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Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Protein Kinases and Phosphatases

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Related Experiment Video

Updated: Jun 27, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

A structural and catalytic model for zinc phosphoesterases.

Rebecca R Buchholz¹, Morgan E Etienne, Anneke Dorgelo

¹School of Molecular and Microbial Sciences, The University of Queensland, Queensland, Australia 4072.

Dalton Transactions (Cambridge, England : 2003)

|December 17, 2008

Summary

This study synthesized a structural model for phosphoesterases, crucial enzymes for degrading neurotoxins. The zinc complex demonstrated catalytic activity in breaking down organophosphate neurotoxins.

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Published on: May 13, 2020

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Modeling an Enzyme Active Site using Molecular Visualization Freeware

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Area of Science:

Coordination Chemistry
Bioinorganic Chemistry
Enzyme Mimicry

Background:

Phosphoesterases are vital enzymes that hydrolyze organophosphate compounds, including dangerous neurotoxins.
Developing artificial models of enzyme active sites can provide insights into their mechanisms and lead to new catalysts.

Purpose of the Study:

To synthesize and characterize a structural model of a phosphoesterase active site using zinc(II) complexes.
To investigate the catalytic activity of the synthesized zinc complex in the hydrolysis of organophosphate substrates.

Main Methods:

Synthesis and characterization of a novel ligand (H(3)L1) and its zinc(II) complexes.
Structural elucidation using X-ray crystallography.
Functional studies involving kinetic analysis of substrate hydrolysis (bis(4-nitrophenyl)phosphate).

Main Results:

A tetrameric structure of dinuclear zinc complexes bridged by phosphate and acetate ligands was revealed by X-ray crystallography.
The zinc complex with HL1(2-) ligand was found to be a competent catalyst for the hydrolysis of bis(4-nitrophenyl)phosphate.
A catalytic rate constant (kcat) of 1.26 ± 0.06 x 10^-6 s^-1 was determined for the hydrolysis reaction.

Conclusions:

The synthesized zinc complex serves as a functional structural model for phosphoesterase active sites.
This model demonstrates the potential for designing artificial enzymes for the degradation of organophosphate neurotoxins.
The study provides a foundation for further development of efficient catalytic systems for detoxification.