Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Feature 1:TPP-binding site [chemical binding site]
Evidence:
Comment:TPP = thiamine pyrophosphate or thiamine diphosphate
Structure:1DTW; Human pyruvate dehydrogenase binds TPP and divalent metal ion; contacts at 3.5A
Structure:1OLX; Human branched-chain alpha-ketoacid dehydrogenase binds TPP and divalent metal ion; contacts at 3.5A
Structure:1UMD; Thermus thermophilus branched-chain 2-oxo Acid Dehydrogenase binds the reaction intermediate 2-(1-hydroxyalkyl)-TPP and divalent metal ion; contacts at 3.5A
Structure:1QSO; Pseudomonas 2-oxoisovalerate dehydrogenase binds TPP and divalent metal ion; contacts at 3.5A
Jiyao W et al.(2023). "The conserved domain database in 2023.",