Literature DB >> 361398

Enzymic and chemical synthesis of epilson-N-(L-propionyl-2)-L-lysine.

M Fujioka, M Tanaka.   

Abstract

Pyruvate was shown to act as an oxo acid substrate in the reverse direction of saccharopine dehydrogenase [epsilon N-(L-glutaryl-2)-L-lysine: NAD oxidoreductase (L-lysine-forming)] reaction. The enzymic condensation product of lysine and pyruvate was isolated and identified as epsilon-N-(L-propionyl-2)-L-lysine by comparison with the synthetic compound. A method for the chemical preparation of diastereoisomers of epsilon-N-(propionyl-2)-L-lysine is also described.

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Year:  1978        PMID: 361398     DOI: 10.1111/j.1432-1033.1978.tb12603.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  Comprehensive analysis of maillard protein modifications in human lenses: effect of age and cataract.

Authors:  Mareen Smuda; Christian Henning; Cibin T Raghavan; Kaid Johar; Abhay R Vasavada; Ram H Nagaraj; Marcus A Glomb
Journal:  Biochemistry       Date:  2015-04-07       Impact factor: 3.162

2.  Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae.

Authors:  Hengyu Xu; Ann H West; Paul F Cook
Journal:  Biochemistry       Date:  2007-06-02       Impact factor: 3.162

3.  Glycation-mediated protein crosslinking and stiffening in mouse lenses are inhibited by carboxitin in vitro.

Authors:  Sandip K Nandi; Johanna Rankenberg; Stefan Rakete; Rooban B Nahomi; Marcus A Glomb; Mikhail D Linetsky; Ram H Nagaraj
Journal:  Glycoconj J       Date:  2020-11-27       Impact factor: 3.009

  3 in total

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