AK1 Human

AK1 is a small enzyme with a molecular weight of approximately 23.7 kDa. It consists of three functional domains:

1. CORE Domain: The catalytic and oligomerization regulatory enzyme domain.
2. LID Domain: The ligand interaction domain.
3. Substrate Binding Site: The site where the substrate binds and the reaction occurs .

The enzyme is predominantly found in the cytosol of skeletal muscle, brain, and erythrocytes. It plays a vital role in regulating the adenine nucleotide composition within these cells .

The gene encoding AK1 is located on human chromosome 9 at the position 9q34.11. There are nine distinct isoenzymes of adenylate kinase in human tissues, named AK1 to AK9. Each isoenzyme has a specific role and localization within the cell .

Human recombinant AK1 is typically expressed in Escherichia coli and purified using conventional chromatography techniques. The recombinant protein is often fused to a His-tag at the N-terminus to facilitate purification .

AK1 is involved in various physiological processes and its dysregulation can lead to several medical conditions. For instance, defects in the AK1 gene are associated with a form of hemolytic anemia. Additionally, low levels of AK1 can cause an imbalance in adenine nucleotide pools, which may contribute to other metabolic disorders .

In the context of neurodegenerative diseases, AK1 is upregulated in the brains of Alzheimer’s disease patients and downregulated in Duchenne muscular dystrophy. It is responsible for abnormal phosphorylation of tau via the AMPK-GSK3β pathway, leading to tau-mediated neurodegeneration .

Due to its critical role in cellular energy metabolism, AK1 is a target for research in various fields, including cancer, neurodegenerative diseases, and metabolic disorders. Understanding the structure and function of AK1 can aid in the development of new therapeutic strategies for these conditions .

In summary, Adenylate Kinase 1 is a vital enzyme with significant roles in cellular energy homeostasis and various physiological processes. Its recombinant form, expressed in E. coli, provides a valuable tool for research and potential therapeutic applications.