Aldehyde dehydrogenase 4 family, member A1

Aldehyde dehydrogenase 4 family, member A1 (ALDH4A1) is an enzyme that plays a crucial role in the metabolism of amino acids, specifically in the proline degradation pathway. This enzyme is part of the larger aldehyde dehydrogenase (ALDH) superfamily, which is involved in the oxidation of aldehydes to their corresponding carboxylic acids.

Function

ALDH4A1 is primarily responsible for the conversion of pyrroline-5-carboxylate (P5C) to glutamate in the mitochondria. This reaction is a key step in the catabolism of proline, an amino acid that can be used as a source of energy and as a precursor for the synthesis of other biomolecules. The enzyme requires NAD+ as a cofactor to facilitate the oxidation process.

Genetics

The gene encoding ALDH4A1 is located on chromosome 1 in humans. Mutations in this gene can lead to a rare metabolic disorder known as hyperprolinemia type II, which is characterized by elevated levels of proline and P5C in the blood. This condition can result in neurological symptoms, including seizures and intellectual disability.

Clinical Significance

Due to its role in proline metabolism, ALDH4A1 is of interest in the study of metabolic disorders and potential therapeutic targets. Understanding the function and regulation of this enzyme can provide insights into the treatment of conditions associated with proline metabolism.

Research

Ongoing research is focused on elucidating the structure-function relationship of ALDH4A1, understanding its regulation, and exploring its role in various physiological and pathological processes. Studies often utilize model organisms and biochemical assays to investigate the enzyme's activity and its impact on cellular metabolism.

Also see

• Aldehyde dehydrogenase
• Proline metabolism
• Hyperprolinemia
• Metabolic disorders