Autotrophy in Nitrosocystis oceanus.
Enzymatic assays of cell-free extracts of the ammonia-oxidizing bacterium Nitrosocystis oceanus failed to establish that the biochemical basis of its obligate autotrophy stemmed solely from a metabolic defect. All of the Embden-Meyerhof enzymes except phosphofructokinase, and all of the tricarboxylic acid-cycle enzymes, as well as reduced nicotinamide adenine dinucleotide oxidase, were found in these extracts. A phosphoenolpyruvate-CO(2)-fixing system was also demonstrated. Resting cells incubated with (14)C-d-glucose and (14)C-l-glutamate and cells grown in the presence of (14)C-labeled glucose, glutamate, pyruvate, and methionine incorporated these compounds into cellular material, but at a level too low to provide the cells' major carbon and energy needs.
D001419:Bacteria / Q000201:enzymology / Q000378:metabolism*; D002245:Carbon Dioxide / Q000378:metabolism; D002247:Carbon Isotopes; D002952:Citric Acid Cycle; D005947:Glucose / Q000378:metabolism; D005971:Glutamates / Q000378:metabolism; D006038:Glyoxylates / Q000378:metabolism; D008660:Metabolism; D008715:Methionine / Q000378:metabolism; D010101:Oxygen Consumption; D011773:Pyruvates / Q000378:metabolism
D002247:Carbon Isotopes; D005971:Glutamates; D006038:Glyoxylates; D011773:Pyruvates; D002245:Carbon Dioxide; D008715:Methionine; D005947:Glucose