IPR033177
Phosphatidylserine decarboxylase, bacterial/eukaryotic
InterPro entry
Short name | PSD-B |
family relationships |
Description
This entry represents Phosphatidylserine decarboxylase proenzyme and similar sequences mainly found in eukaryotes and bacteria. Phosphatidylserine decarboxylase (PSD,
4.1.1.65) is synthesised 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). This enzyme catalyses the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). It is an integral membrane protein.
Phosphatidylserine decarboxylases (PSDs) have been classified in two types. Type I PSDs include enzymes of eukaryotic mitochondria and bacterial origin which contain the amino acid sequence LGST as a characteristic motif. Type II PSDs are found in the endomembrane system of eukaryotes and contain a typical GGST motif. These characteristic motifs are considered as autocatalytic cleavage sites where proenzymes are split into alpha and beta subunits
[1].
References
1.Phosphatidylserine decarboxylases, key enzymes of lipid metabolism. Schuiki I, Daum G. IUBMB Life 61, 151-62, (2009). View articlePMID: 19165886
Further reading
2. Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning and mapping of the gene, heterologous expression, and creation of the null allele. Trotter PJ, Pedretti J, Yates R, Voelker DR. J. Biol. Chem. 270, 6071-80, (1995). View articlePMID: 7890740
3. Phosphatidylserine decarboxylase from Saccharomyces cerevisiae. Isolation of mutants, cloning of the gene, and creation of a null allele. Trotter PJ, Pedretti J, Voelker DR. J. Biol. Chem. 268, 21416-24, (1993). View articlePMID: 8407984
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Genome Properties
Contributing Member Database Entry
- NCBIfam:TIGR00163
Representative structure
7cnw: Crystal structure of Apo PSD from E. coli (1.90 A)