EC Number   |
General Information |
Reference |
|---|
   1.2.1.104 | malfunction |
deletion of the E1a or E3 subunit genes of Plasmodium yoelii PDH causes no defect in blood stage development, mosquito stage development or early liver stage development. However, the gene deletions completely block the ability of the e1alpha- and e3-deficient parasites to form exo-erythrocytic merozoites during late liver stage development, thus preventing the initiation of a blood stage infection |
713056 |
| 1.2.1.104 | physiological function |
a hybrid complex consisting of E1p (thiamine diphosphate-dependent pyruvate dehydrogenase, AceE), E2 (dihydrolipoamide acetyltransferase, AceF), E3 (dihydrolipoamide dehydrogenase, Lpd), and E1o (thiamine diphosphate-dependent 2-oxoglutarate dehydrogenase, OdhA) contains six copies of E2 in its core. E2 forms a stable complex with E3 (E2-E3 subcomplex) in vitro, hypothetically comprised of two E2 trimers and four E3 dimers. E1o exists mainly as a hexamer in solution and is ready to form an active ODH complex when mixed with the E2-E3 subcomplex. In vitro, there is E1p- and E1o-dependent inhibition of ODH and PDH, respectively, actively supporting the formation of the hybrid complex, in which both E1p and E1o associate with a single E2-E3 |
-, 759743 |
| 1.2.1.104 | physiological function |
addition of excess pure E3 from Enterococcus faecalis may substitute for loss of Lactococcus lactis E3 during purification |
759422 |
| 1.2.1.104 | physiological function |
all the substrates, pyruvate, CoA and NAD+, exhibit cooperative klnetics towards the native enzyme complex. the calculated Hill coefficient for pyruvate is 1.34 |
758851 |
| 1.2.1.104 | physiological function |
complete cross-reactivity is found with antibodies directed against the pyruvate dehydrogenase complex from Escherichia coli and electron micrographs of both enzyme complexes reveal identical structures |
758852 |
| 1.2.1.104 | physiological function |
dihydrolipoyl transacetylase subunit consists of 24 apparently identical polypeptide chains organized into a cube-like structure, and has the potential to bind 24 pyruvate dehydrogenase dimers in the absence of flavoprotein and 24 flavoprotein dimers in the absence of the pyruvate dehydrogenase subunit. The transacetylase can accommodate a total of only about 12 pyruvate dehydrogenase dimers and six flavoprotein dimers and this stoichiometry, which is the same as that of the native pyruvate dehydrogenase complex, produces maximum activity. Steric hindrance between the relatively bulky pyruvate dehydrogenase and flavoprotein molecules prevents the transacetylase from binding 24 molecules of each ligand |
760075 |
| 1.2.1.104 | physiological function |
disintegration of the pyruvate dehydrogenase complex core via double truncations (eight residues from E2 and seven residues from E3 binding protein PdhX) leads to the formation of highly active (approximately 70% of wild-type) unordered clusters or agglomerates and inactive nonagglomerated species (hexamer/trimer). After additional deletion of N-terminal swinging arms, the C-terminal truncations also cause the formation of agglomerates of minimized E2/E3 binding protein complexes |
758755 |
| 1.2.1.104 | physiological function |
during lactate consumption, component E1 subunit alpha Ser293 and Ser300 phosphorylation levels are 33% higher compared to the phase of glucose excess. At the same time, the relative phosphorylation level of Ser232 increases steadily throughout the cultivation (66% increase overall). The intracellular pyruvate accumulates only during the period of high lactate production, while acetyl-CoA shows nearly no accumulation |
762973 |
| 1.2.1.104 | physiological function |
high salt intake downregulates sirtuin SIRT3 level in brown adipose tissue, accompanied by decreased oxygen consumption rate, and causes a severe loss of brown adipose tissue characteristics. SIRT3 interacts with pyruvate dehydrogenase E1alpha (PDHA1) and deacetylates residue Lys83 both in vitro and in vivo under high salt intake. In parallel, high salt intake suppresses salt-induced kinase (Sik) 2 phosphorylation. Silencing Sik2 further diminishes SIRT3 activity and enhances acetylation of PDHA1 K83. Reconstruction of SIRT3 restores PDH activity and thermogenic markers expression in differentiated brown adipocytes from SIRT3 knockout mice |
762889 |
| 1.2.1.104 | physiological function |
in Corynebacterium glutamicum, the PDH-ODH hybrid complex consists of six copies of subunit E2 in its core. E2 forms a stable complex with E3 (E2-E3 subcomplex) in vitro, hypothetically comprised of two E2 trimers and four E3 dimers. E1o exists mainly as a hexamer in solution and is ready to form an active ODH complex when mixed with the E2-E3 subcomplex. Inhibition of ODH and PDH is E1p- and E1o-dependent, respectively, actively supporting the formation Iof the hybrid complex, in which both E1p and E1o associate with a single E2-E3 |
-, 759743 |
