DDAH1

Official Full Name

dimethylarginine dimethylaminohydrolase 1

Organism

Homo sapiens

GeneID

23576

Background

This gene belongs to the dimethylarginine dimethylaminohydrolase (DDAH) gene family. The encoded enzyme plays a role in nitric oxide generation by regulating cellular concentrations of methylarginines, which in turn inhibit nitric oxide synthase activity. [provided by RefSeq, Jul 2008]

Synonyms

DDAH; DDAHI; DDAH-1; HEL-S-16;

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Detailed Information

Dimethylarginine dimethylaminohydrolase 1 (DDAH1) is an enzyme that plays a crucial role in the metabolism of arginine, a versatile amino acid with diverse functions in various cellular processes. The DDAH1 gene encodes for the enzyme dimethylarginine dimethylaminohydrolase 1, which is primarily involved in the degradation of dimethylarginine (DMA) and other polyamine substrates. In recent years, research on the DDAH1 gene has gained significant attention due to its potential involvement in various pathological conditions, including cancer, cardiovascular diseases, and neurodegenerative disorders.

Structure of DDAH1

The DDAH1 enzyme is a member of the amidohydrolase superfamily, which consists of enzymes that catalyze the hydrolysis of various substrates, including amides, esters, and other nitrogen-containing compounds. The DDAH1 enzyme has a characteristic alpha/beta-hydrolase fold, which is a common structural feature of amidohydrolases. The active site of DDAH1 contains a His-His-Asp catalytic triad, which is responsible for the hydrolysis of substrates.

Function of DDAH1

The function of DDAH1 is to hydrolyze dimethylarginine (DMA) to generate L-arginine and dimethylamine. DMA is a natural product of protein metabolism and is also synthesized in the body through the methylation of L-arginine. The generated L-arginine serves as a precursor for various biological processes, including the synthesis of proteins, polyamines, and nitric oxide (NO). NO is a crucial signaling molecule involved in vascular relaxation, neurotransmission, and immune response. Therefore, DDAH1 plays a vital role in maintaining the appropriate levels of arginine and its metabolites, which are essential for normal cellular function.

DDAH1 in Human Diseases

Altered DDAH1 expression has been observed in various pathological conditions, including cancer, cardiovascular diseases, and neurodegenerative disorders. In cancer, DDAH1 has been reported to be overexpressed, which leads to increased production of polyamines, promoting tumor growth and survival. In cardiovascular diseases, DDAH1 is involved in the pathophysiology of atherosclerosis, where it modulates endothelial function and vascular tone. Moreover, decreased DDAH1 expression has been associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases, likely due to its role in the metabolism of polyamines and maintenance of neuronal function.

The role of DDAH1 in human health also extends to its involvement in the regulation of immune response and inflammation. The enzyme has been shown to modulate the production of cytokines and other pro-inflammatory mediators, which can impact the immune response and the development of various autoimmune diseases.

DDAH1 as a Therapeutic Target

The involvement of DDAH1 in various pathological conditions has led to its consideration as a potential therapeutic target. In cancer, targeting DDAH1 can lead to decreased polyamine production, thereby inhibiting tumor growth and survival. Similarly, in cardiovascular diseases and neurodegenerative disorders, modulating DDAH1 activity can have a significant impact on the disease progression.

Several approaches have been proposed to target DDAH1 for therapeutic purposes. These include the development of small molecules that inhibit the enzyme's activity, as well as the use of antisense oligonucleotides to decrease DDAH1 expression. Additionally, gene therapy approaches have been explored to increase DDAH1 expression in cases where its reduced expression is associated with disease pathophysiology.

References:

Xie, Ziang et al. "Mechanical force promotes dimethylarginine dimethylaminohydrolase 1-mediated hydrolysis of the metabolite asymmetric dimethylarginine to enhance bone formation." Nature communications vol. 13,1 50. 10 Jan. 2022, doi:10.1038/s41467-021-27629-2
Gao, Junling et al. "Dimethylarginine dimethylaminohydrolase 1 protects PM2.5 exposure-induced lung injury in mice by repressing inflammation and oxidative stress." Particle and fibre toxicology vol. 19,1 64. 14 Oct. 2022, doi:10.1186/s12989-022-00505-7

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