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Aminoglycoside 3'-phosphotransferases I and II in Pseudomonas aeruginosa.

Aminoglycoside 3'-phosphotransferases I and II in three strains of Pseudomonas aeruginosa were studied in comparison with those in two strains of R factor-carrying Escherichia coli. The strain TI-13 of P. aeruginosa produced the former and strain H-9 the latter. Strain B-13 produced the both enzymes. The 3'-phosphotransferases of type I in P. aeruginosa TI-13, B-13 and E. coli K12 J5 R11-2 were different from each other in chromatographic behavior, molecular weight, pH optimum, and Ii. The 3'-phosphotransferase of type II in P. aeruginosa H-9 and E. coli JR66/W677 showed the same behavior.

Aminoglycosides↗

Biotransformation, a new approach to aminoglycoside biosynthesis. I. Sisomicin.

Utilizing a mutant of Micromonospora inyoensis which requires the addition of 2-deoxystreptamine for sisomicin production, the bioconversion of 2-deoxstreptamine containing pseudodisaccharides and pseudotrisaccharides into sisomicin was demonstrated. The trisaccharides tested were structurally related minor components found in the sisomicin or gentamicin fermentations. Based upon the specificity of the structural configuration of those compounds which were converted to sisomicin versus those which were not, a pathway for the biosynthesis of sisomicin is proposed.

Aminoglycosides↗

Aminoglycoside 3'-phosphotransferase III, a new phosphotransferase. Resistance mechanism.

The aminoglycoside phosphotransferase of Pseudomonas aeruginosa 21-75 was purified by affinity chromatography using dibekacin-Sephadex 4B or lividomycin A-Sepharose 4B followed by DEAE Sephadex A-50 chromatography. It had activities of both the known aminoglycoside 3'-phosphotransferases I and II, and transferred phosphate from ATP to the 3'-hydroxyl group of kanamycin A, ribostamycin and butirosin A and 5-hydroxyl group of lividomycin A. This enzyme was designated aminoglycoside 3'-phosphotransferase III. It showed strong substrate inhibition by kanamycin A and ribostamycin when their concentration exceeded 6 muM. Purification and characterization of this enzyme are reported.

Aminoglycosides↗

Comparative study of field desorption and secondary ion mass spectra for antibiotics.

Nonvolatile and thermolabile antibiotics are investigated both by field desorption and by secondary ion mass spectrometry (SIMS). It has been successfully demonstrated that these two methods are complementary in obtaining informations about molecular weight and structure. Although FD is most widely used for the investigation of nonvolatile biologically active compounds, there are some compounds of which FD can not provide reliable information. SIMS is successfully applied to obtain structural information of these compounds. SIMS spectra frequently depend on the surface conditions of sample holder materials.

Aminoglycosides↗