Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Adaptor Proteins, Signal Transducing / chemistry*
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Adaptor Proteins, Signal Transducing / genetics
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Adaptor Proteins, Signal Transducing / metabolism
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Kinetics
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Membrane Proteins / chemistry*
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Membrane Proteins / genetics
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Membrane Proteins / metabolism
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Models, Molecular
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Palmitoyl-CoA Hydrolase / chemistry*
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Palmitoyl-CoA Hydrolase / metabolism
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Protein Conformation
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Thermodynamics
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Thiolester Hydrolases
Substances
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Adaptor Proteins, Signal Transducing
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Membrane Proteins
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THEM4 protein, human
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Thiolester Hydrolases
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Palmitoyl-CoA Hydrolase