EC |
4.1.1.65 |
Accepted name: |
phosphatidylserine decarboxylase |
Reaction: |
phosphatidyl-L-serine = phosphatidylethanolamine + CO2 |
Other name(s): |
PS decarboxylase; phosphatidyl-L-serine carboxy-lyase |
Systematic name: |
phosphatidyl-L-serine carboxy-lyase (phosphatidylethanolamine-forming) |
Comments: |
The enzyme contains a tightly-bound pyruvoyl cofactor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-78-8 |
References: |
1. |
Kanfer, J. and Kennedy, E.P. Metabolism and function of bacterial lipids. II. Biosynthesis of phospholipids in Escherichia coli. J. Biol. Chem. 239 (1964) 1720–1726. [PMID: 14213340] |
2. |
Satre, M. and Kennedy, E.P. Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli. J. Biol. Chem. 253 (1978) 479–483. [PMID: 338609] |
3. |
Hovius, R., Faber, B., Brigot, B., Nicolay, K. and de Kruijff, B. On the mechanism of the mitochondrial decarboxylation of phosphatidylserine. J. Biol. Chem. 267 (1992) 16790–16795. [PMID: 1512221] |
4. |
Auchi, L., Tsvetnitsky, V., Yeboah, F.A. and Gibbons, W.A. Purification of plasma membrane rat liver phosphatidylserine decarboxylase. Biochem Soc Trans. 21:488S (1993). [DOI] [PMID: 8132055] |
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[EC 4.1.1.65 created 1976] |
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