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Results 1 - 5 of 5
EC Number Reaction Commentary Reference
Show all pathways known for 2.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.13L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid mechanism -, 637130, 637137
Show all pathways known for 2.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.13L-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
Show all pathways known for 2.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.13L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid reaction mechanism and kinetics, overview -, 758756
Show all pathways known for 2.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.13L-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
Show all pathways known for 2.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.13L-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
Results 1 - 5 of 5