In enzymology, a tRNA sulfurtransferase (EC 2.8.1.4) is an enzyme that catalyzes the chemical reaction
| tRNA sulfurtransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.8.1.4 | ||||||||
| CAS no. | 9055-57-6 | ||||||||
| 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 | ||||||||
| |||||||||
- L-cysteine + 'activated' tRNA L-serine + tRNA containing a thionucleotide
Thus, the two substrates of this enzyme are L-cysteine and 'activated' tRNA, whereas its two products are L-serine and tRNA containing a thionucleotide.
This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is L-cysteine:tRNA sulfurtransferase. Other names in common use include transfer ribonucleate sulfurtransferase, RNA sulfurtransferase, ribonucleate sulfurtransferase, transfer RNA sulfurtransferase, and transfer RNA thiolase.
References
edit- Abrell JW, Kaufman EE, Lipsett MN (1971). "The biosynthesis of 4-thiouridylate. Separation and purification of two enzymes in the transfer ribonucleic acid-sulfurtransferase system". J. Biol. Chem. 246 (2): 294–301. doi:10.1016/S0021-9258(18)62490-1. PMID 5541999.
- Hayward RS, Weiss SB (1966). "RNA thiolase: the enzymatic transfer of sulfur from cysteine to sRNA in Escherichia coli extracts". Proc. Natl. Acad. Sci. U.S.A. 55 (5): 1161–8. doi:10.1073/pnas.55.5.1161. PMC 224294. PMID 5334200.
- Lipsett MN, Peterkofsky A (1966). "Enzymatic thiolation of E. coli sRNA". Proc. Natl. Acad. Sci. U.S.A. 55 (5): 1169–74. doi:10.1073/pnas.55.5.1169. PMC 224295. PMID 5334201.
- Wong TW, Weiss SB, Eliceiri GL, Bryant J (1970). "Ribonucleic acid sulfurtransferase from Bacillus subtilis W168 Sulfuration with beta-mercaptopyruvate and properties of the enzyme system". Biochemistry. 9 (11): 2376–86. doi:10.1021/bi00813a024. PMID 4987417.
