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pubmed-article:25650pubmed:abstractTextN4-Ethyl-L-[u-14C]asparagine and L-[U-14C]aspartate give identical metabolites, mainly intermediates of the tricarboxylic acid cycle and related amino acids, in whole cells of Pseudomonas stutzeri. The labelled asparagine derivative is converted into [14C]-aspartate by cell-free extracts, and this reaction, which has an optimum pH of 8.8 +/- 0.2, is neither inhibited by unlabelled asparagine nor enhanced by unlabelled 2-oxoglutarate. No labelled keto acid corresponding to N4-ethylasparagine was detected in either whole cells or cell-free extracts. Thus N4-ethyl-L-asparagine, like asparagine, must be broken down by hydrolysis, at least in this bacterium.lld:pubmed
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pubmed-article:25650pubmed:authorpubmed-author:GrayD ODOlld:pubmed
pubmed-article:25650pubmed:authorpubmed-author:DineenR WRWlld:pubmed
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pubmed-article:25650pubmed:pagination487-93lld:pubmed
pubmed-article:25650pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:25650pubmed:articleTitleThe biochemical pathway for the breakdown of N4-ethyl-L-asparagine in the bacterium Pseudomonas stutzeri.lld:pubmed
pubmed-article:25650pubmed:publicationTypeJournal Articlelld:pubmed