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Related Experiment Video

Updated: May 12, 2026

Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry

Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry

Published on: October 18, 2019

Biosynthesis of the urease metallocenter.

Mark A Farrugia¹, Lee Macomber, Robert P Hausinger

¹Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.

The Journal of Biological Chemistry

|March 30, 2013

Summary

This summary is machine-generated.

This study reviews the intricate assembly of nickel active sites in urease, a crucial enzyme. Accessory proteins like UreD/UreH, UreE, UreF, and UreG are essential for nickel insertion and enzyme activation.

Keywords:

Biosynthesis Chaperone Chaperonin GTPase Metalloenzymes Nickel Urease

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Last Updated: May 12, 2026

Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry

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Published on: October 18, 2019

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

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Published on: April 4, 2014

Area of Science:

Biochemistry
Enzymology
Metalloprotein chemistry

Background:

Metalloenzymes require complex systems for assembling their active sites.
The dinuclear nickel enzyme urease serves as a model for studying metallocenter assembly.
Urease plays a significant role in medicine.

Purpose of the Study:

To review the current understanding of urease metallocenter assembly.
To elucidate the roles of accessory proteins in urease activation.
To present recent findings on the urease maturation process.

Main Methods:

Minireview of existing literature.
Analysis of accessory protein functions (UreD/UreH, UreE, UreF, UreG).
Discussion of GTP-dependent nickel insertion mechanisms.

Main Results:

Accessory proteins are critical for delivering nickel to the urease active site.
These proteins facilitate conformational changes and post-translational modifications.
The precise roles and interactions of each accessory protein are under active investigation.

Conclusions:

Urease activation is a complex, multi-protein-mediated process.
Understanding urease assembly provides insights into metalloenzyme function.
Ongoing research continues to refine the model of urease maturation.