Dihydrostreptomycin-6-phosphate 3'alpha-kinase

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
dihydrostreptomycin-6-phosphate 3'-alpha-kinase
Identifiers
EC no.2.7.1.88
CAS no.39391-14-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.