Urocanase: Difference between revisions
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== Urocanase == | == Urocanase == | ||
[[File:PDB_2fkn_EBI.png|thumb|right|Crystal structure of urocanase (PDB ID: 2fkn)]] | |||
'''Urocanase''' is an enzyme that plays a crucial role in the [[histidine]] degradation pathway. It catalyzes the conversion of [[urocanic acid]] to [[imidazolonepropionic acid]], a key step in the catabolism of histidine. This enzyme is found in various organisms, including bacteria, fungi, and mammals. | |||
Urocanase is | == Function == | ||
Urocanase is responsible for the hydration of urocanic acid, resulting in the formation of imidazolonepropionic acid. This reaction is part of the metabolic pathway that breaks down histidine, an essential amino acid, into smaller molecules that can be utilized for energy production or other biosynthetic processes. | |||
== | == Structure == | ||
The enzyme urocanase is a member of the [[amidohydrolase]] superfamily. It typically functions as a homodimer, with each subunit contributing to the active site. The crystal structure of urocanase, as shown in the image, reveals a complex arrangement of alpha-helices and beta-sheets that form the active site pocket where the substrate binds. | |||
== Mechanism == | |||
Urocanase catalyzes the hydration of urocanic acid through a mechanism that involves the addition of a water molecule across the double bond of the imidazole ring. This reaction is facilitated by the presence of a tightly bound [[NAD+]] cofactor, which is essential for the enzyme's activity. The conversion of urocanic acid to imidazolonepropionic acid is a reversible reaction, although in vivo it proceeds predominantly in the forward direction. | |||
=== | == Biological Significance == | ||
In humans, urocanase is primarily found in the liver, where it participates in the degradation of dietary histidine. The product of the urocanase reaction, imidazolonepropionic acid, is further metabolized to form [[glutamic acid]], which can then enter the [[tricarboxylic acid cycle]] for energy production. Deficiencies in urocanase activity can lead to the accumulation of urocanic acid, which has been associated with certain metabolic disorders. | |||
== Clinical Relevance == | |||
Urocanase deficiency is a rare metabolic disorder that can result in elevated levels of urocanic acid in the body. This condition, known as urocanic aciduria, may present with symptoms such as developmental delay and skin abnormalities. Diagnosis is typically made through the detection of increased urocanic acid in the urine. | |||
== Related Pages == | |||
* [[Histidine metabolism]] | |||
* [[Amidohydrolase]] | |||
* [[NAD+]] | |||
* [[Tricarboxylic acid cycle]] | |||
[[File:Imidazol-4-one-5-propionic_acid.png|thumb|right|Chemical structure of imidazolonepropionic acid]] | |||
{{Enzyme-stub}} | |||
{{Metabolism-stub}} | |||
[[Category:Enzymes]] | [[Category:Enzymes]] | ||
[[Category:Metabolism]] | [[Category:Metabolism]] | ||
[[Category: | [[Category:Histidine metabolism]] | ||
Latest revision as of 18:48, 23 March 2025
Urocanase[edit]
Urocanase is an enzyme that plays a crucial role in the histidine degradation pathway. It catalyzes the conversion of urocanic acid to imidazolonepropionic acid, a key step in the catabolism of histidine. This enzyme is found in various organisms, including bacteria, fungi, and mammals.
Function[edit]
Urocanase is responsible for the hydration of urocanic acid, resulting in the formation of imidazolonepropionic acid. This reaction is part of the metabolic pathway that breaks down histidine, an essential amino acid, into smaller molecules that can be utilized for energy production or other biosynthetic processes.
Structure[edit]
The enzyme urocanase is a member of the amidohydrolase superfamily. It typically functions as a homodimer, with each subunit contributing to the active site. The crystal structure of urocanase, as shown in the image, reveals a complex arrangement of alpha-helices and beta-sheets that form the active site pocket where the substrate binds.
Mechanism[edit]
Urocanase catalyzes the hydration of urocanic acid through a mechanism that involves the addition of a water molecule across the double bond of the imidazole ring. This reaction is facilitated by the presence of a tightly bound NAD+ cofactor, which is essential for the enzyme's activity. The conversion of urocanic acid to imidazolonepropionic acid is a reversible reaction, although in vivo it proceeds predominantly in the forward direction.
Biological Significance[edit]
In humans, urocanase is primarily found in the liver, where it participates in the degradation of dietary histidine. The product of the urocanase reaction, imidazolonepropionic acid, is further metabolized to form glutamic acid, which can then enter the tricarboxylic acid cycle for energy production. Deficiencies in urocanase activity can lead to the accumulation of urocanic acid, which has been associated with certain metabolic disorders.
Clinical Relevance[edit]
Urocanase deficiency is a rare metabolic disorder that can result in elevated levels of urocanic acid in the body. This condition, known as urocanic aciduria, may present with symptoms such as developmental delay and skin abnormalities. Diagnosis is typically made through the detection of increased urocanic acid in the urine.
Related Pages[edit]
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