[Isolation and substrate specificity of neomycin (paromomycin)--phosphotransferase from Actinomyces fradiae, a producer of neomycin].
Neomycin (paromomycin) phosphotransferase was isolated from the mycelium and fermentation broth filtrates of Act. fradiae. The substance was partially purified by means of fractionation with ammonium sulphate followed by gel-filtration through Sefadex G-100. The extracellular and intracellular forms of the enzyme had the same substrate specificity and used only neomycin and paromomycin as substrates. The other aminoglycosides, including kanamycins A and B, lividomycin and ribostamycin were not used. The both forms had the same thermolability. The intracellular form of the enzyme was detected in the mycelium at the early stages of the organism development, while the extracellular form was found in detectable amounts in the culture medium only at the late stages of the actinomycete development. Therefore, the neomycin-producing organism, i.e. Act. fradiae had one enzyme which phosphorilated neomycin and paromomycin and was excreted from the mycellium into the culture medium during the fermentation process.
D000255:Adenosine Triphosphate; D004789:Enzyme Activation; D008274:Magnesium; D009355:Neomycin / Q000037:antagonists & inhibitors / Q000096:biosynthesis* / Q000378:metabolism; D010085:Oxidative Phosphorylation; D010303:Paromomycin / Q000378:metabolism*; D010770:Phosphotransferases / Q000302:isolation & purification* / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D013997:Time Factors
D010303:Paromomycin; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D009355:Neomycin; D008274:Magnesium
Vydelenie i substratnaia spetsifichnost' neomitsin (paromomitsin)--fosfotransferazy iz Actinomyces fradiae--produtsenta neomitsina.