Dihydrostreptomycin-6-phosphate 3'alpha-kinase
Appearance
dihydrostreptomycin-6-phosphate 3'-alpha-kinase | |||||||||
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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 | ||||||||
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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
[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.