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Urease activity in the crystalline state

M B Moncrief¹, L G Hom, E Jabri

¹Department of Biochemistry, Michigan State University, East Lansing 48824-1101, USA.

Protein Science : a Publication of the Protein Society

|October 1, 1995

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Crystalline urease from Klebsiella aerogenes shows minimal activity (<0.05%) compared to soluble enzyme. This inactivity is not due to salt inhibition or denaturation, but likely conformational changes in the crystal structure.

Area of Science:

Biochemistry
Enzymology
Structural Biology

Background:

Urease is a crucial enzyme catalyzing urea hydrolysis.
Understanding enzyme activity in crystalline form is vital for structural and functional studies.
Klebsiella aerogenes urease crystallization was previously reported.

Purpose of the Study:

To investigate the low activity of crystalline Klebsiella aerogenes urease.
To determine the factors contributing to the diminished catalytic rate in the crystalline state.
To elucidate the structural basis for urease inactivity in crystals.

Main Methods:

Enzyme activity assays of crystalline and soluble urease.
Investigation of lithium sulfate (Li2SO4) inhibition.
Analysis of enzyme activity after crystal dissolution.

Related Experiment Videos

Assessment of substrate diffusion limitations in crystals.

Main Results:

Crystalline urease exhibited <0.05% activity of soluble urease.
Lithium sulfate showed mixed inhibition but did not fully explain the low activity.
Crystal dissolution recovered ~43% of soluble enzyme activity.
Crushed crystals showed only a minor increase in activity, ruling out diffusion limitation.

Conclusions:

Urease is largely inactive in its crystalline form.
Conformational restrictions, potentially an active site lid, likely cause the inactivity.
Observed low activity may stem from surface enzyme or minor dissolution.