@article{mbs:/content/journal/micro/10.1099/00221287-93-2-259, author = "Taylor, I. J. and Anthony, C.", title = "A Biochemical Basis for Obligate Methylotrophy: Properties of a Mutant of Pseudomonasam1 lacking 2-Oxoglutarate Dehydrogenase", journal= "Microbiology", year = "1976", volume = "93", number = "2", pages = "259-265", doi = "https://doi.org/10.1099/00221287-93-2-259", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-93-2-259", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Summary: Pseudomonas am1 is a facultative methylotroph which grows on a wide range of carbon compounds. A mutant of Pseudomonas am1 (ict41) grew only on C1 compounds and is thus an artificial obligate methylotroph. Measurements of activities of the components of the 2-oxoglutarate dehydrogenase complex suggest that the E2 component (dihydrolipoamide transsuccinylase) is not functional. All other tricarboxylic acid cycle enzymes were present with activities comparable to those in wild-type Pseudomonas am1 and cytochrome levels were unchanged in the mutant. Suspensions of the mutant oxidized pyruvate, lactate, β-hydroxybutyrate, acetoacetate and 2-oxoglutarate at very low rates. By contrast, C1 compounds were oxidized at the same rate as in wild-type bacteria. Two revertants of ict41 which regained 2-oxoglutarate dehydrogenase activity also regained the ability to oxidize and grow on the same substrates as wild-type bacteria. It is concluded that lack of 2-oxoglutarate dehydrogenase may well be the basis of obligate methylotrophy in some bacteria.", }