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Journal of Biomedicine and Biotechnology
Volume 2009, Article ID 907614, 9 pages
Research Article

Biochemical Characterization of Bovine Brain Myristoyl-CoA:Protein N-Myristoyltransferase Type 2

Department of Pathology and Laboratory Medicine, College of Medicine and Health Research Division, Saskatchewan Cancer Agency, University of Saskatchewan, 20 Campus Drive, Saskatoon, SK, Canada S7N 4H4

Received 6 February 2009; Revised 9 June 2009; Accepted 15 June 2009

Academic Editor: Matthew B. Wheeler

Copyright © 2009 Ponniah Selvakumar et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Protein N-myristoylation is a lipidic modification which refers to the covalent attachment of myristate, a 14-carbon saturated fatty acid, to the N-terminal glycine residue of a number of mammalian, viral, and fungal proteins. In this paper, we have cloned the gene coding for myristoyl-CoA:protein N-myristoyltransferase (NMT) from Bos tarus brain. The open reading frame codes for a 410-amino-acid protein and overexpressed in Escherichia coli. Kinetic studies suggested that bovine brain NMT2 and human NMT1 show significant differences in their peptide substrate specificities. The metal ion had stimulatory effects on NMT2 activity while and inhibited the enzyme activity. In addition, NMT2 activity was inhibited by various organic solvents and other detergents while NMT1 had a stimulatory effect. Biochemical characterization suggested that both forms of NMT have unique characteristics. Further analysis towards functional role NMT2 will lead the development of therapeutic target for the progression of various diseases such as cancer, cardiovascular diseases, and neurodegenerative diseases.