The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family.
Herein, we report on an in vitro kinetic activity analysis that demonstrates that the protein known as the Akt C-terminal modulator protein is a broad-range, high-activity acyl-CoA thioesterase. In vitro tests of possible activity regulation by product inhibition or by Akt1 binding gave negative results. Truncation mutants confined the thioesterase activity to the C-terminal domain, consistent with our threading model. The N-terminal domain of unknown fold and function was found to contribute to solubility.
Zhao
Hong
H
Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, New Mexico 87131, USA.
Martin
Brian M
BM
Bisoffi
Marco
M
Dunaway-Mariano
Debra
D
D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D010170:Palmitoyl-CoA Hydrolase / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D013816:Thermodynamics; D013869:Thiolester Hydrolases
D048868:Adaptor Proteins, Signal Transducing; D008565:Membrane Proteins; C437985:THEM4 protein, human; D013869:Thiolester Hydrolases; D010170:Palmitoyl-CoA Hydrolase