シッフ塩基
The mechanism of threonine ammonia-lyase is analogous to other deaminating PLP enzymes in its use of Schiff base intermediates. Initially, the amine group of threonine attacks the lysine/PLP Schiff base, displacing lysine. After deprotonation of the amino acid alpha carbon and subsequent dehydration (hence the common name threonine "dehydratase"), a new Schiff base is formed. This Schiff base is replaced by lysine attack, reforming the catalytically active PLP and releasing an initial alkene-containing product. This product tautomerizes, and after hydrolysis of the Schiff base, the final products are generated. After the final alpha-ketobutyrate product is generated, isoleucine is synthesized by progressing through the intermediates alpha-acetohydroxybutyrate to alpha-beta-dihydroxy-beta-methylvalerate, then to alpha-keto-beta-methylvalerate.