CKMT1A is encoded by the CKMT1A gene, which is located on chromosome 15. The gene produces a protein that exists in two isoenzymes: sarcomeric mitochondrial creatine kinase (sMtCK) and ubiquitous mitochondrial creatine kinase (uMtCK). These isoenzymes are encoded by separate genes but share a high degree of homology .
The primary function of CKMT1A is to facilitate the transfer of high-energy phosphate from mitochondria to the cytosolic carrier, creatine. This process is essential for maintaining cellular energy homeostasis, especially in tissues with high and fluctuating energy demands, such as muscles and the brain .
CKMT1A operates in two different oligomeric forms: dimers and octamers. This structural versatility allows it to efficiently manage energy transfer under varying cellular conditions. The enzyme’s activity is crucial for the rapid regeneration of ATP, which is vital for muscle contraction and other energy-intensive cellular processes .
CKMT1A is highly expressed in tissues with high energy demands, including skeletal muscle, heart muscle, and the brain. Its role in energy metabolism makes it a critical player in various physiological processes. Additionally, overexpression of CKMT1A has been observed in several malignant cancers with poor prognosis, suggesting a potential link between CKMT1A activity and cancer cell metabolism .
Mutations or dysregulation of the CKMT1A gene can lead to metabolic disorders and have been associated with conditions such as mitochondrial complex I deficiency and reticular dysgenesis. The enzyme’s role in energy metabolism also makes it a potential target for therapeutic interventions in metabolic diseases and cancer .
Human recombinant CKMT1A is used in various research applications to study its function and regulation. Recombinant proteins are produced through genetic engineering techniques, allowing researchers to investigate the enzyme’s properties and interactions in a controlled environment. This research is essential for developing targeted therapies and understanding the enzyme’s role in health and disease .