3′-Phosphoadenosine-5′-phosphosulfate , or FAFS , is a derivative of adenosine monophosphate with a phosphoric acid residue in the 3′-position and a sulfo group attached to 5′- phosphate . This anion is a standard cofactor in all sulfo group transfer reactions. Formed from adenosine 5′-phosphosulfate (APS) by phosphorylation to the 3′-position [1] .
| 3′-Phosphoadenosine-5′-phosphosulfate | |
|---|---|
 | |
| Are common | |
| Systematic name | 6-amino-9 - [('' 2R, 3R, 4S, 5R '') - 3-hydroxy-5- [(hydroxy-sulfoxy-phosphoryl) oxymethyl] -4-phosphonoxy-tetrahydrofuran-2-yl] purine |
| Traditional names | FAFS phosphoadenosine phosphosulfate |
| Chem. formula | C 10 H 15 N 5 O 13 P 2 S |
| Physical properties | |
| Molar mass | 507.266 g / mol |
| Classification | |
| Reg. CAS number | |
| PubChem | |
| Reg. EINECS number | |
| Smiles | |
| Inchi | |
| Chebi | 17980 |
| ChemSpider | |
Synthesis and restoration
APS and FAFS are involved in the process of reducing sulfate to sulfite . This is an endothermic reaction carried out by bacteria and plant chloroplasts . Since sulfate cannot be directly reduced, it must be activated by reaction with ATP . As a result of the reaction, an activated sulfate APS carrier is formed, and then FAFS. The first reaction is carried out by the enzyme ATP-sulfurylase:
- SO 4 2− + ATF → APS + FF n
The conversion of APS to FAFS catalyzes the enzyme APS kinase :
- APS + ATP → FAFS + ADP
FAFS is used to synthesize sulfated compounds, that is, to transfer sulfo groups to them, and further restoration of the APS leads to the formation of sulfite and then hydrogen sulfide , which can be removed from the cell in the case of sulfur respiration (dissimilation sulfate reduction) or used for the synthesis of amino acids (assimilation sulfate reduction) [2] .
Notes
- ↑ Negishi M., Pedersen LG, Petrotchenko E. et al. Structure and function of sulfotransferases (English) // Archives of Biochemistry and Biophysics : journal. - Elsevier , 2001 .-- Vol. 390 , no. 2 . - P. 149-157 . - DOI : 10.1006 / abbi.2001.2368 . - PMID 11396917 .
- ↑ Ermakov, 2005 , p. 377.
Literature
- Plant Physiology / Ed. I.P. Ermakova. - M .: Academy, 2005 .-- 634 p.