |
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| 3D model (JSmol) |
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| ChemSpider | |
| MeSH | adenosine+thiamine+triphosphate |
| PubChem CID |
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| Properties | |
| C22H31N9O13P3S | |
| Molar mass | 754.52 g·mol−1 |
| Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). | |
 verify (what is  ?) | |
| Infobox references | |
Adenosine thiamine triphosphate (AThTP), or thiaminylated adenosine triphosphate, is a natural thiamine adenine nucleotide.[1] It was discovered in Escherichia coli where it may account for up to 15 - 20% of total thiamine under carbon starvation. AThTP exists also, though at much lower levels, in eukaryotic organisms such as yeast, roots of higher plants and animal tissues. It was found to exist in small amounts in the muscle, heart, brain, kidneys and liver of mice.[2]
In E. coli AThTP is synthesized from thiamine diphosphate (ThDP) according to the following reaction catalyzed by thiamine diphosphate adenylyl transferase:[3]
- ThDP + ATP (ADP) ↔ AThTP + PPi (Pi)
Structure and function
The molecule is made up of thiamine and adenosine joined together with phosphate groups. It is similar in structure to NAD+. The function of AThTP is not currently know but it has been shown to inhibit the activity of PARP-1.[2]
References
- ↑ Bettendorff L, Wirtzfeld B, Makarchikov AF, et al. (2007). "Discovery of a natural thiamine adenine nucleotide". Nat. Chem. Biol. 3 (4): 211–2. PMID 17334376. doi:10.1038/nchembio867.
- 1 2 Tanaka T, Yamamoto D, Sato T, Tanaka S, Usui K, Manabe M, Aoki Y, Iwashima Y, Saito Y, Mino Y, Deguchi H (2011). "Adenosine thiamine triphosphate (AThTP) inhibits poly(ADP-ribose) polymerase-1(PARP-1) activity". J Nutr Sci Vitaminol (Tokyo). 57 (2): 192–6. PMID 21697640.
- ↑ Makarchikov AF, Brans A & Bettendorff L (2007). "Thiamine diphosphate adenylyl transferase from E. coli: functional characterization of the enzyme synthesizing adenosine thiamine triphosphate". BMC Biochem. 8: 17. PMC 1976097
. PMID 17705845. doi:10.1186/1471-2091-8-17.
External links
- "A first for vitamins". Nature. 446 (7132): 112. 2007. doi:10.1038/446112a.
- Jordan F (2007). "Adenosine triphosphate and thiamine cross paths". Nat. Chem. Biol. 3 (4): 202–3. PMID 17372602. doi:10.1038/nchembio0407-202.