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Biomedical subjects

J H Coats

Publications and source records attributed to J H Coats.

At least 19 recordsLinked to original sources
PubMed1992

Isolation and identification of 3-propylidene-delta 1-pyrroline-5-carboxylic acid, a biosynthetic precursor of lincomycin.

An accumulated lincomycin intermediate in UC 8292, a lincomycin nonproducing strain of Streptomyces lincolnensis, has been isolated and purified by employing an assay system based on complementation of UC 11066, another lincomycin nonproducing strain of S. lincolnensis. The structure of the purified intermediate is shown to be 3-propylidene-delta 1-pyrroline-5-carboxylic acid, or 1, 2, 3, 6-tetradehydro-propylproline by mass spectrometry and NMR spectroscopic studies. Based on the structure of this newly found intermediate, a biosynthetic pathway for propylproline is proposed as tyrosine-->L-3-hydroxytyrosine (Dopa)-->-->-->-->3-propylidene-delta 1-pyrroline-5-carboxylic acid-->3-propyl-delta 2-pyrroline-5-carboxylic acid-->propylproline.

Fermentation↗
PubMed1989

Microbial glycosylation of erythromycin A.

Erythromycin A (compound 1) was inactivated by Streptomyces vendargensis ATCC 25507 in fermentation. The inactivation product was isolated and characterized by nuclear magnetic resonance and mass spectroscopy as 2'-(O-[beta-D-glucopyranosyl])erythromycin A (compound 2). The MICs of compounds 1 and 2 were determined. Compound 2 lacked antibiotic activity when tested against several gram-positive pathogens, as well as S. vendargensis.

Chromatography, Thin Layer↗
PubMed1977

Microbial transformation of antibiotics. Clindamycin ribonucleotides.

Addition of clindamycin to whole-cell cultures of Streptomyces coelicolor Müller resulted in the loss of in vitro activity against organisms sensitive to clindamycin. Incubation of such culture filtrates with crude alkaline phosphatase generated a biologically active material identified as clindamycin. Fermentation broths containing inactivated clindamycin yielded clindamycin 3-ribonucleotides and clindamycin 3-phosphate the structure of which was established by physicochemical and enzymatic means. Attempts to transform clindamycin to clindamycin 3-ribonucleotides by lysates or partially purified enzyme preparations from S. coelicolor have failed.

Animals↗
PubMed1971

Genetic recombination in Streptomyces bikiniensis var. zorbonensis.

A genetic recombination system in Streptomyces bikiniensis var. zorbonensis is described. This strain produces a mixture of antibiotics including zorbamycin and zorbonomycin B and C. A genetic map has been constructed from data obtained from an analysis of haploid recombinants which shows linkage relationships of 17 marker loci. Determination of map location has been made for three different loci affecting antibiotic biosynthesis in this strain.

Amino Acids↗
PubMed1971

Microbial transformation of antibiotics: phosphorylation of clindamycin by Streptomyces coelicolor Müller.

Addition of clindamycin to whole-cell cultures of Streptomyces coelicolor Müller resulted in the loss of in vitro activity against organisms sensitive to clindamycin. Incubation of such culture filtrates with alkaline phosphatase generated a biologically active material identified as clindamycin. Fermentation broths containing inactivated clindamycin yielded clindamycin 3-phosphate, the structure of which was established by physical-chemical and enzymatic studies. Clindamycin was phosphorylated by lysates and partially purified enzyme preparations from S. coelicolor Müller. These reactions require a ribonucleoside triphosphate and Mg(2+). The product of the cell-free reactions was identified as clindamycin 3-phosphate.

Adenosine Triphosphate↗