Most cited article - PubMed ID 6125457
Properties of apyrase and inorganic pyrophosphatase in Streptomyces aureofaciens
Mycelia of a low- and a high-production strain of Streptomyces aureofaciens were converted into protoplasts and divided into five subcellular fractions in order to localize exopolyphosphatases (EC 3.6.1.11), triphosphatase (EC 3.6.1.25), inorganic diphosphatase (EC 3.6.1.1), apyrase (EC 3.6.1.5) and glucokinase (EC 2.7.1.2). The highest specific activity of enzymes hydrolyzing polyphosphates was found in cytoplasmic vesicles and membranes. Triphosphatase was detected in the periplasmic fraction. Periplasmic vesicles and cytoplasm exhibited a high activity of diphosphatase. Apyrase was found mainly in the fractions of membranes and cytoplasmic vesicles. Glucokinase was a cytoplasmic enzyme. The enzymes were released from membrane structures into cytoplasm or periplasmic space if benzyl thiocyanate (10 microM) was present in the growth medium.
- MeSH
- Potassium pharmacology MeSH
- Phosphoric Monoester Hydrolases metabolism MeSH
- Glucokinase metabolism MeSH
- Magnesium pharmacology MeSH
- Cations MeSH
- Kinetics MeSH
- Sodium pharmacology MeSH
- Streptomyces aureofaciens drug effects enzymology MeSH
- Subcellular Fractions enzymology MeSH
- Thiocyanates pharmacology MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- benzyl thiocyanate MeSH Browser
- Potassium MeSH
- Phosphoric Monoester Hydrolases MeSH
- Glucokinase MeSH
- Magnesium MeSH
- Cations MeSH
- Sodium MeSH
- Thiocyanates MeSH
ATP diphosphohydrolase activity and inorganic pyrophosphatase reached two maxima during cultivation of the low- and high-producing variant of Streptomyces aureofaciens under conditions of phosphate limitation, i.e. after 30 and 70 h of cultivation. Increased levels of inorganic phosphate in a medium inhibitory to biosynthesis of chlortetracycline markedly decreased the levels of both enzymes. The ATP diphosphohydrolase activity was detected both in the supernatant and membrane fractions of the cell-free preparation of the mycelium.
- MeSH
- Apyrase metabolism MeSH
- Chlortetracycline biosynthesis MeSH
- Phosphoric Monoester Hydrolases metabolism MeSH
- Phosphates pharmacology MeSH
- Culture Media MeSH
- Membranes enzymology MeSH
- Pyrophosphatases metabolism MeSH
- Streptomyces enzymology MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Apyrase MeSH
- Chlortetracycline MeSH
- Phosphoric Monoester Hydrolases MeSH
- Phosphates MeSH
- Culture Media MeSH
- Pyrophosphatases MeSH