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Updated: Apr 7, 2026

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
Published on: December 12, 2013
Ketimine reductase/CRYM catalyzes reductive alkylamination of α-keto acids, confirming its function as an imine
André Hallen1, Arthur J L Cooper2, Jason R Smith3
1Department of Chemistry and Biomolecular Sciences, Macquarie University, Balaclava Road, North Ryde, NSW, 2109, Australia. andre.hallen@students.mq.edu.au.
Abstract:
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.
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