Guanine deaminase

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GDA
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases GDA, guanine deaminase, CYPIN, GUANASE, NEDASIN, Guanine deaminase
External IDs MGI: 95678 HomoloGene: 3171 GeneCards: GDA
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001242505
NM_001242506
NM_001242507
NM_004293

NM_010266

RefSeq (protein)

NP_001229434.1
NP_001229435.1
NP_001229436.1
NP_004284.1

NP_034396.1

Location (UCSC) Chr 9: 72.11 – 72.26 Mb Chr 19: 21.39 – 21.47 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Guanine deaminase also known as cypin, guanase, guanine aminase, GAH, and guanine aminohydrolase is an aminohydrolase enzyme which converts guanine to xanthine.[3][4][5] Cypin is a major cytosolic protein that interacts with PSD-95. It promotes localized microtubule assembly in neuronal dendrites.[6]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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 1078714Freely accessible. PMID 16578130. 
  4. ^ 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. 
  5. ^ 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. 
  6. ^ 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[edit]