Member database | NCBIfam (includes TIGRFAMs) |
NCBIfam type | family |
Short name | PS_decarb |
Description
Catalyzes the decarboxylaton of phospatidyl-L-serine to phosphatidylethanolamine. The related family TIGR00164 includes archaetidylserine decarboxylases from various archaea. Phosphatidylserine decarboxylase is synthesized as a single chain precursor. Generation of the pyruvoyl active site from a Ser is coupled to cleavage of a Gly-Ser bond between the larger (beta) and smaller (alpha chains). It is an integral membrane protein.
References
1. A study of archaeal enzymes involved in polar lipid synthesis linking amino acid sequence information, genomic contexts and lipid composition. Daiyasu H, Kuma K, Yokoi T, Morii H, Koga Y, Toh H. Archaea 1, 399-410, (2005). View articlePMID: 16243780
2. Phosphatidylserine decarboxylase. Voelker DR. Biochim. Biophys. Acta 1348, 236-44, (1997). View articlePMID: 9370338
Integrated to
External Links
Representative structure
7cnw: Crystal structure of Apo PSD from E. coli (1.90 A)