Publisher conditions are provided by RoMEO. The model is then matched with the structures of any of the individual subunits that have been solved by X-ray crystallography or NMR. This part of the reaction is catalyzed by a part of PDC composed of E 1 subunits. Indeed, using quantitative structure activity relationship QSAR analysis on a peptide-xenobiotic conjugate microarray platform, we have demonstrated that when the lipoyl domain of PDC-E2 was modified with specific synthetic small molecule lipoyl mimics, the ensuing structures displayed highly specific reactivity to PBC sera, at levels often higher than the native PDC-E2 molecule. Other names in common use include MtPDC mitochondrial pyruvate dehydogenase complex , pyruvate decarboxylase , pyruvate dehydrogenase , pyruvate dehydrogenase lipoamide , pyruvate dehydrogenase complex , pyruvate: Posted by Laurence A.
The E1-binding domain forms the pivot about which the swinging linker arms holding the L1 and L2 lipoyl domains move. The N-terminal segment appears to be forming a foundation for the stable beginning of the linker segment exterior to the tE2 core. Similarly, the long helix H4 in A. This suggests that the linker regions connecting IC to the E1-binding domain in mammalian E2 must maintain substantial separation.
Cholesterol side-chain cleavage enzyme Steroid beta-hydroxylase Aldosterone synthase Frataxin. Their goal is to characterize as many inhibitors as possible. Briefly, E2 was expressed in E. A detailed comparison of our pseudo atomic model of human tE2 with the atomic model of A. Author information Copyright and License information Disclaimer.