Search results
Results from the WOW.Com Content Network
Deamination is the removal of an amino group from a molecule. [1] 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.
Deamidation reaction of Asn-Gly (top right) to Asp-Gly (at left) or iso(Asp)-Gly (in green at bottom right) Deamidation is a chemical reaction in which an amide functional group in the side chain of the amino acids asparagine or glutamine is removed or converted to another functional group.
11628 Ensembl ENSG00000111732 ENSMUSG00000040627 UniProt Q9GZX7 Q9WVE0 RefSeq (mRNA) NM_020661 NM_001330343 NM_009645 RefSeq (protein) NP_001317272 NP_065712 NP_033775 Location (UCSC) Chr 12: 8.6 – 8.61 Mb Chr 6: 122.53 – 122.54 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Activation-induced cytidine deaminase, also known as AICDA, AID and single-stranded DNA cytosine ...
Oxidative deamination is a form of deamination that generates α-keto acids and other oxidized products from amine-containing compounds, and occurs primarily in the liver. [1] Oxidative deamination is stereospecific, meaning it contains different stereoisomers as reactants and products; this process is either catalyzed by L or D- amino acid ...
Cytosine deamination commonly occurs under physiological conditions and essentially is the deamination of cytosine. This process yields uracil as its product, which is not a base pair found within DNA. This process causes extensive DNA damage.
Monoamine oxidases catalyze the oxidative deamination of monoamines. In the first part of the reaction, cofactor FAD oxidizes the substrate yielding the corresponding imine which converts the cofactor into its reduced form FADH2. The imine is then non-enzymatically hydrolyzed to the corresponding ketone (or aldehyde) and ammonia.
Adenosine deaminase (also known as adenosine aminohydrolase, or ADA) is an enzyme (EC 3.5.4.4) involved in purine metabolism.It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues.
Cytidine deaminase is an enzyme that in humans is encoded by the CDA gene. [5] [6] [7]This gene encodes an enzyme involved in pyrimidine salvaging. The encoded protein forms a homotetramer that catalyzes the irreversible hydrolytic deamination of cytidine and deoxycytidine to uridine and deoxyuridine, respectively.