Search results
Results from the WOW.Com Content Network
Three small proteins Tom5, Tom6, Tom7 interact closely with Tom40 to assemble and stabilize the complex. The TOM complex also consists of a dimer of Tom40 or small Tom proteins that are held together by two Tom22 subunits. [20] [21] Protein sorting into the mitochondrial compartments always starts at the TOM complex. The TOM complex forms two ...
In enzymology, the complex is described as an mitochondrial protein-transporting ATPase (EC 7.4.2.3), or more systematically ATP phosphohydrolase (mitochondrial protein-importing), as the TIM part requires ATP hydrolysis to work. Only 13 proteins necessary for a mitochondrion are actually coded in mitochondrial DNA. The vast majority of ...
The carrier preprotein is then inserted into the inner mitochondrial membrane in a potential-dependent fashion. [10] The membrane potential is necessary for both insertion of the precursor into the carrier translocase and lateral release of the protein into the lipid phase of the inner mitochondrial membrane, which completes protein translocation.
Mitochondrial matrix has a pH of about 7.8, which is higher than the pH of the intermembrane space of the mitochondria, which is around 7.0–7.4. [5] Mitochondrial DNA was discovered by Nash and Margit in 1963. One to many double stranded mainly circular DNA is present in mitochondrial matrix. Mitochondrial DNA is 1% of total DNA of a cell.
The translocase of the outer membrane (TOM) is a complex of proteins found in the outer mitochondrial membrane of the mitochondria. It allows movement of proteins through this barrier and into the intermembrane space of the mitochondrion. Most of the proteins needed for mitochondrial function are encoded by the nucleus of the cell.
The sorting and assembly machinery is required for the assembly of beta barrel proteins, this includes proteins such as the Tom40 import pore and porin.. Like all mitochondrial proteins, beta barrel proteins are transported into the intermembrane space of mitochondria via the translocase of the outer membrane.
Many MC proteins preferentially catalyze the exchange of one solute for another ().A variety of these substrate carrier proteins, which are involved in energy transfer, have been found in the inner membranes of mitochondria and other eukaryotic organelles such as the peroxisome and facilitate the transport of inorganic ions, nucleotides, amino acids, keto acids and cofactors across the membrane.
Since aspartate is an amino acid, an amino radical needs to be added to the oxaloacetate. This is supplied by glutamate, which in the process is transformed into alpha-ketoglutarate by the same enzyme. The second antiporter (AGC1 or AGC2) imports glutamate from the cytosol into the matrix and exports aspartate from the matrix to the cytosol.