Phenylalanine and tyrosine metabolism in the facultative methylotroph Nocardia sp. 239 |
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Authors: | L. de Boer W. Harder L. Dijkhuizen |
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Affiliation: | (1) Department of Microbiology, University of Groningen, Kerklaan 30, NL-9751 NN Haren, The Netherlands |
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Abstract: | Nocardia sp. 239 is able to use l-tyrosine and both d- and l-phenylalanine as carbon-, energy- and nitrogen sources for growth. The catabolism of these compounds is by way of (4-hydroxy)phenylpyruvate and (4-hydroxy)-phenylacetate as intermediates and the pathways merge at the level of homogentisate. The conversion of the amino acids into (4-hydroxy)phenylpyruvate is catalyzed by an inducible NAD-dependent phenylalanine dehydrogenase and l-tyrosine aminotransferase, respectively. Incubation of the organism in media with l-phenylalanine plus phenyl-pyruvate resulted in diauxic growth, with phenylpyruvate used first. Phenylalanine dehydrogenase activity cold only be detected after depletion of phenylpyruvate, in the ensuing second growth phase on l-phenylalanine. During growth on phenylalanine plus methanol, low levels of phenylalanine dehydrogenase were detected and this resulted in simultaneous utilization of the two substrates. Following diepoxyoctane treatment, mutants of Nocardia sp. 239 affected in phenylalanine and phenylpyruvate degradation were isolated. Double mutants blocked in both phenylalanine dehydrogenase and phenylpyruvate decarboxylase completely failed to catabolize phenylalanine. The absence of these enzymes did not affect growth on tyrosine.Abbreviations RuMP ribulose monophosphate - EMS ethylmethanesulphonate - NTG N-methyl-N-nitro-N-nitrosoguanidine |
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Keywords: | Nocardia sp. 239 Aromatic amino acids font-variant:small-caps" >l-Phenylalanine font-variant:small-caps" >l-Tyrosine Phenylalanine dehydrogenase Phenylpyruvate decarboxylase Methanol Methylotrophs Regulation |
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