Guanine deaminase

Guanine deaminase
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols GDA ; CYPIN; GUANASE; NEDASIN
External IDs OMIM: 139260 HomoloGene: 3171 GeneCards: GDA Gene
EC number 3.5.4.3
Orthologs
Species Human Mouse
Entrez 9615 14544
Ensembl ENSG00000119125 ENSMUSG00000058624
UniProt Q9Y2T3 Q9R111
RefSeq (mRNA) NM_001242505 NM_010266
RefSeq (protein) NP_001229434 NP_034396
Location (UCSC) Chr 9:
72.11 – 72.26 Mb
Chr 19:
21.39 – 21.47 Mb
PubMed search

Guanine deaminase also known as cypin, guanase, guanine aminase, GAH, and guanine aminohydrolase is an aminohydrolase enzyme which converts guanine to xanthine.[1][2][3] Cypin is a major cytosolic protein that interacts with PSD-95. It promotes localized microtubule assembly in neuronal dendrites.[4]

References

  1. Hitchings GH, Falco EA (Oct 1944). "The Identification of Guanine in Extracts of Girella Nigricans: The Specificity of Guanase". Proceedings of the National Academy of Sciences of the United States of America 30 (10): 294–7. doi:10.1073/pnas.30.10.294. PMC 1078714. PMID 16578130.
  2. Kalckar HM (1947). "Differential spectrophotometry of purine compounds by means of specific enzymes; studies of the enzymes of purine metabolism". J. Biol. Chem. 167 (2): 461–75. PMID 20285041.
  3. Rabinowitz JC, Barker HA (Jan 1956). "Purine fermentation by Clostridium cylindrosporum. II. Purine transformations". The Journal of Biological Chemistry 218 (1): 161–73. PMID 13278325.
  4. Firestein BL, Firestein BL, Brenman JE, Aoki C, Sanchez-Perez AM, El-Husseini AE, Bredt DS (1999). "Cypin: a cytosolic regulator of PSD-95 postsynaptic targeting". Neuron 24 (3): 659–72. doi:10.1016/S0896-6273(00)81120-4. PMID 10595517.

External links

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