Guanine deaminase
| GDA | |||||||||||||||||
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| Aliases | GDA, guanine deaminase, CYPIN, GUANASE, NEDASIN, Guanine deaminase | ||||||||||||||||
| External IDs | MGI: 95678 HomoloGene: 3171 GeneCards: GDA | ||||||||||||||||
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| Species | Human | Mouse | |||||||||||||||
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| Location (UCSC) | Chr 9: 72.11 – 72.26 Mb | Chr 19: 21.39 – 21.47 Mb | |||||||||||||||
| PubMed search | [1] | [2] | |||||||||||||||
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| 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]
xanthine. Note nitrogen replaced with oxygen. (Ignore rotation.)
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ 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)
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