@article{mbs:/content/journal/micro/10.1099/00221287-78-2-319, author = "Roberts, Barbara K. and Midgley, M. and Dawes, E. A.", title = "The Metabolism of 2-Oxogluconate by Pseudomonas aeruginosa", journal= "Microbiology", year = "1973", volume = "78", number = "2", pages = "319-329", doi = "https://doi.org/10.1099/00221287-78-2-319", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-78-2-319", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "SUMMARY: The 2-oxogluconate kinase and 2-oxogIuconate 6-phosphate reductase of Pseudomonas aeruginosa were purified approx. 100-fold. The activities of these enzymes, and a 2-oxogluconate transport system, were induced when the organism was grown on glucose, gluconate or 2-oxogluconate but were absent when the organism was grown on glycerol, succinate or citrate. Gluconate dehydrogenase is membrane-bound and acts extracellularly.", }