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Target intelligence / Profile preview
O-acyl-ADP-ribose deacylase 1 (OARD1)
- Target
- OARD1
- Molecular classification
- Enzyme, Hydrolase, Macrodomain-containing protein
01
Overview
O-acyl-ADP-ribose deacylase 1 (OARD1), also known as terminal ADP-ribose protein glycohydrolase 1 and C6orf130, is an enzyme in the macrodomain family. It catalyzes the hydrolysis of O-acyl-ADP-ribose molecules (including O-acetyl-, O-propionyl-, and O-butyryl-ADP-ribose) that are generated as byproducts of NAD⁺-dependent deacylation reactions catalyzed by sirtuins[1][4][5]. OARD1 specifically removes mono-ADP-ribose attached to glutamate residues on proteins, regulating cellular levels of ADP-ribose and potentially impacting chromatin structure, gene expression, metabolic processes, and cell signaling. The enzyme contains a single macrodomain, adopting a canonical structure with a deep ligand-binding cleft, and relies on residues such as Ser-35 and Asp-125 for catalysis[4]. Mutations or dysfunction in OARD1 are linked to developmental abnormalities and may influence susceptibility to metabolic or neurological disorders. No direct drug modulators are yet documented, and the enzyme is considered a biochemically important therapeutic target for modulating ADP-ribosylation-dependent signaling[1][4].
- Other names
- ADP-ribose glycohydrolase OARD1C6orf130TARG1MGC19570dJ34B21.3Terminal ADP-ribose protein glycohydrolase 1O-acetyl-ADP-ribose deacetylase 1[Protein ADP-ribosylglutamate] hydrolase OARD1
02
Mechanism of action
Hydrolysis and removal of mono-ADP-ribosylated residues from proteins and histones; deacylation of O-acyl-ADP-ribose metabolites
03
Biological functions
Protein deacylationPost-translational modification (removal of mono-ADP-ribose from glutamate residues)NAD+-metabolite processingRegulation of signaling molecule levelsModulation of chromatin structure and gene activityReversal of protein/histone acylation
04
Disease associations
Brachydactyly, type A4Eastern equine encephalitis (associations reported)Other (potentially metabolic and epigenetic diseases due to involvement in protein/histone modification)
05
Safety considerations
No major therapeutic safety concerns documentedPotential for broad physiological impact if inhibited or deficient due to central role in protein deacylation and chromatin regulation
06
Biomarkers
None established for clinical usePotential marker for metabolic or epigenetic states is inferred from its activity in histone modification and sirtuin pathways, but this is not clinically validated
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