Transaminases and Nitrogen Transfers

The video tutorial explains the process of transamination, where transaminase enzymes interconvert amino acids and alpha ketoacids by swapping amine and carbonyl groups. The reaction is influenced by Le Chatelier's principle due to its equilibrium constant being close to one. The tutorial also covers the role of pyridoxal phosphate as a cofactor. Practical examples of transamination reactions are provided, including oxaloacetate to aspartate, glyoxylate to glycine, and glutamate to alpha ketoglutarate. The catabolism of tyrosine is also discussed, highlighting the formation of para hydroxyphenyl pyruvate.

What is the primary function of alanine transaminase in transamination?

• To convert amino acids into sugars

• To interconvert amino acids and alpha-keto acids

• To break down proteins into amino acids

• To synthesize new proteins from amino acids

How does the equilibrium constant of transaminase reactions affect the direction of the reaction?

• It makes the reaction irreversible

• It prevents the reaction from occurring

• It allows the reaction to shift based on the concentration of reactants and products

• It causes the reaction to favor the formation of amino acids

Which cofactor is essential for transaminase activity?

• Coenzyme A

• Pyridoxal phosphate

• NADH

• Vitamin C

What is the product of transamination when oxaloacetate is used as a substrate?

• Glutamate

• Aspartate

• Alanine

• Glycine

What amino acid is formed when glyoxylate undergoes transamination?

• Serine

• Glycine

• Valine

• Leucine

What is the product of transamination of glutamate?

• Alpha-ketoglutarate

• Oxaloacetate

• Lactate

• Pyruvate

Which molecule is produced from tyrosine through transamination?

• Histidine

• Para-hydroxyphenyl pyruvate

• Tryptophan

• Phenylalanine