Pre-purified preparations of myoinositol-1-phosphate synthase (E.C. 5.5.1.4) from rat testes can be purified to homogeneity by first crystallizing the enzyme according to JAKOBY and then recrystallizing it at a pH value close to the isoelectric point while slowly increasing the temperature from 0 to
Myo-inositol-1-phosphate synthase from streptomyces griseus (Studies on the biosynthesis of cyclitols, XXXVIII1)
โ Scribed by Fritz Pittner; Irina I. Tovarova; Elena Ya. Kornitskaya; Aleksander S. Khokhlov; Otto Hoffmann-Ostenhof
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 271 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0300-8177
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โฆ Synopsis
It could be shown that Streptomyces griseus, the microorganism producing the antibiotic streptomycin and also mutant strains of this species that cannot synthesize streptomycin, possess myo-inositol-1-phosphate synthase (EC 5.5.1.4), the enzyme cyclizing D-glucose 6-phosphate. The enzyme isolated from that organism is extremely instable, its molecular weight is approximately 260,000, and it requires a divalent metal ion for its activity. This is the first instance that an enzyme of this specificity has been found in a prokaryotic organism.
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