NYMC Faculty Publications
Ketimine Reductase/CRYM Catalyzes Reductive Alkylamination of α-Keto Acids, Confirming its Function as an Imine Reductase
Author Type(s)
Faculty
DOI
10.1007/s00726-015-2044-8
Journal Title
Amino Acids
First Page
2457
Last Page
2461
Document Type
Article
Publication Date
11-1-2015
Department
Biochemistry and Molecular Biology
Keywords
Animals, Catalysis, Crystallins, Humans, Mice, Multiprotein Complexes, Oxidoreductases Acting on CH-NH Group Donors, Phenylpyruvic Acids, mu-Crystallins
Disciplines
Medicine and Health Sciences
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 α-Keto Acids, Confirming its Function as an Imine Reductase. Amino Acids, 47 (11), 2457-2461. https://doi.org/10.1007/s00726-015-2044-8
