Literature DB >> 8674990

Energy production and peptidase activity in Eikenella corrodens.

N J Gully1, A H Rogers.   

Abstract

Eikenella corrodens 33EK(L), a clinical isolate, was assayed for its ability to utilise amino acids as substrates in the reduction of nitrate to nitrite. The metabolism of proline, glutamate, serine and glutamine was found to result in relatively high rates of nitrate reduction. The ability of cells to metabolise these amino acids from a variety of small peptides was also determined. E. corrodens was found to possess a relatively specific proline aminopeptidase as well as a putative carboxypeptidase activity for glutamate. Energy production in this organism appears to be via oxidative deamination of these key amino acids linked to a respiratory chain, with nitrate acting as the ultimate electron acceptor.

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Year:  1996        PMID: 8674990     DOI: 10.1111/j.1574-6968.1996.tb08204.x

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  1 in total

Review 1.  Resolving the Contradictory Functions of Lysine Decarboxylase and Butyrate in Periodontal and Intestinal Diseases.

Authors:  Martin Levine; Zsolt M Lohinai
Journal:  J Clin Med       Date:  2021-05-27       Impact factor: 4.241

  1 in total

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