Streptomycin-6-phosphatase

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In enzymology, a streptomycin-6-phosphatase (EC 3.1.3.39) is an enzyme that catalyzes the chemical reaction

streptomycin 6-phosphate + H₂O $\rightleftharpoons$ streptomycin + phosphate

Thus, the two substrates of this enzyme are streptomycin 6-phosphate and H₂O, whereas its two products are streptomycin and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is streptomycin-6-phosphate phosphohydrolase. Other names in common use include streptomycin 6-phosphate phosphatase, streptomycin 6-phosphate phosphohydrolase, and streptomycin-6-P phosphohydrolase. This enzyme participates in streptomycin biosynthesis.

[edit] References

IUBMB entry for 3.1.3.39
BRENDA references for 3.1.3.39 (Recommended.)
PubMed references for 3.1.3.39
PubMed Central references for 3.1.3.39
Google Scholar references for 3.1.3.39
Walker JB, Skorvaga M (1973). "Streptomycin biosynthesis and metabolism. Phosphate transfer from dihydrostreptomycin 6-phosphate to inosamines, streptamine, and 2-deoxystreptamine". J. Biol. Chem. 248: 2441–6. PMID 4121457.
Walker MS, Walker JB (1971). "Streptomycin biosynthesis. Separation and substrate specificities of phosphatases acting on guanidinodeoxy-scyllo-inositol phosphate and streptomycin-(streptidino)phosphate". J. Biol. Chem. 246: 7034–40. PMID 4331203.