| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-121 |
Sentence |
denotes |
Tetrameric assembly and conservation in the ATP-binding domain of rat branched-chain alpha-ketoacid dehydrogenase kinase. |
| T2 |
122-248 |
Sentence |
denotes |
We showed previously that the rat branched-chain alpha-ketoacid dehydrogenase (BCKD) kinase is capable of autophosphorylation. |
| T3 |
249-390 |
Sentence |
denotes |
However, despite its sequence similarity to bacterial histidine protein kinases, BCKD kinase does not function as a histidine protein kinase. |
| T4 |
391-556 |
Sentence |
denotes |
In the present study, we report that the rat BCKD kinase exists as a homotetramer of M(r) = 185,000, based on results of gel filtration and dynamic light scattering. |
| T5 |
557-666 |
Sentence |
denotes |
This is in contrast to the related mammalian pyruvate dehydrogenase kinase isozymes that occur as homodimers. |
| T6 |
667-837 |
Sentence |
denotes |
The tetrameric assembly of BCKD kinase was confirmed by the presence of four 5'-adenylyl-imidodiphosphate-binding sites (K(D) = 4.1 x 10(-6)m) per molecule of the kinase. |
| T7 |
838-1028 |
Sentence |
denotes |
Incubation of the BCKD kinase with increasing concentrations of urea resulted in dissociation of the tetramer to dimers and eventually to monomers as separated on a sucrose density gradient. |
| T8 |
1029-1163 |
Sentence |
denotes |
Both tetramers and dimers, but not the monomer, maintained the conformation capable of binding ATP and undergoing autophosphorylation. |
| T9 |
1164-1356 |
Sentence |
denotes |
BCKD kinase depends on a fully lipoylated transacylase for maximal activity, but the interaction between the kinase and the transacylase is impeded in the presence of high salt concentrations. |
| T10 |
1357-1507 |
Sentence |
denotes |
Alterations of conserved residues in the ATP-binding domain led to a marked reduction or complete loss in the catalytic efficiency of the BCKD kinase. |
| T11 |
1508-1642 |
Sentence |
denotes |
The results indicate that BCKD kinase, similar to pyruvate dehydrogenase kinase isozymes, belongs to the superfamily of ATPase/kinase. |
