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Insulin-degrading enzyme hydrolyzes ATP.

María Del Carmen Camberos¹, Juan C Cresto

¹Centro de Investigaciones Endocrinológicas (CEDIE), Hospital de Niños "Ricardo Gutierrez," Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires, Argentina.

Experimental Biology and Medicine (Maywood, N.J.)

|January 30, 2007

Summary

Insulin-degrading enzyme (IDE) possesses ATPase activity, hydrolyzing ATP to facilitate insulin binding and degradation. This activity is concentration-dependent but unaffected by insulin itself.

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Area of Science:

Biochemistry
Enzymology
Molecular Biology

Background:

Insulin-degrading enzyme (IDE) previously shown to be inhibited by ATP.
Investigating ATP hydrolysis as a mechanism for reversing IDE inhibition.

Purpose of the Study:

To determine if IDE possesses ATPase activity.
To understand the relationship between ATP hydrolysis, insulin degradation, and IDE function.

Main Methods:

Assessing ATP hydrolysis via (32)P release from gamma[(32)P]ATP.
Utilizing Sephadex G200 chromatography, immunoprecipitation, and nondissociating gel electrophoresis.
Kinetic analysis (Michaelis-Menten) and inhibitor studies (orthovanadate).

Main Results:

IDE exhibits ATP hydrolysis, correlating with insulin degradation.
ATP hydrolysis follows Michaelis-Menten kinetics (Vmax: 570.45 ± 113.08 pmol Pi/hr, Km: 63.13 ± 3.48 μM).
IDE has one active hydrolytic ATP binding site; insulin binding induces conformational changes, but insulin does not alter IDE's ATPase activity.

Conclusions:

IDE possesses intrinsic ATPase activity.
Insulin binding and degradation are dependent on ATP concentration.
IDE's ATPase function is distinct from its insulin-degrading role, though linked.