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Enzymes

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

Enzyme Inhibition

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.

Feedback Inhibition

Feedback Inhibition

Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!

Indirect-Acting Cholinergic Agonists: Mechanism of Action

Indirect-Acting Cholinergic Agonists: Mechanism of Action

Indirect-acting cholinergic agonists work by interacting with an enzyme called acetylcholinesterase (AChE) in the synaptic cleft. They can be reversible or irreversible inhibitors and have different effects on the enzyme.
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex,...

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Engineering Antiviral Agents via Surface Plasmon Resonance

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Structural Basis for Inhibition of the SARS-CoV-2 nsp16 by Substrate-Based Dual Site Inhibitors.

Gints Kalnins¹, Laura Rudusa², Anna L Bula²

¹Latvian Biomedical Research and Study Centre, Ratsupites 1 k-1, LV1067, Riga, Latvia.

|September 11, 2024

Summary

Coronaviruses use specific enzymes for mRNA capping, crucial for evading immunity. Targeting these enzymes, like nsp16-nsp10, with dual-site inhibitors shows promise for developing antiviral therapies.

Keywords:

Medicinal chemistry Methyltransferase SARS-CoV-2 Structural biology nsp16

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Last Updated: Jun 13, 2025

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Published on: June 14, 2022

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Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

Area of Science:

Virology
Structural Biology
Biochemistry

Background:

Coronaviruses, including SARS-CoV-2, utilize a unique mRNA 5' capping mechanism.
Two key enzymes, nsp14 and nsp16-nsp10, are involved in viral mRNA methylation.
The 2'-O-methylation by nsp16-nsp10 is vital for viral RNA to evade host innate immunity.

Purpose of the Study:

To investigate the nsp16-nsp10 enzyme's active site using X-ray crystallography.
To analyze the binding of S-adenosylmethionine (SAM) analogues to nsp16-nsp10.
To explore potential inhibition strategies against coronavirus replication.

Main Methods:

X-ray crystallography was used to determine the 3D structures of nsp16-nsp10 complexes.
Eleven crystal structures were obtained with SAM-derived inhibitors.
Analysis focused on the binding interactions within the enzyme's active site.

Main Results:

Eleven distinct 3D crystal structures of nsp16-nsp10 with SAM analogues were determined.
Observed variations in the conformations of the methionine-substituting moieties within the inhibitors.
Confirmed that simultaneously targeting both SAM and RNA binding sites enhances inhibitory potential.

Conclusions:

The nsp16-nsp10 enzyme's active site accommodates SAM analogues, revealing structural insights.
Dual-site inhibition strategies targeting both SAM and RNA binding sites are effective.
This research provides a foundation for designing potent nsp16-nsp10 inhibitors as antiviral agents.