2.6.1.13	L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid	mechanism	-, 637130, 637137	
2.6.1.13	L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid	mechanism of the L-ornithine transamination catalysed by ornithine aminotransferase (OAT) and reaction intermediate forms, detailed overview. Like every PLP-dependent transaminases, OAT operates via a ping-pong mechanism, in which two half-reactions complete a full transamination cycle. In the first half-transamination reaction, L-ornithine reacts with the PLP form of the enzyme (OAT-PLP) to yield L-glutamate 5-semialdehyde and the pyridoxamine 5'-phosphate form of the enzyme (OAT-PMP). In the second half transamination, 2-oxoglutarate reacts with OAT-PMP to reform OAT-PLP and L-glutamate	759181	
2.6.1.13	L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid	reaction mechanism and kinetics, overview	-, 758756	
2.6.1.13	L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid	the enzyme performs a OAT-like PLP-dependent transaminase ping-pong mechanism, two half-reactions completing a full transamination cycle. Like other transaminases, ornithine delta-aminotransferase (OAT) in the absence of substrates forms an internal aldimine with the PLP cofactor covalently bound on a lysine residue through a Schiff base. In the first half-reaction, ornithine forms an external aldimine with PLP, no longer covalently bound to the enzyme, but retained in the active site through non-covalent interactions. Enzyme OAT thus acts as an omega-transaminase in the first half-reaction, and as an alpha-transaminase in the second half-reaction: although the alpha-amino group is more reactive then the distal one, in the first half-reaction OAT transaminates the distal OAT amino group	758876	
2.6.1.13	L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid	the enzyme performs a OAT-like PLP-dependent transaminase ping-pong mechanism, two half-reactions completing a full transamination cycle. Like other transaminases, ornithine delta-aminotransferase in the absence of substrates forms an internal aldimine with the PLP cofactor covalently bound on a lysine residue through a Schiff base. In the first half-reaction, ornithine forms an external aldimine with PLP, no longer covalently bound to the enzyme, but retained in the active site through non-covalent interactions. Enzyme OAT thus acts as an omega-transaminase in the first half-reaction, and as an alpha-transaminase in the second half-reaction: although the alpha-amino group is more reactive then the distal one, in the first half-reaction OAT transaminates the distal OAT amino group	758876