Guanine deaminase: Difference between revisions

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Latest revision as of 07:43, 10 January 2019

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]

File:Guanine-xanthine.png

Xanthine synthesis from guanine

References

↑ 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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[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.

[pmid20285041-2] 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.

[pmid10595517-4] 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.

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v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase
3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase
3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase
3.5.5: Nitriles/ Aminohydrolases	Nitrilase
3.5.99: Other	Riboflavinase Thiaminase II

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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Guanine deaminase: Difference between revisions

Latest revision as of 07:43, 10 January 2019

References

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