Ketimine reductase/CRYM catalyzes reductive alkylamination of α-keto acids, confirming its function as an imine reductase

André Hallen*, Arthur J L Cooper, Jason R. Smith, Joanne F. Jamie, Peter Karuso

*Corresponding author for this work

Research output: Contribution to journalArticle

6 Citations (Scopus)


Recently, crystalized mouse ketimine reductase/CRYM complexed with NADPH was found to have pyruvate bound in its active site. We demonstrate that the enzyme binds α-keto acids, such as pyruvate, in solution, and catalyzes the formation of N-alkyl-amino acids from alkylamines and α-keto acids (via reduction of imine intermediates), but at concentrations of these compounds not expected to be encountered in vivo. These findings confirm that, mechanistically, ketimine reductase/CRYM acts as a classical imine reductase and may explain the finding of bound pyruvate in the crystallized protein.

Original languageEnglish
Pages (from-to)2457-2461
Number of pages5
JournalAmino Acids
Issue number11
Publication statusPublished - 1 Nov 2015


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