Aminotransferase enzyme dependent on pyridoxal phosphate

Aminotransferases dependent on pyridoxal phosphate are a large family of enzymes that catalyze the transfer of an amino group from an amino acid to a keto acid—a process known as transamination. These enzymes require pyridoxal 5'-phosphate (PLP), the active form of vitamin B6, as a coenzyme. PLP acts both as an electron sink and electrophilic catalyst during these reactions by forming a Schiff base with substrate molecules at the enzyme's active site. This enables stabilization and transformation of reaction intermediates critical for biosynthesis and degradation pathways involving most natural amino acids. The activity and specificity depend on both protein structure—especially residues involved in π–π stacking with PLP—and proper binding pocket formation[1][2]. Dysfunction or inhibition can lead to significant metabolic disturbances affecting neurological health, liver function, and overall nitrogen balance in humans[2][3].

Other names

PLP-dependent aminotransferasePyridoxal 5'-phosphate-dependent aminotransferaseTransaminase (when referring to the class of enzymes)

Drugs or compounds that inhibit these enzymes typically act by binding to the active site and preventing transamination reactions, often by mimicking substrate or cofactor structure.