Abstract
Glycerophosphodiester phosphodiesterase (GDPD/GDE) catalyzes the hydrolysis of glycerophosphodiesters to glycerol 3-phosphate and alcohol. It was discovered that the glycerophosphodiesterase family plays a role in lipid metabolism and signal pathway in recent years, but little has been known about the characteristics of chicken GDEs. Here, chicken GDE5 (cGDE5) was identified and characterized for the first time. The full length coding cDNA sequence of cGDE5 was cloned, which encoded a polypeptide with 678 amino acids containing a carbohydrate-binding module 20 (CBM20) and a GDPD domain. Tissue expression profiles showed that cGDE5 mRNA was high in various tissues. such as heart, brain, skeletal muscle and testis. Moreover, cGDE5 was demonstrated to exhibit glycerophosphocholine phosphodiesterase activity. These results together suggested that cGDE5, as a unique member of GDE family, may play multiple roles as a cytoplasmic glycerophosphocholine phosphodiesterase.