Mitochondrial Trifunctional Protein
A mitochondrial protein consisting of four alpha-subunits and four beta-subunits. It contains enoyl-CoA hydratase, long-chain-3-hydroxyacyl-CoA dehydrogenase, and acetyl-CoA C-acyltransferase activities and plays an important role in the metabolism of long chain FATTY ACIDS.
Mitochondrial Trifunctional Protein, alpha Subunit
The alpha subunit of mitochondrial trifunctional protein. It contains both enoyl-CoA hydratase activity (EC 4.2.1.17) and long-chain-3-hydroxyacyl-CoA dehydrogenase activity (EC 1.1.1.211). There are four of these alpha subunits in each mitochondrial trifunctional protein molecule.
Mitochondrial Trifunctional Protein, beta Subunit
The beta subunit of mitochondrial trifunctional protein that contains acetyl-CoA C-acyltransferase activity. There are four of these beta subunits in each trifunctional protein complex.
Long-Chain-3-Hydroxyacyl-CoA Dehydrogenase
3-Hydroxyacyl CoA Dehydrogenases
Multienzyme Complexes
GTP-Binding Protein beta Subunits
Heterotrimeric GTP-binding protein subunits that tightly associate with GTP-BINDING PROTEIN GAMMA SUBUNITS. A dimer of beta and gamma subunits is formed when the GTP-BINDING PROTEIN ALPHA SUBUNIT dissociates from the GTP-binding protein heterotrimeric complex. The beta-gamma dimer can play an important role in signal transduction by interacting with a variety of second messengers.
Enoyl-CoA Hydratase
Acetyl-CoA C-Acyltransferase
Phospholipase C beta
Lipid Metabolism, Inborn Errors
Heterotrimeric GTP-Binding Proteins
GTP-BINDING PROTEINS that contain three non-identical subunits. They are found associated with members of the seven transmembrane domain superfamily of G-PROTEIN-COUPLED RECEPTORS. Upon activation the GTP-BINDING PROTEIN ALPHA SUBUNIT of the complex dissociates leaving a dimer of a GTP-BINDING PROTEIN BETA SUBUNIT bound to a GTP-BINDING PROTEIN GAMMA SUBUNIT.
Formate-Tetrahydrofolate Ligase
RGS Proteins
A large family of evolutionarily conserved proteins that function as negative regulators of HETEROTRIMERIC GTP-BINDING PROTEINS. RGS PROTEINS act by increasing the GTPase activity of the G alpha subunit of a heterotrimeric GTP-binding protein, causing it to revert to its inactive (GDP-bound) form.