AK3L1 Human

AK3L1 is unique among adenylate kinases due to its lack of enzymatic activity, despite sharing high sequence homology with other members of the family . It retains the capability of binding nucleotides, which suggests it may have a regulatory role within the cell. The enzyme is composed of 460 amino acids and has a calculated molecular mass of approximately 53 kDa .

The expression of AK3L1 is tissue-specific and developmentally regulated. It is predominantly found in the mitochondrial matrix, where it is involved in regulating the adenine and guanine nucleotide compositions within the cell .

Recombinant human AK3L1 is produced using baculovirus-insect cell expression systems. The recombinant protein is often tagged with polyhistidine and GST (Glutathione S-transferase) to facilitate purification and detection . The recombinant AK3L1 protein is used in various research applications to study its structure, function, and potential role in cellular metabolism and disease.

Although AK3L1 itself lacks enzymatic activity, its role in nucleotide binding and regulation suggests it may be involved in various cellular processes. Dysregulation or mutation of adenylate kinases, in general, has been linked to several medical conditions, including metabolic syndrome, neurodegenerative diseases, and primary male infertility . Further research is needed to fully understand the physiological functions and potential clinical implications of AK3L1.