CATH Classification

Domain Context

CATH Clusters

Superfamily Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain
Functional Family [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial

Enzyme Information

2.7.11.2
[Pyruvate dehydrogenase (acetyl-transferring)] kinase.
based on mapping to UniProt Q15119
ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.
-!- Has no activating compound but is specific for its substrate. -!- A mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. -!- Phosphorylation inactivates EC 1.2.4.1. -!- Formerly EC 2.7.1.99.

UniProtKB Entries (1)

Q15119
PDK2_HUMAN
Homo sapiens
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial

PDB Structure

PDB 5M4N
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Application of Off-Rate Screening in the Identification of Novel Pan-Isoform Inhibitors of Pyruvate Dehydrogenase Kinase.
Brough, P.A., Baker, L., Bedford, S., Brown, K., Chavda, S., Chell, V., D'Alessandro, J., Davies, N.G., Davis, B., Le Strat, L., Macias, A.T., Maddox, D., Mahon, P.C., Massey, A.J., Matassova, N., McKenna, S., Meissner, J.W., Moore, J.D., Murray, J.B., Northfield, C.J., Parry, C., Parsons, R., Roughley, S.D., Shaw, T., Simmonite, H., Stokes, S., Surgenor, A., Stefaniak, E., Robertson, A., Wang, Y., Webb, P., Whitehead, N., Wood, M.
J. Med. Chem.