Recombinant Human NMT1 Protein, N-His

Description of Recombinant Human NMT1 Protein, N-His

Introduction

Recombinant Human NMT1 Protein, also known as N-myristoyltransferase 1, is a key enzyme involved in the post-translational modification of proteins. This protein is encoded by the NMT1 gene and plays a crucial role in a variety of cellular processes, making it a valuable tool in scientific research and potential therapeutic applications.

Structure of Recombinant Human NMT1 Protein

The Recombinant Human NMT1 Protein is a 52 kDa protein consisting of 471 amino acids. It is composed of two domains – an N-terminal catalytic domain and a C-terminal myristoyl-binding domain. The catalytic domain is responsible for the transfer of myristic acid to the N-terminal glycine of target proteins, while the myristoyl-binding domain helps in the recognition and binding of target proteins.

The crystal structure of Recombinant Human NMT1 Protein has been determined, revealing its unique three-dimensional structure. This structure provides insights into the mechanism of action of this enzyme and aids in the design and development of inhibitors and modulators.

Activity of Recombinant Human NMT1 Protein

The primary function of Recombinant Human NMT1 Protein is to catalyze the transfer of myristic acid from myristoyl-CoA to the N-terminal glycine residue of target proteins. This modification, known as N-myristoylation, is essential for the proper functioning and localization of many proteins involved in signal transduction, membrane targeting, and protein-protein interactions.

Recombinant Human NMT1 Protein has been found to have a broad substrate specificity, with the ability to myristoylate a wide range of proteins. This includes viral proteins, such as HIV-1 Gag and Rous sarcoma virus Gag, as well as cellular proteins, such as the α subunit of G proteins and Src family kinases.

In addition to its role in protein myristoylation, Recombinant Human NMT1 Protein has been shown to have other activities as well. It has been found to have protein kinase activity, phosphorylating certain substrates in vitro. It has also been reported to have RNA binding activity, suggesting a potential role in RNA metabolism.

Applications of Recombinant Human NMT1 Protein

The unique structure and activity of Recombinant Human NMT1 Protein make it a valuable tool in scientific research and potential therapeutic applications. Some of its applications include:

1. Understanding the role of N-myristoylation in cellular processes

Recombinant Human NMT1 Protein has been used to study the importance of N-myristoylation in various cellular processes, such as signal transduction, membrane targeting, and protein-protein interactions. Its ability to myristoylate a wide range of proteins makes it a useful tool in understanding the role of this modification in different biological pathways.

2. Development of inhibitors and modulators

The crystal structure of Recombinant Human NMT1 Protein has aided in the design and development of inhibitors and modulators of this enzyme. These molecules can be used to study the function of NMT1 and its role in diseases, as well as potential therapeutic targets for conditions such as cancer and viral infections.

3. Production of myristoylated proteins for research and therapeutic purposes

Recombinant Human NMT1 Protein can be used to produce myristoylated proteins in vitro. These proteins can then be used for various research purposes, such as structural studies, or as potential therapeutics for diseases where N-myristoylation plays a crucial role.

4. Diagnosis and treatment of NMT1-related diseases

Mutations in the NMT1 gene have been linked to various diseases, such as cancer and neurodegenerative disorders.