Affiliation:
1. Institute of Marine Science, University of Alaska, College, Alaska
2. Department of Microbiology, Oregon State University, Corvallis, Oregon
3. Department of Oceanography, Oregon State University, Corvallis, Oregon
Abstract
Burton, Sheril
D. (Institute of Marine Science, University of Alaska, College),
Richard Y. Morita, and Wayne Miller
. Utilization of acetate by
Beggiatoa
. J. Bacteriol.
91:
1192–1200. 1966.—A proposed system which would permit acetate incorporation into four-carbon compounds without the presence of key enzymes of the citric acid cycle or glyoxylate cycle is described. In this system, acetyl-coenzyme A (CoA) is condensed with glyoxylate to form malate, which, in turn, is converted to oxaloacetate. Oxaloacetate then reacts with glutamate to produce α-ketoglutarate, which is subsequently converted to isocitrate. Cleavage of isocitrate produces glyoxylate and succinate. Thus, the proposed system is similar to the glyoxylate bypass in that malate is produced from glyoxylate and acetyl-CoA, but differs from both the citric acid cycle and the glyoxylate bypass, since citrate and fumarate are not involved. Fumarase, aconitase, catalase, citritase, pyruvate kinase, enolase, phosphoenolpyruvate carboxylase, lactic dehydrogenase, α-ketoglutarate dehydrogenase, and condensing enzyme were not detectable in crude extracts of
Beggiatoa
. Succinate was oxidized by a soluble enzyme not associated with an electron-transport particle. Isocitrate was identified as the sole compound labeled when C
14
O
2
was added to a reduced nicotinamide adenine dinucleotide, CO
2
generating system (crystalline glucose-6-phosphate dehydrogenase and glucose-6-phosphate) in the presence of α-ketoglutarate.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
22 articles.
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