EC Number   |
General Information |
Reference |
|---|
   1.2.4.2 | malfunction |
enzyme knockdown diminishes histone H4K12 succinylation |
762764 |
| 1.2.4.2 | malfunction |
the lack in the expression of enzyme genes reduces respiratory rates and affects the photosynthesis |
759969 |
| 1.2.4.2 | metabolism |
isoform E1-OGDH1 is essential to the final 2-OGDH activity in leaves |
759969 |
| 1.2.4.2 | metabolism |
the enzyme creates an additional source of superoxide/hydrogen peroxide from 2-oxoadipate as alternative substrate |
759216 |
| 1.2.4.2 | physiological function |
during late stages of erythropoiesis, cellular metabolism is remodeled so that glutamine is the precursor for 5-aminolevulinate following deamination to 2-oxoglutarate and conversion to succinyl-CoA by 2-oxoglutarate dehydrogenase without equilibration or passage through the TCA cycle. This may be facilitated by a direct interaction between 5-aminolevulinate synthase 2 and 2-oxoglutarate dehydrogenase. Succinate is not an effective precursor for heme |
762857 |
| 1.2.4.2 | 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 |
| 1.2.4.2 | physiological function |
histone H2A.Z-bound chromatin is associated with metabolic enzymes, oxoglutarate dehydrogenase (OGDH) and acetyl-CoA acyltransferase 2 (ACAA2) in the nucleus. OGDH and ACAA2 predominantly associate with H2A.Z-occupied transcription start sites and enhancers |
756086 |
| 1.2.4.2 | physiological function |
histone H2A.Z-deficient human HAP1 cells exhibit reduced chromatin-bound metabolic enzymes, accompanied with reduced posttranslational histone modifications, including acetylation and succinylation. Knockdown of OGDH diminishes histone H4 succinylation |
756086 |
| 1.2.4.2 | 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 |
| 1.2.4.2 | physiological function |
isoenzymes 2-oxoglutarate dehydrogenase (OGDH) and 2-oxoadipate dehydrogenase (OADH) show a 100fold difference in their ratio in the heart and liver, but similar Michaelis saturations by 2-oxoglutarate are inherent in the enzyme preparations from these tissues. In the heart, OADH/OGDH ratio is about 0.01, and OADH possesses low-affinity sites to 2-oxoadipate. In liver preparation, OADH/OGDH ratio is about 1.6, and OADH a biphasic saturation with 2-oxoadipate |
763067 |
