Selenide, water dikinase
| selenide, water dikinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.9.3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a selenide, water dikinase (EC 2.7.9.3) is an enzyme that catalyzes the chemical reaction
- ATP + selenide + H2O AMP + selenophosphate + phosphate
The 3 substrates of this enzyme are ATP, selenide, and H2O, whereas its 3 products are AMP, selenophosphate, and phosphate.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases). The systematic name of this enzyme class is ATP:selenide, water phosphotransferase. This enzyme is also called selenophosphate synthetase. This enzyme participates in selenoamino acid metabolism.
Evolution
[edit]Vertebrates including humans carry two versions of this enzyme, with one (SEPHS2) being a selenoprotein and the other (SEPHS1) replacing it with a threonine, though still with a vestigial SECIS element. Analysis of animal versions of this enzyme show that the original animal version is a selenoprotein, with SEPHS1 arising later through gene duplication.[1]
Among prokaryotes, most bacteria have a version with cystine instad of selenocystine, suggesting that this may be the ancestral state (which would avoid the chicken-and-egg problem). Some have two versions, one with Sec and the other with Cys. Archaea mostly have the Sec version.[1]
References
[edit]- ^ a b Mariotti, M; Santesmasses, D; Capella-Gutierrez, S; Mateo, A; Arnan, C; Johnson, R; D'Aniello, S; Yim, SH; Gladyshev, VN; Serras, F; Corominas, M; Gabaldón, T; Guigó, R (September 2015). "Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization". Genome Research. 25 (9): 1256–67. doi:10.1101/gr.190538.115. hdl:10230/24968. PMC 4561486. PMID 26194102.
- Veres Z, Tsai L, Scholz TD, Politino M, Balaban RS, Stadtman TC (1992). "Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorus". Proc. Natl. Acad. Sci. U.S.A. 89 (7): 2975–9. Bibcode:1992PNAS...89.2975V. doi:10.1073/pnas.89.7.2975. PMC 48786. PMID 1557403.
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