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. 1967 Nov;105(2):663–667. doi: 10.1042/bj1050663

The dimerization of Δ1-piperidine-2-carboxylic acid

D B Hope 1, K C Horncastle 1, R T Aplin 1
PMCID: PMC1198360  PMID: 5584009

Abstract

The l-amino acid oxidase of Mytilus edulis has been used to oxidize l-lysine on a large scale in the presence of catalase. The α-oxo acid derived from lysine cyclizes to a Schiff base, which readily dimerizes. The dimer undergoes spontaneous dehydration and decarboxylation to form 1,2,3,4,5,6,7,8-octahydropyrido[3,2-a]-indolizin-10(4bH)-one. This structure was established by a study of its molecular weight and infrared, nuclear-magnetic-resonance and mass spectra.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. HASSE K., MAISACK H. Die Reaktionsprodukte der enzymatischen Oxydation von Putrescin und Cadaverin. Biochem Z. 1955;327(4):296–304. [PubMed] [Google Scholar]
  2. Hope D. B., Horncastle K. C. The oxidation of lysine and oxalysine by Mytilus edulis: Identification of the products formed in the presence and the absence of catalase. Biochem J. 1967 Mar;102(3):910–916. doi: 10.1042/bj1020910. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. MEISTER A. The alpha-keto analogues of arginine, ornithine, and lysine. J Biol Chem. 1954 Feb;206(2):577–585. [PubMed] [Google Scholar]

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