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Arginase-boronic acid complex highlights a physiological role in erectile function.

J D Cox¹, N N Kim, A M Traish

¹Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, USA.

Nature Structural Biology

|December 14, 1999

Summary

The crystal structure of arginase bound to ABH reveals its transition state mimicry. Arginase inhibition in the penis enhances erectile function, suggesting therapeutic potential for erectile dysfunction.

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Area of Science:

Biochemistry
Structural Biology
Pharmacology

Background:

Arginase is a binuclear manganese metalloenzyme.
L-arginine is a substrate for arginase and nitric oxide (NO) synthase.
Erectile function is NO-dependent.

Purpose of the Study:

To determine the crystal structure of arginase complexed with 2(S)-amino-6-boronohexanoic acid (ABH).
To investigate the role of penile arginase in erectile function.
To explore arginase as a therapeutic target for erectile dysfunction.

Main Methods:

X-ray crystallography at 1.7 A resolution.
Biochemical assays to assess enzyme activity and binding.
In vitro studies on penile smooth muscle relaxation.

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Main Results:

The crystal structure shows ABH binding as a boronate anion, mimicking a transition state.
This binding mode explains ABH's lack of inhibition against NO synthase.
Arginase activity was detected in the penis, and ABH enhanced smooth muscle relaxation.

Conclusions:

The determined structure provides insights into arginase inhibition mechanisms.
Penile arginase plays a role in regulating NO-dependent smooth muscle relaxation.
Inhibiting penile arginase may be a viable strategy for treating erectile dysfunction.