Article Abstract:
Streptomyces coelicolor A3(2) produces a catalase which is a tetramere containing a M(sub r) 55000 subunit and the N-terminal and peptide sequence of this enzyme are similar to that of catalases produced by other microbes and mammals. This enzyme protects the cell during oxidative stress and increases during growth of the cell being maximum during the stationary phase. A southern blot analysis shows that only one catalase is present in Streptomyces coelicolor A3(2).
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Article Abstract:
Previous research has detected high activity of propionyl-CoA carboxylase (PCC) in cell-free extracts of Streptomyces coelicolor A3(2), suggesting that the enzyme plays a major role in S. coelicolor metabolism. To get a better idea of the precise role of PCC in S. coelicolor, PCC is purified and subjected to N-terminal sequencing. The gene encoding one of the subunits is cloned. It is shown that PCC has a significant impact on cellular metabolism in S. coelicolor.
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Article Abstract:
The Streptomyces and Neurospora 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) synthases are similar to plant DAHP synthases but are otherwise unrelated to other microbial DAHP synthase sequences. This was gleaned from the purification and characterization of the DAHP synthases from Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa and the determination of the N-terminal amino acid sequence for the enzymes.
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