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Y Aharonowitz

Publications and source records attributed to Y Aharonowitz.

46 records · Page 3Linked to original sources
PubMed1979

Nitrogen nutrition and regulation of cephalosporin production in Streptomyces clavuligerus.

When used as sole nitrogen source, certain amino acids (e.g., proline, asparagine) supported both growth and sporulation by Streptomyces clavuligerus streaked onto solid defined medium. Ammonium supported growth but suppressed sporulation. Amino nitrogen was best for cephalosporin production in liquid defined medium, although urea was almost as useful. A comparison of amino acids showed asparagine and glutamine to be the best nitrogen sources and arginine to be almost as good. Ammonium salts supported a somewhat lower growth rate than asparagine, but antibiotic production was very poor on these inorganic nitrogen sources. Addition of ammonium to asparagine did not affect growth rate but increased mycelial mass; cephalosporin production was reduced by about 75%. Antibiotic production was more closely associated with growth in the absence of ammonium than in its presence, indicating a strong inhibitory and (or) repressive effect of NH4+ on antibiotic production. Ammonium exerted its negative effect when added at 24h or earlier, i.e. before antibiotic formation began.

Amino Acids↗
PubMed1978

Carbon catabolite regulation of cephalosporin production in Streptomyces clavuligerus.

Cephalosporin production by Streptomyces clavuligerus is regulated by some type of carbon catabolite control. Increasing concentrations of preferred carbon sources, such as glycerol and maltose, decreased production of the antibiotics. Poorer carbon sources, such as alpha-ketoglutarate and succinate, led to high specific production of cephalosporins and shifted the dynamics of fermentation to a greater degree of association with growth. The results support the concept that the phase in which a product is made by a microorganism is not a function of the particular molecule produced, but rather of the nutritional environment presented to the organism.

Amino Acids↗
PubMed1977

Influence of inorganic phosphate and organic buffers on cephalosporin production by Streptomyces clavuligerus.

A high concentration of potassium phosphate (75--100 mM) stabilized pH and supported extensive growth of Streptomyces clavuligerus in a chemically defined medium; such a concentration also inhibited cephalosporin production. Although Tris buffer was found to have detrimental effects on growth and antibiotic production, 3-(N-morpholine)-propane sulfonate (MOPS) or 2-(NP-morpholine)-ethane sulfonate (MES) buffer provided a nontoxic buffering system. In the presence of MOPS buffer, cephalosporin production was optimal at 25 mM phosphate, whereas higher concentrations of phosphate progressively inhibited antibiotic production up to 85% without modifying the pH pattern. MOPS buffer can be used to conduct fermentations at a relatively constant pH value in shake flasks.

Alkanesulfonates↗
PubMed1976

Translocation in Bacillus subtilis: characterization of elongation factor G by peptidyl-[3H]puromycin synthesis.

This communication describes the characterization of elongation factor G from Bacillus subtilis by the translocation of "native" peptide donors. Translocation was followed by elongation factor G-dependent increase in the synthesis of peptidyl-[3H]puromycin using "washed" ribosomes carrying in vivo-bound peptidyl-transfer ribonucleic acid ("native" peptidyl-transfer ribonucleic acid) molecules as peptide donors. Such ribosomes were obtained from cell extracts by washing at a high salt concentration. The use of "native" peptide donors facilitated the study of translocation under conditions that are closer to the in vivo state than those in the methods previously employed.

Bacillus subtilis↗
PubMedDate not supplied

Recent advances in the structure and function of isopenicillin N synthase.

Isopenicillin N synthase is a key enzyme in the biosynthesis of penicillin and cephalosporin antibiotics, catalyzing the oxidative ring closure of delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine to form isopenicillin N. Recent advances in our understanding of the unique chemistry of this enzyme have come through the combined application of spectroscopic, molecular genetic and crystallographic approaches and led to important new insights into the structure and function of this enzyme. Here we review new information on the nature of the endogenous ligands that constitute the ferrous iron active site, sequence evidence for a novel structural motif involved in iron binding in this and related non-heme iron dependent dioxygenases, crystal structure studies on the enzyme and its substrate complex and the impact of these and site-directed mutagenesis studies for unraveling the mechanism of the isopenicillin N synthase reaction.

Amino Acid Sequence↗