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

Abstract

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 Ca2+ had stimulatory effects on NMT2 activity while Mn2+ and Zn2+ 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.

In silico analysis on catalase protein from Nicotiana tabaccum L.

“…N-myristoylation is a modification in which the covalent attachment of a 14-carbon saturated fatty acid called myristate to the N-terminal glycine residue of proteins. Myristoylation has an effect on the conformational stability of proteins and their interaction with membranes or the hydrophobic domains of other proteins [31]. Casein kinase 2 (CK2) is an active kinase which is expressed constitutively, has key roles in a broad range of cellular events such as transcription and translation, ribosome biogenesis, cell cycle progression, and apoptosis [32].…”