Treatment of the dihydrolipoyl transacetylase-protein X-kinase subcomplex (E2-X-KcKb) with protease Arg C selectively converted protein X into an inner domain fragment (Mr approximately equal to 35,000) and an outer (lipoyl-bearing) domain fragment (Mr approximately equal to 15,500).
Mohammed Rahmatullah+3 more
openalex +4 more sources
Studies were conducted on four pyruvate dehydrogenase kinase-containing fractions: purified pyruvate dehydrogenase complex, the dihydrolipoyl transacetylase-protein X-kinase subcomplex (E2.X.K), a kinase fraction (K fraction) prepared from the E2.X.K subcomplex, and a kinase fraction generated by limited trypsin-digestion of E2.X.K.
Mohammed Rahmatullah+3 more
openalex +4 more sources
Structure/function relationships in the pyruvate dehydrogenase complex form Azotobacter vinelandii [PDF]
The role of the hinge region between the binding domain and the catalytic domain in dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii was addressed by deletion mutagenesis. Mutated dihydrolipoyl transacetylase proteins were constructed with a deletion of 11 amino acids in the hinge region between the binding domain and the N‐terminal part ...
Schulze, E.+3 more
openaire +5 more sources
Mitochondrial transport and metabolism of the vitamin B‐derived cofactors thiamine pyrophosphate, coenzyme A, FAD and NAD+, and related diseases: A review [PDF]
Abstract Multiple mitochondrial matrix enzymes playing key roles in metabolism require cofactors for their action. Due to the high impermeability of the mitochondrial inner membrane, these cofactors need to be synthesized within the mitochondria or be imported, themselves or one of their precursors, into the organelles.
Ferdinando Palmieri+3 more
wiley +3 more sources
A cuproptosis-related gene expression signature predicting clinical prognosis and immune responses in intrahepatic cholangiocarcinoma detected by single-cell RNA sequence analysis [PDF]
Background Cholangiocarcinoma represents a malignant neoplasm originating from the hepatobiliary tree, with a subset of tumors developing inside the liver.
Hefei Ren+9 more
doaj +2 more sources
Subunit Associations in the Mammalian Pyruvate Dehydrogenase Complex
We have further distinguished the structures and roles of the two lipoyl-bearing components of the pyruvate dehydrogenase complex, the dihydrolipoyl transacetylase (E2) component and the component designated as protein X. The amino acid sequences of the NH2-terminal regions of the lipoyl-bearing domain of the E2 component and protein X are different ...
Gary A. Radke+5 more
openaire +4 more sources
Protein thiol modifications visualized in vivo. [PDF]
Thiol-disulfide interconversions play a crucial role in the chemistry of biological systems. They participate in the major systems that control the cellular redox potential and prevent oxidative damage.
Lars I Leichert, Ursula Jakob
doaj +1 more source
Identification of PDHX as a metabolic target for esophageal squamous cell carcinoma
Inoue et al. found that pyruvate dehydrogenase (PDH) component X expression is necessary for PDH activity and is involved in the cancer stemness of esophageal squamous cell carcinoma (ESCC) cells, thereby being metabolically essential for the tumor growth of ESCC.
Jun Inoue+5 more
wiley +1 more source
PDHX acetylation facilitates tumor progression by disrupting PDC assembly and activating lactylation-mediated gene expression. [PDF]
Deactivation of the mitochondrial pyruvate dehydrogenase complex (PDC) is important for the metabolic switching of cancer cell from oxidative phosphorylation to aerobic glycolysis.
Jiang Z+12 more
europepmc +2 more sources
This study shows the unique molecular architecture of the PDH‐ODH hybrid complex in Corynebacterium glutamicum, in which both CgE1p and CgE1o associate with the CgE2‐E3 subcomplex. The core‐forming CgE2‐E3 probably consists of six copies of CgE2, which is relatively compact compared with PDH and ODH in other microorganisms that have 24 copies of E2 ...
Hirokazu Kinugawa+5 more
wiley +1 more source