MBOAT7
Lysophospholipid acyltransferase 7 also known as membrane-bound O-acyltransferase domain-containing protein 7 (MBOAT7) is an enzyme that in humans is encoded by the MBOAT7 gene.[1] It is homologous to other membrane-bound O-acyltransferases.
Function
Function
This gene encodes a member of the membrane-bound O-acyltransferases family of integral membrane proteins that have acyltransferase activity. The encoded protein is a lysophosphatidylinositol acyltransferase that has specificity for arachidonoyl-CoA as an acyl donor. This protein is involved in the re-acylation of phospholipids as part of the phospholipid remodeling pathway known as the Land cycle.[1]
Further reading
Further reading
- Wende H, Volz A, Ziegler A (July 2000). “Extensive gene duplications and a large inversion characterize the human leukocyte receptor cluster”. Immunogenetics. 51 (8–9): 703–13. doi:10.1007/s002510000187. PMID 10941842.
- Lee HC, Inoue T, Imae R, Kono N, Shirae S, Matsuda S, Gengyo-Ando K, Mitani S, Arai H (March 2008). “Caenorhabditis elegans mboa-7, a member of the MBOAT family, is required for selective incorporation of polyunsaturated fatty acids into phosphatidylinositol”. Mol. Biol. Cell. 19 (3): 1174–84. doi:10.1091/mbc.E07-09-0893. PMC 2262980. PMID 18094042.
- Shindou H, Hishikawa D, Harayama T, Yuki K, Shimizu T (April 2009). “Recent progress on acyl CoA: lysophospholipid acyltransferase research”. J. Lipid Res. 50 Suppl: S46–51. doi:10.1194/jlr.R800035-JLR200. PMC 2674719. PMID 18931347.
- Gijón MA, Riekhof WR, Zarini S, Murphy RC, Voelker DR (October 2008). “Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils”. J. Biol. Chem. 283 (44): 30235–45. doi:10.1074/jbc.M806194200. PMC 2573059. PMID 18772128.
- Fukunaga-Johnson N, Lee SW, Liebert M, Grossman HB (1996). “Molecular analysis of a gene, BB1, overexpressed in bladder and breast carcinoma”. Anticancer Res. 16 (3A): 1085–90. PMID 8702217.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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