The Enzyme Database

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EC 3.1.4.62     
Accepted name: phosphatidylethanolamine phospholipase C
Reaction: a phosphatidylethanolamine + H2O = a 1,2-diacyl-sn-glycerol + O-phosphoethanolamine
Other name(s): phosphatidylethanolamine-specific phospholipase C; PE-PLC; SMSr; SAMD8 (gene name); SMS1 (gene name)
Systematic name: phosphatidylethanolamine ethanolaminephosphohydrolase
Comments: This activity, which is similar to that of EC 3.1.4.3, phospholipase C, has been characterized from mammalian cells [1-4]. Multiple enzymes have been shown to catalyse this activity, including human sphingomyelin synthase-related protein (SMSr, gene name; SAMD8) [6-8] and sphingomyelin synthase 1 (SMS1, gene name; SGMS1) [9] (cf. EC 2.7.8.27, sphingomyelin synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hafez, M.M. and Costlow, M.E. Phosphatidylethanolamine turnover is an early event in the response of NB2 lymphoma cells to prolactin. Exp. Cell Res. 184 (1989) 37–43. [DOI] [PMID: 2507337]
2.  Kiss, Z. and Anderson, W.B. ATP stimulates the hydrolysis of phosphatidylethanolamine in NIH 3T3 cells. Potentiating effects of guanosine triphosphates and sphingosine. J. Biol. Chem. 265 (1990) 7345–7350. [PMID: 2185245]
3.  Kiss, Z., Crilly, K. and Chattopadhyay, J. Ethanol potentiates the stimulatory effects of phorbol ester, sphingosine and 4-hydroxynonenal on the hydrolysis of phosphatidylethanolamine in NIH 3T3 cells. Eur. J. Biochem. 197 (1991) 785–790. [DOI] [PMID: 2029907]
4.  Kiss, Z. The long-term combined stimulatory effects of ethanol and phorbol ester on phosphatidylethanolamine hydrolysis are mediated by a phospholipase C and prevented by overexpressed α-protein kinase C in fibroblasts. Eur. J. Biochem. 209 (1992) 467–473. [DOI] [PMID: 1327780]
5.  Kiss, Z. and Tomono, M. Compound D609 inhibits phorbol ester-stimulated phospholipase D activity and phospholipase C-mediated phosphatidylethanolamine hydrolysis. Biochim. Biophys Acta 1259 (1995) 105–108. [DOI] [PMID: 7492608]
6.  Murakami, C. and Sakane, F. Sphingomyelin synthase-related protein generates diacylglycerol via the hydrolysis of glycerophospholipids in the absence of ceramide. J. Biol. Chem. 296:100454 (2021). [DOI] [PMID: 33621517]
7.  Chiang, Y.P., Li, Z., Chen, Y., Cao, Y. and Jiang, X.C. Sphingomyelin synthase related protein is a mammalian phosphatidylethanolamine phospholipase C. Biochim Biophys Acta Mol Cell Biol Lipids 1866:159017 (2021). [DOI] [PMID: 34332077]
8.  Hu, K., Zhang, Q., Chen, Y., Yang, J., Xia, Y., Rao, B., Li, S., Shen, Y., Cao, M., Lu, H., Qin, A., Jiang, X.C., Yao, D., Zhao, J., Zhou, L. and Cao, Y. Cryo-EM structure of human sphingomyelin synthase and its mechanistic implications for sphingomyelin synthesis. Nat. Struct. Mol. Biol. (2024) . [DOI] [PMID: 38388831]
9.  Suzuki, R., Murakami, C., Dilimulati, K., Atsuta-Tsunoda, K., Kawai, T. and Sakane, F. Human sphingomyelin synthase 1 generates diacylglycerol in the presence and absence of ceramide via multiple enzymatic activities. FEBS Lett. 597 (2023) 2672–2686. [DOI] [PMID: 37715942]
[EC 3.1.4.62 created 2024]
 
 


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