期刊
FEBS LETTERS
卷 584, 期 1, 页码 181-186出版社
WILEY
DOI: 10.1016/j.febslet.2009.11.055
关键词
Lysine; Metabolism; [N-15]labeling; Antiquitin; Pipecolic acid; alpha-Aminoadipic; Semialdehyde
The mammalian degradation of lysine is believed to proceed via two distinct routes, the saccharopine and the pipecolic acid routes, that ultimately converge at the level of alpha-aminoadipic semialdehyde (alpha-AASA). alpha-AASA dehydrogenase-deficient fibroblasts were grown in cell culture medium supplemented with either L-[alpha-N-15]lysine or L-[epsilon-N-15]lysine to explore the exact route of lysine degradation. L-[alpha-N-15]lysine was catabolised into [N-15]saccharopine, [N-15]alpha-AASA, [N-15]Delta(1)-piperideine-6-carboxylate, and surprisingly in [N-15]pipecolic acid, whereas L-[epsilon-N-15]lysine resulted only in the formation of [N-15]saccharopine. These results imply that lysine is exclusively degraded in. broblasts via the saccharopine branch, and pipecolic acid originates from an alternative precursor. We hypothesize that pipecolic acid derives from Delta(1)-piperideine-6-carboxylate by the action of Delta(1)-pyrroline-5-carboxylic acid reductase, an enzyme involved in proline metabolism. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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