6,7-dihydropteridine reductase: Difference between revisions
CSV import |
CSV import Tags: mobile edit mobile web edit |
||
| Line 1: | Line 1: | ||
{{DISPLAYTITLE:6,7-Dihydropteridine reductase}} | {{DISPLAYTITLE:6,7-Dihydropteridine reductase}} | ||
== 6,7-Dihydropteridine Reductase == | |||
[[File:6,7-dihydropteridine_reductase_1hdr.jpg|thumb|right|Structure of 6,7-Dihydropteridine Reductase]] | |||
6,7-Dihydropteridine reductase (DHPR) is an enzyme that plays a crucial role in the metabolism of [[tetrahydrobiopterin]] (BH4), a cofactor essential for the hydroxylation of aromatic amino acids such as [[phenylalanine]], [[tyrosine]], and [[tryptophan]]. This enzyme is encoded by the [[QDPR]] gene in humans. | |||
==Function== | == Function == | ||
DHPR is responsible for the | DHPR is responsible for the reduction of [[quinonoid dihydrobiopterin]] (qBH2) back to BH4. This reaction is vital for maintaining adequate levels of BH4, which is necessary for the proper function of several [[hydroxylase]] enzymes. These enzymes are involved in the synthesis of important neurotransmitters, including [[dopamine]], [[serotonin]], and [[norepinephrine]]. | ||
== | == Clinical Significance == | ||
Deficiency in DHPR activity can lead to a rare metabolic disorder known as [[dihydropteridine reductase deficiency]]. This condition is characterized by hyperphenylalaninemia and can result in neurological symptoms due to impaired neurotransmitter synthesis. Early diagnosis and treatment are crucial to prevent severe developmental delays and neurological damage. | |||
== | == Structure == | ||
The | The structure of DHPR has been elucidated through [[X-ray crystallography]], revealing a homodimeric enzyme with each subunit containing a [[NADH]] binding domain. The active site of DHPR is highly conserved and is responsible for the enzyme's catalytic activity. | ||
== | == Related Enzymes == | ||
DHPR | DHPR is part of the [[pteridine]] reductase family, which includes other enzymes involved in the metabolism of pteridine derivatives. These enzymes share structural similarities and often have overlapping substrate specificities. | ||
==Related | == Related Pages == | ||
* [[Tetrahydrobiopterin]] | * [[Tetrahydrobiopterin]] | ||
* [[Phenylalanine hydroxylase]] | * [[Phenylalanine hydroxylase]] | ||
* [[ | * [[Dihydropteridine reductase deficiency]] | ||
* [[Neurotransmitter]] | * [[Neurotransmitter synthesis]] | ||
[[Category:Enzymes]] | [[Category:Enzymes]] | ||
[[Category: | [[Category:Metabolic disorders]] | ||
[[Category: | [[Category:Neurotransmitter metabolism]] | ||
Revision as of 11:35, 15 February 2025
6,7-Dihydropteridine Reductase
6,7-Dihydropteridine reductase (DHPR) is an enzyme that plays a crucial role in the metabolism of tetrahydrobiopterin (BH4), a cofactor essential for the hydroxylation of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. This enzyme is encoded by the QDPR gene in humans.
Function
DHPR is responsible for the reduction of quinonoid dihydrobiopterin (qBH2) back to BH4. This reaction is vital for maintaining adequate levels of BH4, which is necessary for the proper function of several hydroxylase enzymes. These enzymes are involved in the synthesis of important neurotransmitters, including dopamine, serotonin, and norepinephrine.
Clinical Significance
Deficiency in DHPR activity can lead to a rare metabolic disorder known as dihydropteridine reductase deficiency. This condition is characterized by hyperphenylalaninemia and can result in neurological symptoms due to impaired neurotransmitter synthesis. Early diagnosis and treatment are crucial to prevent severe developmental delays and neurological damage.
Structure
The structure of DHPR has been elucidated through X-ray crystallography, revealing a homodimeric enzyme with each subunit containing a NADH binding domain. The active site of DHPR is highly conserved and is responsible for the enzyme's catalytic activity.
Related Enzymes
DHPR is part of the pteridine reductase family, which includes other enzymes involved in the metabolism of pteridine derivatives. These enzymes share structural similarities and often have overlapping substrate specificities.
