Everything about Transaminase totally explained
In
biochemistry, a
transaminase or an
aminotransferase is an
enzyme that
catalyzes a type of reaction between an
amino acid and an
α-keto acid. Specifically, this reaction (
transamination) involves removing the
amino group from the amino acid, leaving behind an α-keto acid, and transferring it to the reactant α-keto acid and converting it into an amino acid. The enzymes are important in the production of various amino acids, and measuring the
concentrations of various transaminases in the blood is important in the diagnosing and tracking many
diseases. Transaminases require the coenzyme
pyridoxal-phosphate, which is converted into
pyridoxamine in the first phase of the reaction, when an amino acid is converted into a keto acid. Enzyme-bound
pyridoxamine in turn reacts with
pyruvate,
oxaloacetate, or
alpha-ketoglutarate, giving
alanine,
aspartic acid, or
glutamic acid, respectively.
The presence of
elevated transaminases can be an indicator of liver damage.
Transaminases in amino acid metabolism in animals
Animals must metabolize proteins to amino acids, at the expense of muscle tissue, when blood sugar is low. The preference of liver transaminases for
oxaloacetate or
alpha-ketoglutarate plays a key role in funneling nitrogen from amino acid metabolism to Asp and Glu for conversion to urea for excretion of nitrogen. Similarly, in muscles the use of pyruvate for transamination gives Ala, which is carried by the bloodstream to the liver. Here other transaminases regenerate pyruvate, which provides a valuable precursor for gluconeogenesis. This alanine cycle is analogous to the Cori cycle which allows anaerobic metabolism by muscles.
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