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CDP-DAG synthesis by peripheral membrane-bound Tam41-type enzymes.
- Source :
-
Journal of Biochemistry . Sep2024, Vol. 176 Issue 3, p175-177. 3p. - Publication Year :
- 2024
-
Abstract
- Cytidine diphosphate diacylglycerol (CDP-DAG) is a critical intermediate that is converted to multiple phospholipids in prokaryotes and eukaryotes. In budding yeast, CDP-DAG synthesis from cytidine triphosphate (CTP) and phosphatidic acid (PA) is catalyzed by the membrane-integrated protein Cds1 in the endoplasmic reticulum and the peripheral membrane-bound protein Tam41 in mitochondria. Although a recent study revealed that the fission yeast SpTam41 consists of a nucleotidyltransferase domain and a winged helix domain, forming an active-site pocket for CTP binding between the two domains together with a C-terminal amphipathic helix for membrane association, how CTP and Mg 2+, a most-favoured divalent cation, are accommodated with PA remains obscure. A more recent report by Kimura et al. (J. Biochem. 2022; 171:429–441) solved the crystal structure of FbTam41, a functional ortholog from a Firmicutes bacterium, with CTP-Mg 2+, successfully providing a detailed molecular view of CDP-DAG synthesis. In this commentary, our current understanding of Tam41-mediated reaction is discussed. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 0021924X
- Volume :
- 176
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 179399880
- Full Text :
- https://doi.org/10.1093/jb/mvae046