Ketimine Reductase/CRYM Catalyzes Reductive Alkylamination of Alpha-Keto Acids, Confirming Its Function as an Imine Reductase

Authors

André Hallen
Arthur J L Cooper, New York Medical CollegeFollow
Jason R. Smith
Joanne F. Jamie
Peter Karuso

First Page

2457

Last Page

2461

Document Type

Article

Publication Date

11-1-2015

Department

Biochemistry and Molecular Biology

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.

Recommended Citation

Hallen, A., Cooper, A. J., Smith, J. R., Jamie, J. F., & Karuso, P. (2015). Ketimine reductase/CRYM catalyzes reductive alkylamination of alpha-keto acids, confirming its function as an imine reductase. Amino Acids, 47(11), 2457-2461. doi:10.1007/s00726-015-2044-8

Publisher's Statement

Originally published in Amino Acids. https://doi.org/10.1007/s00726-015-2044-8