EC Number   |
General Information |
Reference |
|---|
    1.2.1.105 | malfunction |
RNAi knockdown-inducted bloodstream trypanosomes show pronounced growth reduction and often fail to equally distribute kinetoplast DNA to daughter cells, resulting in accumulation of cells devoid of kinetoplast DNA or containing two kinetoplasts |
724891 |
| 1.2.1.105 | metabolism |
hE1o can also utilize 2-oxoadipate (OA) as a substrate. Both E1o-specific and overall complex activities (NADH production) are detected using OA as a substrate. hE1o forms the thiamine diphosphate-enamine and the C2alpha-hydroxyalkyl-thiamine diphosphate with nearly identical rates for 2-oxoglutarate OG and OA, and both OG and OA can reductively acylate lipoyl domain created from dihydrolipoyl succinyltransferase (E2o). Dioxygen can oxidize the thiamine diphosphate-derived enamine from both OG and OA, leading to thiamine diphosphate-enamine radical and generation of superoxide and H2O2. The efficiency of superoxide/H2O2 production is 7-times larger from OA than from OG |
759216 |
| 1.2.1.105 | 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 |
| 1.2.1.105 | physiological function |
enzymes purified from skeletal muscle of euthermic and hibernating ground squirrels are evaluated at 5°C, 22°C, and 37 °C. The enzyme complex from hibernator muscle at all temperatures compared with euthermic controls exhibits a decreased affinity for CoA as well as reduced activation by Ca2+ ions at 5°C from both euthermic and hibernating conditions. The E1, E2 and E3 enzymes of the complex (OGDH, DLST, DLD) all show elevated phosphotyrosine content during hibernation as well as increased ADP-ribosylation and succinylation of hibernator OGDH |
762766 |
| 1.2.1.105 | physiological function |
functional and regulatory crosstalk between the 2-oxoglutarate dehydrogenase complex, and a 2-oxoadipate dehydrogenase complex from the final degradation pathway of L-lysine, L-hydroxylysine and L-tryptophan. The two complexes share the same dihydrolipoyl succinyltransferase (E2) and dihydrolipoyl dehydrogenase (E3) components but display different substrate preferences and different binding modes. Similarly to E1o, the E1a also forms the thiamine diphosphate-enamine radical from 2-oxoadipate in the oxidative half reaction. Both complexes produced superoxide/H2O2 from O2 in the reductive half reaction |
758854 |
| 1.2.1.105 | physiological function |
hybrid complexes consisting of recombinant components of OGDHc and pyruvate dehydrogenase enzymes suggest that a different component is the gatekeeper for specificity for the two multienzyme complexes in bacteria, the E1 component for pyruvate, but the E2 component for 2-oxoglutarate |
758781 |
| 1.2.1.105 | physiological function |
mitochondrial hydrolase ABHD11 signals changes in mitochondrial 2-oxoglutarate metabolism. ABHD11 loss or inhibition drives a rapid increase in 2-oxoglutarate levels by impairing lipoylation of the 2-oxoglutarate dehydrogenase complex. ABHD11 associates with the OGDHc and maintains catalytic activity of lipoyl domain by preventing the formation of lipoyl adducts |
759827 |
| 1.2.1.105 | physiological function |
mutant plants lacking component E1 isoform OGDH1 or OGDH2 exhibit substantial reduction in both respiration and CO2 assimilation rates. Mutant lines exhibit reduced levels of chlorophylls and nitrate, increased levels of sucrose, malate and fumarate and minor changes in total protein and starch levels in leaves. After 4 weeks of growth, a clear decrease in the shoot growth of the OGDH1 mutant lines is observed, while OGDH2 mutant lines exhibit increased growth in comparison to wild type plants. The leaf number is unaltered in OGDH1 mutant lines and increased in OGDH2 mutant lines. Repression of the OGDH1 gene leads to a significative reduction of silique length and the number of seeds per silique. Lack of expression of the OEGDH2 gene does not affect the silique length, but decreases the number of seeds per silique. Isoform OGDH1 is essential to the final 2-OGDH activity in leaves while isoform OGDH2 is not |
759969 |
| 1.2.1.105 | physiological function |
organisms possessing OGDHC respond to succinyl phosphonate inhibition by significantly changing their amino acid pools. Increases in Glu, 4-aminobutanoate and alanine represent the most universal change, and strong perturbation in the relative abundance of amino acids due to the OGDHC inhibition is accompanied by decreased protein content |
758628 |
| 1.2.1.105 | physiological function |
protein-protein interactions in the dehydrogenase complex. Fluorescence studies suggest a strong interaction for the E1-E2 subcomplex, but a much weaker interaction in the E1-E3 subcomplex, and fail to identify any interaction in the E2-E3 subcomplex. Hydrogen-deuterium exchange MS studies show interactions in the E1-E2 and E1-E3. The N-terminal region of E1, peptides 18YVEEM22 and 27ENPKSVHKSWDIF39 constitute the binding region responsible for the assembly of the E1 with both the E2 and E3 components into OGDH. A E2 region comprising residues from both a linker region and from the catalytic domain is critical for interacting with E1 |
759491 |
