Adenosine thiamine triphosphate

Adenosine thiamine triphosphate
Names
	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
CAS Number	30632-11-2 (chloride) ;
3D model (JSmol)	Interactive image; Interactive image;
ChEBI	CHEBI:71394 ;
ChemSpider	13082023 ;
MeSH	adenosine+thiamine+triphosphate
PubChem CID	15938962;
CompTox Dashboard (EPA)	DTXSID40579927 ;
	InChI InChI=1S/C22H30N9O13P3S/c1-11-15(48-10-30(11)6-13-5-25-12(2)29-19(13)23)3-4-40-45(34,35)43-47(38,39)44-46(36,37)41-7-14-17(32)18(33)22(42-14)31-9-28-16-20(24)26-8-27-21(16)31/h5,8-10,14,17-18,22,32-33H,3-4,6-7H2,1-2H3,(H6-,23,24,25,26,27,29,34,35,36,37,38,39)/p+1/t14-,17-,18-,22-/m1/s1 Key: FGOYXNBJKMNPDH-SAJUPQAESA-O ; InChI=1/C22H30N9O13P3S/c1-11-15(48-10-30(11)6-13-5-25-12(2)29-19(13)23)3-4-40-45(34,35)43-47(38,39)44-46(36,37)41-7-14-17(32)18(33)22(42-14)31-9-28-16-20(24)26-8-27-21(16)31/h5,8-10,14,17-18,22,32-33H,3-4,6-7H2,1-2H3,(H6-,23,24,25,26,27,29,34,35,36,37,38,39)/p+1/t14-,17-,18-,22-/m1/s1 Key: FGOYXNBJKMNPDH-YLNAWJOLBZ;
	SMILES NC1=NC=NC2=C1N=CN2[C@H]3[C@H](O)[C@H](O)[C@@H](COP(OP(OP(OCCC4=C(C)[N+](CC5=CN=C(C)N=C5N)=CS4)(O)=O)(O)=O)(O)=O)O3; O=P(O)(OC[C@H]3O[C@@H](n1c2ncnc(N)c2nc1)[C@H](O)[C@@H]3O)OP(=O)(O)OP(=O)(O)OCCc4sc[n+](c4C)Cc5c(nc(nc5)C)N;
Properties
Chemical formula	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).
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	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 also exists in eukaryotic organisms such as yeast, roots of higher plants and animal tissues, albeit at a much lower concentration. 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 + PP_i (P_i)

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 known 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. doi:10.1038/nchembio867. PMID 17334376.
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. doi:10.3177/jnsv.57.192. 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. doi:10.1186/1471-2091-8-17. PMC 1976097. PMID 17705845.

External links

"A first for vitamins". Nature. 446 (7132): 112–113. 2007. doi:10.1038/446112a.
Jordan F (2007). "Adenosine triphosphate and thiamine cross paths". Nat. Chem. Biol. 3 (4): 202–3. doi:10.1038/nchembio0407-202. PMID 17372602.

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[1] Bettendorff L, Wirtzfeld B, Makarchikov AF, et al. (2007). "Discovery of a natural thiamine adenine nucleotide". Nat. Chem. Biol. 3 (4): 211–2. doi:10.1038/nchembio867. PMID 17334376.

[Tanaka_2011-2] 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. doi:10.3177/jnsv.57.192. PMID 21697640.

[3] 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. doi:10.1186/1471-2091-8-17. PMC 1976097. PMID 17705845.