Streptomycin 3"-kinase

streptomycin 3"-kinase
Identifiers
EC no.2.7.1.87
CAS no.39391-15-6
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
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NCBIproteins

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

The enzyme characterised from Streptomyces bacteria converts the antibiotic, streptomycin, to a monophosphate, streptomycin 3''-phosphate, by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1]

This enzyme is a transferases, specifically one 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.[2]

References

  1. ↑ 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.
  2. ↑ Enzyme 2.7.1.87 at KEGG Pathway Database.