deamination
Sign in to saveDeamination is the removal of an amino group from a molecule. Enzymes that catalyse this reaction are called deaminases.
Research
10,732 papers- DHX15 inhibits mouse APOBEC3 deamination.PLoS pathogens · 2025
- Generation of Genomic Alteration from Cytidine Deamination.Advances in experimental medicine and biology · 2018
- Deamination of 1-Aminoalkylphosphonic Acids: Reaction Intermediates and Selectivity.Molecules (Basel, Switzerland) · 2022
- AID and Apobec3G haphazard deamination and mutational diversity.Cellular and molecular life sciences : CMLS · 2013
- Deamination of aliphatic amines by type B monoamine oxidase and semicarbazide-sensitive amine oxidase; pharmacological implications.Journal of neural transmission. Supplementum · 1994
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Article
9 sectionsContents
- Deamination reactions in DNA
- Cytosine
- 5-methylcytosine
- Cytosine deamination increases C-To-T mutations
- Guanine
- Adenine
- Additional proteins performing this function
- See also
- References
Deamination is the removal of an amino group from a molecule. Enzymes that catalyse this reaction are called deaminases.
In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy. The amino group is removed from the amino acid and converted to ammonia. The rest of the amino acid is made up of mostly carbon and hydrogen, and is recycled or oxidized for energy. Ammonia is toxic to the human system, and enzymes convert it to urea or uric acid by addition of carbon dioxide molecules (which is not considered a deamination process) in the urea cycle, which also takes place in the liver. Urea and uric acid can safely diffuse into the blood and then be excreted in urine.