There were two well-established stereotypes in traditional biochemistry. First: all amino acids, both nonessential and essential, undergo reversible transamination in the human body with α-keto acids, except for lysine and threonine. In uremia, it becomes necessary to replace essential amino acids in a low-protein diet with their α-keto analogs, counting on further transamination of the latter, but the keto analogs of lysine and threonine are not used, since it is believed that these two amino acids are not transaminated. At the end of the last century, Japanese biochemists proved that, unlike lysine, threonine undergoes transamination as well as other amino acids. Second: histidine is not synthesized in the animal body, incl. in the human. But if histidine is an essential amino acid for the vast majority of mammals, then for a healthy adult, histidine is a nonessential amino acid. And only in this century, Japanese biochemists discovered an enzyme that catalyzes the last reaction in the pathway of histidine biosynthesis, and this discovery explains the indispensability/replaceability of histidine for one or another animal species, including humans, as well as a dramatic change in the status of histidine in patients with uremia, which gives good reason for the introduction of histidine into the body of people suffering from renal failure. This article presents these discoveries of Japanese biochemists and discusses the practical application of these discoveries in uremia.

Keywords: indispensability, transamination, threonine, histidine