Skip to main content
Article thumbnail
Location of Repository

Role of Ammonium Ion in the Biosynthesis of β-Nitropropionic Acid

By Paul D. Shaw and Anthony B. DeAngelo

Abstract

The metabolism of inorganic nitrogen compounds was studied in extracts of Penicillium atrovenetum which had been grown under conditions in which β-nitropropionic acid (BNP) synthesis varied from 0 to 12.5 μmoles per ml. None of the extracts was able to oxidize ammonium ion or nitrite. An enzyme was detected which catalyzed the oxidation of hydroxylamine with cytochrome c as the electron acceptor. The activity of this enzyme was not related to the ability of the organism to produce BNP. Nitrate and nitrite reductase activities were detected only in P. atrovenetum cultures grown on nitrate as a nitrogen source. These results indicated that BNP synthesis is probably not directly associated with the metabolism of inorganic nitrogen compounds and that an organic pathway for the formation of the nitro group is more likely. The activities of certain enzymes related to the metabolism of aspartic acid were investigated. Aspartate ammonia-lyase activity could not be detected in P. atrovenetum extracts. Aspartate aminotransferase and glutamate dehydrogenase activities were found in the extracts but were highest in the cultures which did not produce BNP. β-Nitroacrylic acid reductase activity was highest in extracts of cultures which were actively synthesizing BNP

Topics: Microbial Physiology and Metabolism
Year: 1969
OAI identifier: oai:pubmedcentral.nih.gov:250039
Provided by: PubMed Central
Sorry, our data provider has not provided any external links therefore we are unable to provide a link to the full text.

Suggested articles


To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.