Ontology highlight
ABSTRACT:
SUBMITTER: Zhao H
PROVIDER: S-EPMC2803014 | biostudies-literature | 2009 Jun
REPOSITORIES: biostudies-literature
Zhao Hong H Martin Brian M BM Bisoffi Marco M Dunaway-Mariano Debra D
Biochemistry 20090601 24
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 ...[more]