IMPDH2: Difference between revisions

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'''Inosine-5'-monophosphate dehydrogenase 2''' ('''IMPDH2''') is an [[enzyme]] that in humans is encoded by the ''IMPDH2'' [[gene]]. IMPDH2 is a member of the IMPDH/GMPR family, which includes [[inosine monophosphate dehydrogenase]] (IMPDH) and [[guanosine monophosphate reductase]] (GMPR).  
 
{{Infobox enzyme
| name = Inosine-5'-monophosphate dehydrogenase 2
| image = <!-- Image removed -->
| width =
| caption =
| EC_number = 1.1.1.205
| CAS_number = 9028-93-1
| GO_code = 0003938
}}
 
'''Inosine-5'-monophosphate dehydrogenase 2''' ('''IMPDH2''') is an [[enzyme]] that plays a crucial role in the [[purine nucleotide]] biosynthesis pathway. It catalyzes the conversion of [[inosine monophosphate]] (IMP) to [[xanthosine monophosphate]] (XMP), a key step in the synthesis of [[guanosine monophosphate]] (GMP).


== Function ==
== Function ==
 
IMPDH2 is a rate-limiting enzyme in the de novo synthesis of [[guanine nucleotides]]. It is essential for the proliferation of [[lymphocytes]] and other rapidly dividing cells. The enzyme is encoded by the [[IMPDH2 gene]] in humans.
The ''IMPDH2'' gene encodes the [[protein]] IMPDH2, which plays a crucial role in the [[purine metabolism|purine metabolic pathway]]. This enzyme catalyzes the [[NAD]]-dependent oxidation of inosine-5'-monophosphate (IMP) into xanthosine-5'-monophosphate (XMP), which is a key step in the de novo synthesis of [[guanine nucleotide]]s.


== Clinical significance ==
== Clinical significance ==
 
IMPDH2 is a target for [[immunosuppressive]] drugs such as [[mycophenolate mofetil]], which is used to prevent [[organ transplant rejection]]. Inhibitors of IMPDH2 are also being investigated for their potential in treating [[cancer]] and [[viral infections]].
Mutations in the ''IMPDH2'' gene have been associated with various diseases. For instance, increased activity of IMPDH2 has been linked to [[cancer]] as it is often overexpressed in tumor cells. Inhibitors of IMPDH2, such as [[mycophenolate mofetil]], are used in [[immunosuppressive therapy]] after organ transplantation and in treatment of autoimmune diseases.


== Structure ==
== Structure ==
The enzyme is a homotetramer, meaning it consists of four identical subunits. Each subunit binds to [[NAD+]] and [[IMP]] as substrates. The active site of IMPDH2 is highly conserved across different species, indicating its importance in cellular metabolism.


The structure of IMPDH2 is composed of two domains: a catalytic domain and a [[Bateman domain]]. The catalytic domain is responsible for the enzymatic activity of IMPDH2, while the Bateman domain is involved in the regulation of the enzyme's activity.
== Regulation ==
IMPDH2 activity is regulated by [[feedback inhibition]] from [[GTP]], the end product of the purine biosynthesis pathway. This regulation ensures a balance between the synthesis of [[adenine]] and guanine nucleotides.


[[File:IMPDH2 structure.png|thumb|right|300px|The structure of IMPDH2. The catalytic domain is shown in blue, and the Bateman domain is shown in green.]]
== Research ==
Recent studies have focused on the role of IMPDH2 in [[metabolic disorders]] and its potential as a [[biomarker]] for certain types of cancer. The enzyme's structure has been elucidated using [[X-ray crystallography]], providing insights into its function and mechanism of action.


== See also ==
== See also ==
* [[Inosine-5'-monophosphate dehydrogenase]]
* [[Purine metabolism]]
* [[Purine metabolism]]
* [[Mycophenolate mofetil]]
* [[Nucleotide synthesis]]
* [[Enzyme inhibitors]]


== References ==
== References ==
<references/>


<references />
== External links ==
* [https://www.wikimd.com/wiki/IMPDH2 IMPDH2 on WikiMD]
* [https://www.ncbi.nlm.nih.gov/gene/3615 IMPDH2 gene information at NCBI]


[[Category:Enzymes]]
[[Category:Enzymes]]
[[Category:Human proteins]]
[[Category:EC 1.1.1]]
[[Category:Genes]]
[[Category:Purine metabolism]]
[[Category:Metabolism]]
[[Category:Immunosuppressive agents]]
{{enzyme-stub}}
{{medicine-stub}}

Latest revision as of 20:35, 30 December 2024


IMPDH2






Inosine-5'-monophosphate dehydrogenase 2 (IMPDH2) is an enzyme that plays a crucial role in the purine nucleotide biosynthesis pathway. It catalyzes the conversion of inosine monophosphate (IMP) to xanthosine monophosphate (XMP), a key step in the synthesis of guanosine monophosphate (GMP).

Function[edit]

IMPDH2 is a rate-limiting enzyme in the de novo synthesis of guanine nucleotides. It is essential for the proliferation of lymphocytes and other rapidly dividing cells. The enzyme is encoded by the IMPDH2 gene in humans.

Clinical significance[edit]

IMPDH2 is a target for immunosuppressive drugs such as mycophenolate mofetil, which is used to prevent organ transplant rejection. Inhibitors of IMPDH2 are also being investigated for their potential in treating cancer and viral infections.

Structure[edit]

The enzyme is a homotetramer, meaning it consists of four identical subunits. Each subunit binds to NAD+ and IMP as substrates. The active site of IMPDH2 is highly conserved across different species, indicating its importance in cellular metabolism.

Regulation[edit]

IMPDH2 activity is regulated by feedback inhibition from GTP, the end product of the purine biosynthesis pathway. This regulation ensures a balance between the synthesis of adenine and guanine nucleotides.

Research[edit]

Recent studies have focused on the role of IMPDH2 in metabolic disorders and its potential as a biomarker for certain types of cancer. The enzyme's structure has been elucidated using X-ray crystallography, providing insights into its function and mechanism of action.

See also[edit]

References[edit]

<references/>

External links[edit]

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