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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.
Oxidative deamination is the first step to breaking down the amino acids so that they can be converted to sugars. The process begins by removing the amino group of the amino acids. The amino group becomes ammonium as it is lost and later undergoes the urea cycle to become urea, in the liver. It is then released into the blood stream, where it ...
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 ...
Ferric chloride test (detects abnormal metabolites in urine) Ninhydrin paper chromatography (detects abnormal amino acid patterns) Guthrie test (detects excessive amounts of specific amino acids in blood) The dried blood spot can be used for multianalyte testing using Tandem Mass Spectrometry (MS/MS). This given an indication for a disorder.
As suggested by the name of the family, LAAOs are flavoenzymes which function to catalyze the stereospecific oxidative deamination of an L-amino acid. [4] The three substrates of the enzymatic reaction are an L-amino acid, water, and oxygen, whereas the three products are the corresponding α-keto acid (2-oxo acid), ammonia, and hydrogen peroxide.
Indole test positive: appearance of pink layer at top (e.g. Escherichia coli) Like many biochemical tests on bacteria, results of an indole test are indicated by a change in color following a reaction with an added reagent. Pure bacterial culture must be grown in sterile tryptophan or peptone broth for 24–48 hours before performing the test.
Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or (serum) glutamic oxaloacetic transaminase (GOT, SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1) that was first described by Arthur Karmen and colleagues in 1954.
Other types of endogeneous DNA damages, given below with their frequencies of occurrence, include depurinations, depyrimidinations, double-strand breaks, O6-methylguanines, and cytosine deamination. DNA can be damaged via environmental factors as well. Environmental agents such as UV light, ionizing radiation, and genotoxic chemicals.