GBA3 Human

GBA3 is encoded by the GBA3 gene located on chromosome 4. The enzyme is composed of 469 amino acids and has a molecular mass of approximately 54 kDa under reducing conditions . The recombinant form of this enzyme is often produced using baculovirus expression systems in insect cells, such as Spodoptera frugiperda (Sf21) .

The primary function of GBA3 is to hydrolyze beta-D-glucosides and beta-D-galactosides. This activity is measured by its ability to hydrolyze synthetic substrates like 4-methylumbelliferyl-beta-D-glucopyranoside . The specific activity of recombinant GBA3 is greater than 1,500 pmol/min/μg under the described conditions .

GBA3 is primarily found in the liver, where it is believed to play a role in the detoxification of plant glycosides . Unlike other beta-glucosidases, such as GBA1 and GBA2, which are involved in the metabolism of glucosylceramide and bile acid 3-O-glucosides respectively, GBA3 does not hydrolyze any known physiological beta-glycosides . This unique substrate specificity suggests a specialized role in the detoxification process.

Recombinant GBA3 is used extensively in biochemical research to study its enzymatic properties and potential applications in detoxification processes. The enzyme’s ability to hydrolyze synthetic substrates makes it a valuable tool for studying the mechanisms of glycoside hydrolysis and the detoxification of plant-derived compounds .

In addition, understanding the structure and function of GBA3 can provide insights into the development of therapeutic strategies for diseases related to glycoside metabolism. For example, inhibitors of GBA3 could potentially be used to modulate the detoxification process and improve drug delivery .