Streptomycin 6-kinase
| streptomycin 6-kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.72 | ||||||||
| CAS no. | 37278-11-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a streptomycin 6-kinase (EC 2.7.1.72) is an enzyme that catalyzes the chemical reaction
- ATP + streptomycin ADP + streptomycin 6-phosphate
Thus, the two substrates of this enzyme are ATP and streptomycin, whereas its two products are ADP and streptomycin 6-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:streptomycin 6-phosphotransferase. Other names in common use include streptidine kinase, SM 6-kinase, streptomycin 6-kinase (phosphorylating), streptidine kinase (phosphorylating), streptomycin 6-O-phosphotransferase, and streptomycin 6-phosphotransferase.
This enzyme participates in streptomycin biosynthesis when it acts on streptidine. It participates in streptomycin resistance when it acts on the analogous position of streptomycin.[1]
References
- ↑ Pierpersberg, W; Distler, J; Heinzel, P; Perez-Gonzalaez, JA (1988). "Antibiotic resistance by modification: Many resistance genes could be derived from cellular control genes in actinomycetes - a hypothesis". Actinomycetologica. 2 (2): 83–98. doi:10.3209/saj.2_83.
- Walker JB, Skorvaga M (1973). "Phosphorylation of streptomycin and dihydrostreptomycin by Streptomyces. Enzymatic synthesis of different diphosphorylated derivatives". J. Biol. Chem. 248 (7): 2435–40. doi:10.1016/S0021-9258(19)44127-6. PMID 4121456.
- Walker JB, Walker MS (1967). "Streptomycin biosynthesis. Enzymatic synthesis of O-phosphorylstreptidine from streptidine and adenosinetriphosphate". Biochim. Biophys. Acta. 148 (2): 335–41. doi:10.1016/0304-4165(67)90128-6. PMID 6075410.