Cargando…
Membrane Association Allosterically Regulates Phospholipase A(2) Enzymes and Their Specificity
[Image: see text] Water-soluble proteins as well as membrane-bound proteins associate with membrane surfaces and bind specific lipid molecules in specific sites on the protein. Membrane surfaces include the traditional bilayer membranes of cells and subcellular organelles formed by phospholipids. Mo...
Autores principales: | Mouchlis, Varnavas D., Dennis, Edward A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9730854/ https://www.ncbi.nlm.nih.gov/pubmed/36315840 http://dx.doi.org/10.1021/acs.accounts.2c00497 |
Ejemplares similares
-
Lipoprotein-associated phospholipase A(2): A paradigm for allosteric regulation by membranes
por: Mouchlis, Varnavas D., et al.
Publicado: (2022) -
Substrate-Specific
Inhibition Constants for Phospholipase
A(2) Acting on Unique Phospholipid Substrates in Mixed Micelles
and Membranes Using Lipidomics
por: Mouchlis, Varnavas D., et al.
Publicado: (2019) -
Allosteric regulation by membranes and hydrophobic subsites in phospholipase A(2) enzymes determine their substrate specificity
por: Dennis, Edward A.
Publicado: (2022) -
Membrane
Allostery and Unique Hydrophobic Sites Promote
Enzyme Substrate Specificity
por: Mouchlis, Varnavas D., et al.
Publicado: (2018) -
Omega-3 versus Omega-6 fatty acid availability is controlled by hydrophobic site geometries of phospholipase A(2)s
por: Hayashi, Daiki, et al.
Publicado: (2021)