Nucleoside-diphosphatase: Difference between revisions

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'''Nucleoside-diphosphatase''' is an [[enzyme]] that catalyzes the hydrolysis of [[nucleoside diphosphates]]. This enzyme plays a crucial role in the [[purine metabolism|metabolism of purines]] and [[pyrimidine metabolism|pyrimidines]], which are vital components of [[nucleic acids]] such as [[DNA]] and [[RNA]].
{{DISPLAYTITLE:Nucleoside-diphosphatase}}
 
== Nucleoside-diphosphatase ==
[[File:2h2n.jpg|thumb|right|Structure of Nucleoside-diphosphatase]]
 
'''Nucleoside-diphosphatase''' (NDPase) is an enzyme that catalyzes the hydrolysis of nucleoside diphosphates into nucleoside monophosphates and inorganic phosphate. This enzyme plays a crucial role in nucleotide metabolism and is involved in various cellular processes, including [[DNA replication]], [[RNA synthesis]], and [[cell signaling]].


== Function ==
== Function ==
Nucleoside-diphosphatase is responsible for the conversion of nucleoside diphosphates (NDPs) to nucleoside monophosphates (NMPs) by removing a phosphate group. This reaction is important for maintaining the balance of nucleotides within the cell and for the recycling of nucleotides during nucleic acid metabolism.


Nucleoside-diphosphatase is involved in the process of [[nucleotide]] degradation, where it catalyzes the conversion of nucleoside diphosphates into nucleoside monophosphates and inorganic [[phosphate]]. This reaction is important for the regulation of nucleotide pools within the cell, ensuring that there is a balance between the synthesis and degradation of nucleotides.
== Mechanism ==
The enzyme operates by binding to the nucleoside diphosphate substrate and facilitating the cleavage of the phosphoanhydride bond. This process involves the coordination of a water molecule, which acts as a nucleophile to attack the phosphorus atom, leading to the release of inorganic phosphate and the formation of a nucleoside monophosphate.


== Structure ==
== Structure ==
Nucleoside-diphosphatases are typically composed of a single polypeptide chain that folds into a specific three-dimensional structure necessary for its enzymatic activity. The active site of the enzyme is usually located in a cleft or pocket that accommodates the substrate and facilitates the catalytic reaction.


The structure of nucleoside-diphosphatase is highly conserved across different species, indicating its importance in cellular function. The enzyme is typically composed of a single polypeptide chain, with a catalytic site that binds to the nucleoside diphosphate substrate.
== Biological Importance ==
 
Nucleoside-diphosphatases are essential for the proper functioning of cellular processes that require nucleotides. They are involved in the regulation of nucleotide pools, which is critical for [[DNA repair]], [[cell division]], and [[signal transduction]].
== Clinical significance ==


Alterations in the activity of nucleoside-diphosphatase have been associated with several diseases, including [[cancer]], [[autoimmune diseases]], and [[neurodegenerative diseases]]. In particular, increased activity of this enzyme has been observed in certain types of cancer, suggesting that it may play a role in tumor growth and progression.
== Related Enzymes ==
 
Nucleoside-diphosphatase is part of a larger family of enzymes known as [[nucleotidases]], which are responsible for the hydrolysis of nucleotides. Other related enzymes include [[nucleoside-triphosphatase]] and [[nucleoside-monophosphatase]], which act on different substrates within the nucleotide metabolism pathway.
== See also ==


== Related pages ==
* [[Nucleotide metabolism]]
* [[Enzyme kinetics]]
* [[Phosphatase]]
* [[Nucleoside]]
* [[Nucleoside]]
* [[Nucleotide]]
* [[Enzyme]]
* [[Purine metabolism]]
* [[Pyrimidine metabolism]]
== References ==
<references />
{{medicine-stub}}


[[Category:Enzymes]]
[[Category:Enzymes]]
[[Category:Metabolism]]
[[Category:Nucleotide metabolism]]
[[Category:Biochemistry]]
[[Category:Cell biology]]
[[Category:Molecular biology]]

Latest revision as of 10:59, 15 February 2025


Nucleoside-diphosphatase[edit]

Structure of Nucleoside-diphosphatase

Nucleoside-diphosphatase (NDPase) is an enzyme that catalyzes the hydrolysis of nucleoside diphosphates into nucleoside monophosphates and inorganic phosphate. This enzyme plays a crucial role in nucleotide metabolism and is involved in various cellular processes, including DNA replication, RNA synthesis, and cell signaling.

Function[edit]

Nucleoside-diphosphatase is responsible for the conversion of nucleoside diphosphates (NDPs) to nucleoside monophosphates (NMPs) by removing a phosphate group. This reaction is important for maintaining the balance of nucleotides within the cell and for the recycling of nucleotides during nucleic acid metabolism.

Mechanism[edit]

The enzyme operates by binding to the nucleoside diphosphate substrate and facilitating the cleavage of the phosphoanhydride bond. This process involves the coordination of a water molecule, which acts as a nucleophile to attack the phosphorus atom, leading to the release of inorganic phosphate and the formation of a nucleoside monophosphate.

Structure[edit]

Nucleoside-diphosphatases are typically composed of a single polypeptide chain that folds into a specific three-dimensional structure necessary for its enzymatic activity. The active site of the enzyme is usually located in a cleft or pocket that accommodates the substrate and facilitates the catalytic reaction.

Biological Importance[edit]

Nucleoside-diphosphatases are essential for the proper functioning of cellular processes that require nucleotides. They are involved in the regulation of nucleotide pools, which is critical for DNA repair, cell division, and signal transduction.

Related Enzymes[edit]

Nucleoside-diphosphatase is part of a larger family of enzymes known as nucleotidases, which are responsible for the hydrolysis of nucleotides. Other related enzymes include nucleoside-triphosphatase and nucleoside-monophosphatase, which act on different substrates within the nucleotide metabolism pathway.

Related pages[edit]