Subcellular localization of enzymes in Streptomyces aureofaciens and its alteration by benzyl thiocyanate. I: Phosphatases and ATP-glucokinase

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...

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Bibliographic Details
Published in:Folia microbiologica 1987, Vol.32 (5), p.402-410
Main Authors: TRILISENKO, L. V, NOVOTNA, J, ERBAN, V, BEHAL, V, HOSTALEK, Z, KULAEV, I. S
Format: Article
Language:English
Subjects:
Bacteriology
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Cations
Fundamental and applied biological sciences. Psychology
Glucokinase - metabolism
Kinetics
Magnesium - pharmacology
Metabolism. Enzymes
Microbiology
Mission oriented research
Phosphoric Monoester Hydrolases - metabolism
Physiology and metabolism
Potassium - pharmacology
Sodium - pharmacology
Streptomyces aureofaciens - drug effects
Streptomyces aureofaciens - enzymology
Subcellular Fractions - enzymology
Thiocyanates - pharmacology
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Summary: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.
ISSN:0015-5632
1874-9356