Imidazolonepropionase

Imidazolonepropionase is an enzyme that catalyzes the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimino-L-glutamate. This enzyme plays a crucial role in the histidine degradation pathway, specifically in the fifth step. It is also known as imidazolone 5-propionate hydrolase or imidazolonepropionate hydrolase.

Structure

Imidazolonepropionase is a homodimeric enzyme, meaning it consists of two identical subunits. Each subunit is composed of a TIM barrel domain and a beta-sandwich domain. The active site of the enzyme is located in the TIM barrel domain.

Function

Imidazolonepropionase catalyzes the hydrolysis of imidazolone 5-propionate to N-formimino-L-glutamate. This reaction is part of the histidine degradation pathway, which is responsible for the breakdown of histidine to glutamate. Glutamate can then be used in various metabolic processes, including protein synthesis and energy production.

Clinical significance

Mutations in the gene encoding imidazolonepropionase can lead to histidinemia, a rare metabolic disorder characterized by elevated levels of histidine in the blood. This condition can cause a variety of symptoms, including intellectual disability, speech delay, and growth retardation.

See also

• Histidine
• Histidinemia
• Enzyme
• Hydrolysis

References

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