PMID: 5001321May 1, 1971

Relationship between alkaline phosphatase and neomycin formation in Streptomyces fradiae

The Biochemical Journal
M K Majumdar, S K Majumdar


Studies on phosphatase activity of Streptomyces fradiae 3535 grown in three different media indicate that neomycin formation varies directly with enzyme activity, sodium nitrate-maltose-mineral salts medium giving the highest yields of alkaline phosphatase and neomycin. S. fradiae contains more than one alkaline phosphatase and the phosphatase responsible for hydrolysis of neomycin phosphate appears to be substrate specific. The same enzyme apparently hydrolyses both the N-P and P-O-P bonds of neomycin pyrophosphate. The enzyme is stimulated by Ca(2+), is inactive at a pH below 7 and is inhibited by EDTA. Enzymic activity increases when mycelia are incubated in mineral salts medium, but decreases when phosphate or glucose is included in the medium, although the latter is more effective. The inhibitory effect of EDTA on neomycin formation by resting mycelia is completely reversed by Ca(2+).


May 1, 1975·CRC Critical Reviews in Microbiology·H A Lechevalier
Jul 23, 2002·Biological & Pharmaceutical Bulletin·Masayuki NittaYoshio Okawa
Jan 1, 1983·Zeitschrift für allgemeine Mikrobiologie·P J MüllerJ H Ozegowski
Jan 1, 1986·Journal of Basic Microbiology·S Kretschmer
Jan 1, 1983·Zeitschrift für allgemeine Mikrobiologie·P J MüllerH Bocker

Related Concepts

Alkaline Phosphatase
Edetic Acid, Calcium, Sodium Salt
Anhydrous Dextrose
Hydrogen-Ion Concentration

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