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At least 19 recordsLinked to original sources

PubMed1989

[Oleandomycin and its natural and synthetic analogs. II. Structure and properties of oleandomycin B, a new compound of the oleandomycin group].

The revealed regularities of mass spectroscopic disintegration of oleandomycin and its derivatives made it possible to determine analytic criteria for identification of compounds related by their structure to oleandomycin. Analysis of the extracts from oleandomycin fermentation broth filtrates on the basis of the selected group of diagnostic ions showed that along with the main antibiotic there formed during the biosynthesis oleandomycin B, a structurally close minor component. The structure of the substance was assigned and its physico-chemical and biological properties were studied.

Chemical Phenomena↗

PubMed1989

[Oleandomycin and its natural and synthetic analogs. I. Dissociative ionization of oleandomycin and its derivatives].

Regularities of dissociative ionization of compounds belonging to the oleandomycin group were studied. Mass spectra of oleandomycin and some of its derivatives including anhydrooleandomycin, oleandomycin chlorhydrine, desoleandomycin, oleandomycin oxide, trimethylsilyl and acetyl derivatives were analyzed comparatively. Directions of disintegration with breakage of the glycoside bonds, macrolactone and carbon cycles were detected. The data are useful in structural analysis of not described oleandomycin-related compounds formed during biosynthesis and isolation of the main product.

Chemical Phenomena↗

PubMed1995

Biosynthesis of the macrolide oleandomycin by Streptomyces antibioticus. Purification and kinetic characterization of an oleandomycin glucosyltransferase.

The oleandomycin (OM) producer, Streptomyces antibioticus, possesses a mechanism involving two enzymes for the intracellular inactivation and extracellular reactivation of the antibiotic. Inactivation takes place by transfer of a glucose molecule from a donor (UDP-glucose) to OM, a process catalyzed by an intracellular glucosyltransferase. Glucosyltransferase activity is detectable in cell-free extracts concurrent with biosynthesis of OM. The enzyme has been purified 1,097-fold as a monomer, with a molecular mass of 57.1 kDa by a four-step procedure using three chromatographic columns. The reaction operates via a compulsory-order mechanism. This has been shown by steady-state kinetic studies using either OM or an alternative substrate (rosaramycin) and dead-end inhibitors, and isotopic exchange reactions at equilibrium. OM binds first to the enzyme, followed by UDP-glucose. A ternary complex is thus formed prior to transfer of glucose. UDP is then released, followed by the glycosylated oleandomycin (GS-OM).

Erythromycin↗

PubMed1997

Interaction between ATP, oleandomycin and the OleB ATP-binding cassette transporter of Streptomyces antibioticus involved in oleandomycin secretion.

The OleB protein of Streptomyces antibioticus, oleandomycin (OM) producer, constitutes an ATP-binding cassette transporter containing two nucleotide-binding domains and is involved in OM resistance and its secretion in this producer strain. We have characterized some properties of the first nucleotide-binding domain of OleB using an overexpressed fusion protein (MBP-OleB') between a maltose-binding protein (MBP) and the first half of OleB (OleB'). Extrinsic fluorescence of the base-modified fluorescent nucleotide analogue 1,N6-ethenoadenosine 5'-triphosphate (epsilon ATP) and 2'(3')-o-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate was determined in the presence of MBP and the fusion protein MBP-OleB', and it was found that epsilon ATP binds to MBP-OleB' with a stoichiometry of 0.9. Measurements of the intrinsic fluorescence of the MBP-OleB' fusion protein indicated that ATP induces a decrease in the accessibility of the MBP-OleB' tryptophans to acrylamide, an indication of a folding effect. This conclusion was confirmed by the fact that ATP also induces considerable stabilization against guanidine chloride denaturation of MBP-OleB'. Two effects were found to be associated with the presence of Mg2+ ions: (1) an increase in the quenching of MBP-OleB' intrinsic fluorescence by ATP; and (2) an increase in the accessibility of MBP-OleB' tryptophans to acrylamide. Significant changes in the intrinsic fluorescence of the fusion protein were also observed in the presence of OM, demonstrating the existence of interaction between the transporter and the antibiotic in the absence of any hydrophobic membrane component.

ATP-Binding Cassette Transporters↗

PubMed1962