Asp295 Stabilizes the Active-Site Loop Structure of Pyruvate Dehydrogenase, Facilitating Phosphorylation of Ser292 by Pyruvate Dehydrogenase-Kinase

Kinetic parameters of WT AtPDC E1 and site-directed mutants. Activities were determined by assaying decarboxylation of [1-14C] pyruvate in the presence of 1.8 μM K3Fe(CN)6.

Enzyme Research

tab2

Table 2

Table 2: Asp295 Stabilizes the Active-Site Loop Structure of Pyruvate Dehydrogenase, Facilitating Phosphorylation of Ser292 by Pyruvate Dehydrogenase-Kinase 

Table 2 | Asp295 Stabilizes the Active-Site Loop Structure of Pyruvate Dehydrogenase, Facilitating Phosphorylation of Ser292 by Pyruvate Dehydrogenase-Kinase 