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Guanine deaminase (GDA)
- Target
- GDA
- Molecular classification
- Enzyme, aminohydrolase
01
Overview
Guanine deaminase (GDA) is an enzyme that catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia[2][6]. GDA is a key component in the purine degradation pathway, essential for the breakdown of purine nucleotides derived from DNA and RNA. This process helps maintain cellular nucleotide pools, prevents accumulation of toxic metabolites, and balances purine synthesis and degradation[1][6]. In the nervous system, the GDA protein (also called cypin) interacts with PSD-95 and promotes microtubule assembly in neuronal dendrites[2][3]. Dysregulation of GDA activity or purine metabolism can be associated with diseases such as gout (due to excess uric acid), hyperuricemia, certain cancers, and some skin disorders[1][3].
- Other names
- cypinguanaseguanine aminaseGAHguanine aminohydrolaseKIAA1258p51-nedasinnedasincytoplasmic PSD-95 interactor[2][3]
02
Mechanism of action
Enzyme inhibition or modulation to regulate purine metabolism or balance nucleotide pools; therapeutic targeting in purine metabolism disorders[1]
03
Biological functions
Purine nucleotide catabolismhydrolytic deamination of guanineproduction of xanthine and ammoniaregulation of intracellular nucleotide poolsmicrotubule assembly (neuronal dendrites through PSD-95 interaction)[1][2][3][6]
04
Disease associations
Gouthyperuricemiapotential roles in cancerkeratosis (seborrheic)acanthomametabolic disorders[1][3]
05
Safety considerations
Altered purine metabolism may lead to undesirable changes in uric acid or nucleotide levels (e.g., hypouricemia, hyperuricemia, disturbances in DNA/RNA synthesis)[1]
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