The CRYZL1 gene is located on chromosome 13 in humans . The gene undergoes alternative splicing, resulting in multiple transcript variants, although the full-length nature of these variants has not been completely determined . The protein encoded by this gene is involved in various cellular processes, including the reduction of quinones to hydroquinones, which helps in detoxifying reactive quinones and preventing oxidative stress .
Quinone oxidoreductase-like protein 1 functions as a two-electron reductase, catalyzing the reduction of quinones to hydroquinones . This reaction is essential for detoxifying quinones, which can generate reactive oxygen species (ROS) through redox cycling mechanisms . By reducing quinones to hydroquinones, CRYZL1 helps in preventing the formation of semiquinone free radicals and other harmful oxidative species .
The physiological role of CRYZL1 extends beyond its enzymatic activity. It is involved in maintaining cellular redox balance and protecting cells from oxidative damage . The enzyme’s activity is crucial in tissues exposed to high levels of oxidative stress, such as the liver and lungs . Additionally, CRYZL1 plays a role in the metabolism of vitamin K, which is essential for blood clotting and bone health .
Mutations or alterations in the CRYZL1 gene can have significant clinical implications. For instance, certain polymorphic forms of the protein may be associated with an increased risk of developing various diseases, including cancer . The enzyme’s role in detoxifying reactive quinones and maintaining cellular redox balance makes it a potential target for therapeutic interventions in diseases characterized by oxidative stress and redox imbalance .
The human recombinant form of Quinone Oxidoreductase-like Protein 1 is produced using recombinant DNA technology. This involves inserting the CRYZL1 gene into an expression vector, which is then introduced into a host cell (such as E. coli or yeast) to produce the protein . The recombinant protein is purified and used in various research applications, including studies on enzyme function, drug development, and disease mechanisms .