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dc.contributor.advisor Walker, James B.
dc.creatorDrake, Nancy Jean
dc.date.accessioned 2018-12-18T21:20:59Z
dc.date.available 2018-12-18T21:20:59Z
dc.date.issued 1975
dc.identifier.urihttps://hdl.handle.net/1911/104324
dc.description.abstract The filamentous soil "bacterium, Streptomyces hygrosooplcus forma glebosus ATCC 1467 ( S. glebosus ), synthesizes the antibiotic bluensomycln, a monoguanidinated analogue of dihydrostreptomycin (DSM) Cell-free extracts of’ S, glebosus were found to synthesize mono- and diphosphorylated derivatives of dihydrostreptomycin. The diphosphorylated compound produced by S. glebosus differs from the diphosphorylated product (DSM-3 c,6-diP) produced by S. blklnlensls ATCC 1162, a streptomycin producer. The monophosphorylated dihydrostreptomycin is neither dihydrostreptomycin-6-p nor dihydrostreptomycin-3-P. It has the chromatographic mobilities and characteristics of dihydrostreptomycin-3-P. Dihydrostreptomycin-6-P, dihydrostreptomycln-3'6-P, dihydrostreptomycin-3'-Pt and the isolated monophosphorylated product could all be further phosphorylated to diphosphorylated dihydrostreptomycins by S. glebosus extracts. Streptomycin 6-kinase found in S. blklnlensls phosphorylated the monophosphorylated dihydrostreptomycin product from S. glebosus. The resulting dlpnosphorylated product had the chromatographic behavior of dihydrostreptomycln-3,6-dip No streptomycin-6-P phosphatase activity, which occurs in streptomycin producers, could he detected in S. glebosus. It is suggested that extracts of S. glebosus contain an ATPjdlhydrostreptomycin 3-phosphotransferase (3-kinase) (Reaction 1) and a somewhat less active ATPtdihydrostreptomycin 6-phosphotransferase (6-kinase) which phosphorylates the product of the 3-kinase (Reaction 2). MgATp + DSM 2ü-klnase ^ MgADp + DSM-3"-P (1) S. glebosus MgATP + DSM-3"-P -6~klnase ) MgADP + DSM-3,6-diP (2) S. glebosus If the structure of the product of Reaction 1 can be confirmed, for the first time a stable 3-kinase has been found in a Streptomyces. It is particularly curious, and might be significant, that Streptomyces which synthesize streptomycin contain a 3-kinase, whereas a strain which synthesizes a dihydrostreptomycin analogue contains a different kinase. Certain clinical isolates of E. coll and Pseudomonads containing R factors are resistant to streptomycin. The major streptomycin-inactivating reaction is the phosphorylation of streptomycin by a 3M-kinase. Therefore, S. glebosus might have a gene for a 3-kinase similar to that found in E. coll and Pseudomonads containing streptomycin-resistant plasmids. One evolutionary theory suggests that the two kinases are fragments of a dihydrostreptomycin biosynthetic pathway remaining in S. glebosus, the bluensomycin producer.
dc.format.extent 96 pp
dc.language.iso eng
dc.title Phosphorylated derivatives of dihydrostreptomycin produced by Streptomyces glebosus
dc.identifier.digital RICE1956
dc.type.genre Thesis
dc.type.material Text
thesis.degree.department Biochemistry and Cell Biology
thesis.degree.discipline Natural Sciences
thesis.degree.grantor Rice University
thesis.degree.level Masters
thesis.degree.name Master of Arts
dc.format.digitalOrigin reformatted digital
dc.identifier.callno Thesis Biochem. 1975 Drake
dc.identifier.citation Drake, Nancy Jean. "Phosphorylated derivatives of dihydrostreptomycin produced by Streptomyces glebosus." (1975) Master’s Thesis, Rice University. https://hdl.handle.net/1911/104324.


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