Biochemistry/Biomolecules Transamination Reaction Quiz

Transamination

• Pyridoxal phosphate (PLP), derived from vitamin B6, is the coenzyme required for transamination reactions.
• In transamination, the amino group of the amino acid is first transferred to pyridoxal phosphate (PLP).
• The amino groups collected through transamination reactions are ultimately converted to urea and excreted.
• Glutamate functions as an amino group donor for further processing of amino groups following transamination.
• Pyridoxal phosphate (PLP) acts as a carrier of the amino group during transamination, forming a Schiff base intermediate with the amino acid.
• In a transamination reaction, an amino group is interchanged between an α-amino acid and an α-keto acid.
• Aminotransferases are the enzymes required for transamination reactions.
• Pyridoxal phosphate (PLP) is the coenzyme commonly accepted by most aminotransferases.
• The primary chemical change in transamination reactions is the transfer of an amino group from an amino acid to an α-keto acid.
• Transamination reactions do not lose or gain carbon atoms.
• Transamination is named as such because it involves the transfer of an amino group.

Oxidative Deamination

• The enzyme glutamate dehydrogenase catalyzes the oxidative deamination of glutamate, producing α-ketoglutarate and ammonia.
• Aspartate serves as a source of nitrogen for the urea cycle.
• The product of oxidative deamination of glutamate is α-ketoglutarate.
• Glutamate dehydrogenase is considered unusual among enzymes because it can use either NAD+ or NADP+ as a cofactor.
• Mitochondria play a significant role in oxidative deamination reactions.
• α-ketoglutarate, the product of glutamate dehydrogenase, is a key intermediate in the citric acid cycle.