Kinase: Difference between revisions

From WikiMD's Wellness Encyclopedia

CSV import
Tags: mobile edit mobile web edit
CSV import
Line 1: Line 1:
'''Kinase''' is a type of [[enzyme]] that catalyzes the transfer of [[phosphate groups]] from high-energy, phosphate-donating molecules to specific substrates. This process, known as [[phosphorylation]], is a key part of many cellular processes.
{{Short description|Enzyme that catalyzes the transfer of phosphate groups}}
{{Use dmy dates|date=October 2023}}


== Function ==
==Overview==
A '''kinase''' is an [[enzyme]] that catalyzes the transfer of [[phosphate]] groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as [[phosphorylation]], a critical mechanism in the regulation of cellular activities. Kinases are part of a larger family of enzymes called [[phosphotransferases]].


Kinases play a crucial role in a variety of cellular processes, including [[cell division]], [[protein regulation]], and [[signal transduction]]. They are involved in the regulation of many types of cellular functions, including [[cell growth]], [[cell differentiation]], [[cell cycle]] control, and [[cell migration]].
==Function==
Kinases play a pivotal role in a wide array of cellular processes, including [[signal transduction]], [[metabolism]], [[cell cycle]] progression, and [[apoptosis]]. By adding phosphate groups to proteins, kinases can alter the activity, interactions, and localization of these proteins, thereby modulating their function.


== Classification ==
==Types of Kinases==
Kinases are classified based on the substrate they phosphorylate:


Kinases can be classified into two broad categories: [[protein kinases]] and [[lipid kinases]]. Protein kinases are responsible for the phosphorylation of proteins, while lipid kinases phosphorylate lipids.
* '''[[Protein kinase|Protein kinases]]''': These enzymes phosphorylate the [[amino acid]] residues of proteins, typically [[serine]], [[threonine]], or [[tyrosine]]. Protein kinases are further divided into serine/threonine kinases and tyrosine kinases.


=== Protein Kinases ===
* '''[[Lipid kinase|Lipid kinases]]''': These kinases phosphorylate lipids, such as [[phosphatidylinositol]], playing a crucial role in [[cell signaling]] pathways.


Protein kinases are a group of enzymes that modify other proteins by chemically adding phosphate groups to them. There are several types of protein kinases, including [[tyrosine kinases]], [[serine/threonine kinases]], and [[dual-specificity kinases]].
* '''[[Carbohydrate kinase|Carbohydrate kinases]]''': These enzymes phosphorylate sugars, which is essential in [[glycolysis]] and other metabolic pathways.


=== Lipid Kinases ===
* '''[[Nucleotide kinase|Nucleotide kinases]]''': These kinases are involved in the phosphorylation of nucleotides, which is important for [[DNA replication]] and [[RNA synthesis]].


Lipid kinases are a group of enzymes that phosphorylate lipids, which are a type of fat molecule. These kinases play a crucial role in [[cell signaling]] and other cellular processes.
==Mechanism of Action==
Kinases function by transferring a phosphate group from a donor molecule, such as [[adenosine triphosphate]] (ATP), to an acceptor molecule. This transfer is facilitated by the kinase's active site, which binds both the donor and acceptor molecules, positioning them for efficient phosphate transfer.


== Role in Disease ==
==Regulation==
The activity of kinases is tightly regulated through various mechanisms, including:


Abnormal kinase activity can lead to a variety of diseases, including [[cancer]], [[inflammatory diseases]], and [[neurodegenerative diseases]]. For example, mutations in the [[BRAF (gene)|BRAF]] gene, which codes for a protein kinase, are associated with several types of cancer.
* '''[[Allosteric regulation]]''': Binding of molecules at sites other than the active site can enhance or inhibit kinase activity.


== See Also ==
* '''[[Phosphorylation]]''': Kinases can be activated or deactivated by phosphorylation by other kinases.


* '''[[Protein-protein interactions]]''': Interaction with other proteins can modulate kinase activity.
* '''[[Subcellular localization]]''': Kinases may be sequestered in specific cellular compartments, affecting their access to substrates.
==Clinical Significance==
Kinases are implicated in numerous diseases, particularly [[cancer]], where dysregulation of kinase activity can lead to uncontrolled cell proliferation. As a result, kinases are a major target for [[drug development]], with many [[kinase inhibitors]] being used as therapeutic agents.
==Images==
[[File:Kinase reaction.svg|thumb|right|300px|Diagram of a kinase reaction, showing the transfer of a phosphate group.]]
[[File:Protein kinase structure.png|thumb|left|300px|Structure of a protein kinase, highlighting the active site.]]
==Related Pages==
* [[Phosphatase]]
* [[Phosphatase]]
* [[Enzyme]]
* [[Signal transduction]]
* [[Signal transduction]]
* [[Protein phosphorylation]]
* [[Cell cycle]]
 
* [[Cancer]]
== References ==
 
<references />


[[Category:Enzymes]]
[[Category:Enzymes]]
[[Category:Cell biology]]
[[Category:Signal transduction]]
[[Category:Molecular biology]]
[[Category:Phosphotransferases]]
[[Category:Biochemistry]]
 
{{stub}}
<gallery>
File:Active_site_of_Dihydroxyacetone_Kinase.png|Kinase
File:Basic_phosphorylation_reaction.png|Kinase
File:Edwin_G._Krebs.jpg|Kinase
File:signal_transduction_pathways.png|Kinase
File:Components_of_the_MAPK_Pathway.png|Kinase
File:PI3_Kinase.tif|Kinase
File:PI3kinase_mechanism.png|Kinase
File:Glycolysis_including_irreversible_steps.png|Kinase
File:Riboflavin_kinase.png|Kinase
File:Riboflavin_mechanism.png|Kinase
File:Thymidine_kinase.png|Kinase
</gallery>

Revision as of 17:33, 18 February 2025

Enzyme that catalyzes the transfer of phosphate groups



Overview

A kinase is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, a critical mechanism in the regulation of cellular activities. Kinases are part of a larger family of enzymes called phosphotransferases.

Function

Kinases play a pivotal role in a wide array of cellular processes, including signal transduction, metabolism, cell cycle progression, and apoptosis. By adding phosphate groups to proteins, kinases can alter the activity, interactions, and localization of these proteins, thereby modulating their function.

Types of Kinases

Kinases are classified based on the substrate they phosphorylate:

Mechanism of Action

Kinases function by transferring a phosphate group from a donor molecule, such as adenosine triphosphate (ATP), to an acceptor molecule. This transfer is facilitated by the kinase's active site, which binds both the donor and acceptor molecules, positioning them for efficient phosphate transfer.

Regulation

The activity of kinases is tightly regulated through various mechanisms, including:

  • Allosteric regulation: Binding of molecules at sites other than the active site can enhance or inhibit kinase activity.
  • Phosphorylation: Kinases can be activated or deactivated by phosphorylation by other kinases.
  • Subcellular localization: Kinases may be sequestered in specific cellular compartments, affecting their access to substrates.

Clinical Significance

Kinases are implicated in numerous diseases, particularly cancer, where dysregulation of kinase activity can lead to uncontrolled cell proliferation. As a result, kinases are a major target for drug development, with many kinase inhibitors being used as therapeutic agents.

Images

File:Kinase reaction.svg
Diagram of a kinase reaction, showing the transfer of a phosphate group.
File:Protein kinase structure.png
Structure of a protein kinase, highlighting the active site.

Related Pages