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- W2082164954 abstract "The aerobic metabolism of β-amino-n-butyric acid was studied with cell-free extracts of a strain of Pseudomonas putida isolated in pure culture through enrichment from a liquid medium containing DL-β-amino-n-butyrate as the sole energy source. The extracts catalyze the decomposition of L-(+)-β-amino-n-butyrate in the presence of pyruvate. D-(−)-β-amino-n-butyrate is not decomposed and does not inhibit the deamination of the L-isomer. The products of the transamination reaction are aceto- acetate and alanine. Experiments on the substrate specificity of the transaminase activity showed that other β- and γ-amino acids can serve as efficient amino donors, whereas corresponding α-amino acids are poor substrates. The further metabolism of acetoacetate is discussed on the basis of the demonstration of acetoacetyl-CoA: succinyl-CoA transferase and acetoacetyl-CoA thiolase activities in the crude extracts as well as activities of glyoxylate cycle enzymes. A complete reaction scheme for the ultimate conversion of β-amino-n-butyric acid to succinate is presented and discussed." @default.
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- W2082164954 date "1971-05-01" @default.
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- W2082164954 title "Aerobic metabolism of β-amino-n-butyric acid by Pseudomonas putida" @default.
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- W2082164954 doi "https://doi.org/10.1016/0304-4165(71)90319-9" @default.
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