Article
Bivalent recognition of fatty acyl-CoA by a human integral membrane palmitoyltransferase.
Proceedings of the National Academy of Sciences of the United States of America - 15 Feb 2022
Lee Chul-Jin, Stix Robyn, Rana Mitra S, Shikwana Flowreen, Murphy R Elliot, Ghirlando Rodolfo, Faraldo-Gómez José D, Banerjee Anirban
Abstract excerpt
S-acylation, also known as palmitoylation, is the most abundant form of protein lipidation in humans. This reversible posttranslational modification, which targets thousands of proteins, is catalyzed by 23 members of the DHHC family of integral membrane enzymes. DHHC enzymes use fatty acyl-CoA as the ubiquitous fatty acyl donor and become autoacylated at a catalytic cysteine; this intermediate subsequently...
Topics
- Acyl Coenzyme A
- Acyltransferases
- Catalytic Domain
- Cell Membrane
- Gene Expression Regulation, Enzymologic
- Humans
- Lipoylation
- Models, Molecular
- Molecular Dynamics Simulation
- Mutation
- Protein Binding
- Protein Conformation