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Related Concept Videos

Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
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Related Experiment Video

Updated: Jun 25, 2026

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
07:02

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

Published on: December 16, 2021

A molecular perspective on dimethylarginine dimethylaminohydrolases structure and function.

Luana Ruta1, Mirco Dindo1, Ilaria Bellezza1

  • 1Department of Medicine and Surgery, University of Perugia, P.le Severi 1, 06132 Perugia, Italy.

The Biochemical Journal
|June 24, 2026
PubMed
Summary

Dimethylarginine dimethylaminohydrolase (DDAH) enzymes regulate nitric oxide (NO) bioavailability by metabolizing endogenous NOS inhibitors. DDAH1 is a therapeutic target for diseases linked to NO dysregulation, while DDAH2 function requires further definition.

Keywords:
dimethylargininedimethylarginine dimethylaminohydrolasesendothelial dysfunctionenzyme inhibition

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Last Updated: Jun 25, 2026

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Nitric oxide (NO) is crucial for vascular tone, neurotransmission, and immunity.
  • Dysregulated NO production, influenced by NOS inhibitors like ADMA, contributes to various diseases.
  • Dimethylarginine dimethylaminohydrolase (DDAH) enzymes control NO bioavailability by metabolizing these inhibitors.

Purpose of the Study:

  • To review molecular, biochemical, and structural insights into DDAH isoforms (DDAH1 and DDAH2).
  • To discuss the potential of DDAH isoforms as pharmacological targets for diseases associated with altered NO signaling.

Main Methods:

  • Structural analysis of DDAH isoforms to understand biochemical property differences.
  • Review of existing literature on DDAH1 function and its role in disease.
  • Exploration of potential therapeutic strategies targeting DDAH enzymes.

Main Results:

  • DDAH1 actively catabolizes ADMA, and its dysregulation is linked to endothelial dysfunction and oxidative stress.
  • DDAH2 exhibits functionally divergent roles, potentially involving regulation and signaling.
  • Key amino acid substitutions in the active site differentiate the biochemical properties of DDAH1 and DDAH2.

Conclusions:

  • DDAH1 is an emerging therapeutic target for conditions involving impaired NO signaling.
  • Further research is needed to fully elucidate the function of DDAH2.
  • Targeting DDAH isoforms holds promise for treating cardiovascular, renal, and neurodegenerative diseases.