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The molecular mechanism of DHHC protein acyltransferases.
- Source :
-
Biochemical Society Transactions . 2/28/2019, Vol. 47 Issue 1, p157-167. 11p. - Publication Year :
- 2019
-
Abstract
- Protein S-acylation is a reversible lipidic posttranslational modification where a fatty acid chain is covalently linked to cysteine residues by a thioester linkage. A family of integral membrane enzymes known as DHHC protein acyltransferases (DHHC-PATs) catalyze this reaction. With the rapid development of the techniques used for identifying lipidated proteins, the repertoire of S-acylated proteins continues to increase. This, in turn, highlights the important roles that S-acylation plays in human physiology and disease. Recently, the first molecular structures of DHHC-PATs were determined using X-ray crystallography. This review will comment on the insights gained on the molecular mechanism of S-acylation from these structures in combination with a wealth of biochemical data generated by researchers in the field. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 03005127
- Volume :
- 47
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Biochemical Society Transactions
- Publication Type :
- Academic Journal
- Accession number :
- 135004974
- Full Text :
- https://doi.org/10.1042/BST20180429