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 amino acid is produced from the transamination of glyoxylate?

What is the product of transamination when glutamate is the substrate?

What is the outcome of transaminating tyrosine, and what is the significance of the resulting compound?