| dihydrostreptomycin-6-phosphate 3'-alpha-kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.88 | ||||||||
| CAS no. | 39391-14-5 | ||||||||
| 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 dihydrostreptomycin-6-phosphate 3'alpha-kinase (EC 2.7.1.88) is an enzyme that catalyzes the chemical reaction
- ATP + dihydrostreptomycin 6-phosphate ADP + dihydrostreptomycin 3'alpha,6-bisphosphate
Thus, the two substrates of this enzyme are ATP and dihydrostreptomycin 6-phosphate, whereas its two products are ADP and dihydrostreptomycin 3'alpha,6-bisphosphate.
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:dihydrostreptomycin-6-phosphate 3'alpha-phosphotransferase. Other names in common use include dihydrostreptomycin 6-phosphate kinase (phosphorylating), and ATP:dihydrostreptomycin-6-P 3'alpha-phosphotransferase.
References
- 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.
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