| S-methyl-5-thioribose kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.100 | ||||||||
| CAS no. | 68247-56-3 | ||||||||
| 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 S-methyl-5-thioribose kinase (EC 2.7.1.100) is an enzyme that catalyzes the chemical reaction
- ATP + S-methyl-5-thio-D-ribose ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Thus, the two substrates of this enzyme are ATP and S-methyl-5-thio-D-ribose, whereas its two products are ADP and S-methyl-5-thio-alpha-D-ribose 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:S-methylmethyl-5-thio-D-ribose 1-phosphotransferase. Other names in common use include 5-methylthioribose kinase (phosphorylating), methylthioribose kinase, 5-methylthioribose kinase, and ATP:S5-methyl-5-thio-D-ribose 1-phosphotransferase. This enzyme participates in methionine metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 2OLC, 2PU8, 2PUI, 2PUL, 2PUN, and 2PUP.
References
- Ferro AJ, Barrett A, Shapiro SK (1978). "5-Methylthioribose kinase. A new enzyme involved in the formation of methionine from 5-methylthioribose". J. Biol. Chem. 253 (17): 6021–5. PMID 210167.
- Guranowski A (1983). "Plant 5-methylthioribose kinase". Plant Physiol. 71 (4): 932–935. doi:10.1104/pp.71.4.932. PMC 1066146. PMID 16662931.