Subcellular localization of enzymes in Streptomyces aureofaciens and its alteration by benzyl thiocyanate. I. Phosphatases and ATP-glucokinase
Language English Country United States Media print
Document type Journal Article
PubMed
2826319
DOI
10.1007/bf02887570
Knihovny.cz E-resources
- 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
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.
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