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A catalase from Streptomyces coelicolor A3(2)

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).

Author: Hunter, Iain S., Walker, G.E., Dunbar, Bryan, Nimmo, Hugh G., Coggins, John R.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
Microbial enzymes

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Propionyl-CoA carboxylase from Streptomyces coelicolor A3(2): cloning of the gene encoding the biotin-containing subunit

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.

Author: Hunter, Iain S., Nimmo, Hugh G., Coggins, John R., Bramwell, Helena
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
Enzymes, Enzyme structure-activity relationships, Cell metabolism

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Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa

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.

Author: Hunter, Iain S., Dunbar, Bryan, Nimmo, Hugh G., Coggins, John R., Walker, Graeme E.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
Amino acid sequence, Amino acid sequencing

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Subjects list: Research, Streptomyces
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