Streptomycin 6-kinase

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In enzymology, a streptomycin 6-kinase (EC 2.7.1.72) is an enzyme that catalyzes the chemical reaction

ATP + streptomycin $\rightleftharpoons$ ADP + streptomycin 6-phosphate

Thus, the two substrates of this enzyme are ATP and streptomycin, whereas its two products are ADP and streptomycin 6-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 6-phosphotransferase. Other names in common use include streptidine kinase, SM 6-kinase, streptomycin 6-kinase (phosphorylating), streptidine kinase (phosphorylating), streptomycin 6-O-phosphotransferase, and streptomycin 6-phosphotransferase. This enzyme participates in streptomycin biosynthesis.

[edit] References

IUBMB entry for 2.7.1.72
BRENDA references for 2.7.1.72 (Recommended.)
PubMed references for 2.7.1.72
PubMed Central references for 2.7.1.72
Google Scholar references for 2.7.1.72
Walker JB, Skorvaga M (1973). "Phosphorylation of streptomycin and dihydrostreptomycin by Streptomyces. Enzymatic synthesis of different diphosphorylated derivatives". J. Biol. Chem. 248: 2435–40. PMID 4121456.
Walker JB, Walker MS (1967). "Streptomycin biosynthesis. Enzymatic synthesis of O-phosphorylstreptidine from streptidine and adenosinetriphosphate". Biochim. Biophys. Acta. 148: 335–41. PMID 6075410.