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Guanine deaminase also known as cypin, guanase, guanine aminase, GAH, and guanine aminohydrolase is an aminohydrolase enzyme which converts guanine to xanthine.[5][6][7] Cypin is a major cytosolic protein that interacts with PSD-95. It promotes localized microtubule assembly in neuronal dendrites.[8]
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Xanthine synthesis from guanine
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000119125 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000058624 - Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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
- Guanine+deaminase at the US National Library of Medicine Medical Subject Headings (MeSH)
- Overview of all the structural information available in the PDB for UniProt: Q9Y2T3 (Human Guanine deaminase) at the PDBe-KB.