| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-158 |
Sentence |
denotes |
The C-terminal hinge region of lipoic acid-bearing domain of E2b is essential for domain interaction with branched-chain alpha-keto acid dehydrogenase kinase. |
| T2 |
159-393 |
Sentence |
denotes |
The branched-chain alpha-keto acid dehydrogenase (BCKD) kinase (abbreviated as BCK) down-regulates activity of the mammalian mitochondrial BCKD complex by reversible phosphorylation of the decarboxylase (E1b) component of the complex. |
| T3 |
394-511 |
Sentence |
denotes |
The binding of BCK to the holotransacylase (E2b) core of the BCKD complex results in the stimulation of BCK activity. |
| T4 |
512-638 |
Sentence |
denotes |
Here we show that the lipoylated lipoic acid-bearing domain (lip-LBD) (residues 1-84) of E2b alone does not interact with BCK. |
| T5 |
639-820 |
Sentence |
denotes |
However, lip-LBD constructs containing various lengths of the C-terminal hinge region of LBD are able to bind to BCK as measured by a newly developed solubility-based binding assay. |
| T6 |
821-1100 |
Sentence |
denotes |
Isothermal titration calorimetry measurements produced a dissociation constant of 8.06 x 10(-6) m and binding enthalpy of -3.68 kcal/mol for the interaction of BCK with a construct containing lip-LBD and the Glu-Glu-Asp-Xaa-Xaa-Glu sequence of the C-terminal hinge region of LBD. |
| T7 |
1101-1311 |
Sentence |
denotes |
These thermodynamic parameters are similar to those obtained for binding of BCK to a lipoylated di-domain construct, which harbors LBD, the entire hinge region, and the downstream subunit-binding domain of E2b. |
| T8 |
1312-1491 |
Sentence |
denotes |
Our data establish that the C-terminal hinge region of LBD containing the above negatively charged residues is essential for the interaction between the lip-LBD construct and BCK. |
