Streptomycin 3"-kinase
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 | This article includes a list of references, related reading, or external links, but its sources remain unclear because it lacks inline citations. (August 2020) |
| streptomycin 3"-kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.87 | ||||||||
| CAS no. | 39391-15-6 | ||||||||
| 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 | ||||||||
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In enzymology, a streptomycin 3"-kinase (EC 2.7.1.87) is an enzyme that catalyzes the chemical reaction
- ATP + streptomycin ADP + streptomycin 3"-phosphate
Thus, the two substrates of this enzyme are ATP and streptomycin, whereas its two products are ADP and streptomycin 3''-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 3"-phosphotransferase. Other names in common use include streptomycin 3"-kinase (phosphorylating), and streptomycin 3"-phosphotransferase.
References[edit]
- 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. PMID 4121456.
