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L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
mechanism
-
L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
mechanism
-
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
L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
reaction mechanism and kinetics, overview
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
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
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
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
-
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
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
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
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
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
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
L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
reaction mechanism and kinetics, overview
-
-
L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
mechanism
-
-
L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
reaction mechanism and kinetics, overview
-
-
L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
-
-
-
-
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acetylornithine + 2-oxoglutarate
? + L-glutamate
beta-lysine + 2-oxoglutarate
glutamate + 3-amino-7-oxooctanoic acid
D-ornithine + 2-oxoglutarate
D-glutamate 5-semialdehyde + L-glutamate
D-ornithine + 2-oxoglutarate
glutamate + DELTA1-pyrroline-5-carboxylate
L-lysine + 2-oxoglutarate
glutamate + 2-amino-7-oxooctanoic acid
-
weak
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + glutamate
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
L-ornithine + 2-oxoglutarate
glutamate + DELTA1-pyrroline-5-carboxylate
L-ornithine + 2-oxoglutarate
L-glutamate + DELTA1-pyrroline-5-carboxylate
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
L-ornithine + a 2-oxo carboxylate
L-glutamate 5-semialdehyde + an L-amino acid
-
-
-
r
L-ornithine + glyoxylate
DELTA1-pyrroline-5-carboxylate + glycine
L-ornithine + pyruvate
DELTA1-pyrroline-5-carboxylate + L-alanine
N-acetylornithine + 2-oxoglutarate
glutamate + N-acetyl-glutamate-gammasemialdehyde
-
-
-
-
?
ornithine + oxaloacetate
DELTA1-pyrroline-5-carboxylate + L-aspartate
additional information
?
-
acetylornithine + 2-oxoglutarate
? + L-glutamate
-
-
-
r
acetylornithine + 2-oxoglutarate
? + L-glutamate
-
-
-
r
acetylornithine + 2-oxoglutarate
? + L-glutamate
-
-
-
r
beta-lysine + 2-oxoglutarate
glutamate + 3-amino-7-oxooctanoic acid
-
weak
-
-
?
beta-lysine + 2-oxoglutarate
glutamate + 3-amino-7-oxooctanoic acid
-
weak
-
-
?
D-ornithine + 2-oxoglutarate
D-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
D-ornithine + 2-oxoglutarate
D-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
D-ornithine + 2-oxoglutarate
D-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
D-ornithine + 2-oxoglutarate
glutamate + DELTA1-pyrroline-5-carboxylate
-
6% the rate of L-ornithine
-
-
?
D-ornithine + 2-oxoglutarate
glutamate + DELTA1-pyrroline-5-carboxylate
-
6% the rate of L-ornithine
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + glutamate
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + glutamate
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
r
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
glutamate-gamma semialdehyde spontaneously cyclizes to form DELTA1-pyrroline-5-carboxylate
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
glutamate-gamma semialdehyde spontaneously cyclizes to form DELTA1-pyrroline-5-carboxylate
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
Erwinia aroidea
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
glutamate-gamma semialdehyde spontaneously cyclizes to form DELTA1-pyrroline-5-carboxylate
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
urea cycle
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
glutamate-gamma semialdehyde spontaneously cyclizes to form DELTA1-pyrroline-5-carboxylate
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
glutamate-gamma semialdehyde spontaneously cyclizes to form DELTA1-pyrroline-5-carboxylate
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
DL-pyrroline-5-carboxylate
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
glutamate-gamma semialdehyde spontaneously cyclizes to form DELTA1-pyrroline-5-carboxylate
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
ornithine pathway
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
glutamate-gamma semialdehyde spontaneously cyclizes to form DELTA1-pyrroline-5-carboxylate
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
glutamate-gamma semialdehyde spontaneously cyclizes to form DELTA1-pyrroline-5-carboxylate
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
glutamate-gamma semialdehyde spontaneously cyclizes to form DELTA1-pyrroline-5-carboxylate
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
DL-pyrroline-5-carboxylate
r
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
D-ornithine is not accepted as substrate
equilibrium constant: 71
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
exchanges the pro-S hydrogen on the delta-carbon atom of ornithine exclusively, also transfers the alpha amino group of glutamate, kinetics of the half reactions between the enzyme and both amino acids
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
metabolism of proline to ornithine
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
glutamate + DELTA1-pyrroline-5-carboxylate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
glutamate + DELTA1-pyrroline-5-carboxylate
-
-
-
-
?
L-ornithine + 2-oxoglutarate
L-glutamate + DELTA1-pyrroline-5-carboxylate
-
-
-
?
L-ornithine + 2-oxoglutarate
L-glutamate + DELTA1-pyrroline-5-carboxylate
-
-
-
?
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
the forward reaction is favoured
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
the forward reaction is favoured
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
the forward reaction is favoured
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
the forward reaction is favoured
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
the forward reaction is favoured
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
the forward reaction is favoured
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
the forward reaction is favoured
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
the forward reaction is favoured
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
the forward reaction is favoured
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
the forward reaction is favoured
-
-
r
L-ornithine + glyoxylate
DELTA1-pyrroline-5-carboxylate + glycine
-
weak
-
-
?
L-ornithine + glyoxylate
DELTA1-pyrroline-5-carboxylate + glycine
-
weak
-
-
?
L-ornithine + glyoxylate
DELTA1-pyrroline-5-carboxylate + glycine
-
-
-
-
?
L-ornithine + glyoxylate
DELTA1-pyrroline-5-carboxylate + glycine
-
weak
-
-
?
L-ornithine + glyoxylate
DELTA1-pyrroline-5-carboxylate + glycine
-
-
-
-
?
L-ornithine + pyruvate
DELTA1-pyrroline-5-carboxylate + L-alanine
-
-
-
-
?
L-ornithine + pyruvate
DELTA1-pyrroline-5-carboxylate + L-alanine
-
-
-
-
?
L-ornithine + pyruvate
DELTA1-pyrroline-5-carboxylate + L-alanine
-
-
-
-
?
L-ornithine + pyruvate
DELTA1-pyrroline-5-carboxylate + L-alanine
-
weak
-
-
?
L-ornithine + pyruvate
DELTA1-pyrroline-5-carboxylate + L-alanine
-
-
-
-
?
L-ornithine + pyruvate
DELTA1-pyrroline-5-carboxylate + L-alanine
-
considerably less effective than 2-oxoglutarate
-
-
?
ornithine + oxaloacetate
DELTA1-pyrroline-5-carboxylate + L-aspartate
-
-
-
-
?
ornithine + oxaloacetate
DELTA1-pyrroline-5-carboxylate + L-aspartate
-
weak
-
-
?
ornithine + oxaloacetate
DELTA1-pyrroline-5-carboxylate + L-aspartate
-
weak
-
-
?
ornithine + oxaloacetate
DELTA1-pyrroline-5-carboxylate + L-aspartate
-
-
-
-
?
ornithine + oxaloacetate
DELTA1-pyrroline-5-carboxylate + L-aspartate
-
weak
-
-
?
ornithine + oxaloacetate
DELTA1-pyrroline-5-carboxylate + L-aspartate
-
-
-
-
?
additional information
?
-
-
ornithine aminotransferase feeds pyrroline-5-carboxylate exclusively into the catabolic branch of proline metabolism, which yields glutamate as an end product. Proline biosynthesis occurs predominantly or exclusively via the glutamate pathway in Arabidopsis thaliana and does not depend on glutamate produced by arginine and ornithine catabolism
-
-
?
additional information
?
-
-
inactive as amino group donor: L-lysine
-
-
?
additional information
?
-
-
inactive as amino group donor: 4-aminobutanoate
-
-
?
additional information
?
-
-
specific for ornithine
-
-
?
additional information
?
-
-
inactive as amino group donor: L-arginine
-
-
?
additional information
?
-
-
inactive as amino group donor: putrescine
-
-
?
additional information
?
-
-
inactive as amino group donor: D-ornithine
-
-
?
additional information
?
-
spontaneous cyclization of glutamate 5-semialdehyde (GSA) to form (S)-DELTA1-pyrroline-5-carboxylate (P5C), the aldehyde can spontaneously react to give a hydrated form of GSA, making the reaction almost irreversible in vitro
-
-
-
additional information
?
-
-
specific for 2-oxoglutarate
-
-
?
additional information
?
-
-
spontaneous cyclization of glutamate 5-semialdehyde (GSA) to form (S)-DELTA1-pyrroline-5-carboxylate (P5C), the aldehyde can spontaneously react to give a hydrated form of GSA, making the reaction almost irreversible in vitro
-
-
-
additional information
?
-
glutamic-gamma-semialdehyde (GSA) product of this reaction undergoes spontaneous cyclization forming DELTA1-pyrroline-5-carboxylate (P5C). NMR analysis of P5C and of 1-pyrroline-2-carboxylate (P2C), generated by alpha-transamination of L-ornithine. Substrate molecular docking study and interaction analysis, NMR analysis, overview
-
-
-
additional information
?
-
spontaneous cyclization of glutamate 5-semialdehyde (GSA) to form (S)-DELTA1-pyrroline-5-carboxylate (P5C), the aldehyde can spontaneously react to give a hydrated form of GSA, making the reaction almost irreversible in vitro
-
-
-
additional information
?
-
-
specific for 2-oxoglutarate
-
-
?
additional information
?
-
-
inactive as amino group donor: L-leucine
-
-
?
additional information
?
-
-
inactive as amino group donor: L-lysine
-
-
?
additional information
?
-
-
inactive as amino group acceptor: 2-oxoisohexanoate
-
-
?
additional information
?
-
-
inactive as amino group acceptor: 2-oxoisopentanoate
-
-
?
additional information
?
-
-
inactive as amino group donor: butylamine
-
-
?
additional information
?
-
-
inactive as amino group donor: L-alanine
-
-
?
additional information
?
-
-
inactive as amino group donor: L-2-aminobutanoate
-
-
?
additional information
?
-
-
inactive as amino group donor: taurine
-
-
?
additional information
?
-
-
specific for ornithine
-
-
?
additional information
?
-
-
inactive as amino group donor: L-aspartate
-
-
?
additional information
?
-
-
inactive as amino group donor: L-citrulline
-
-
?
additional information
?
-
-
inactive as amino group donor: L-arginine
-
-
?
additional information
?
-
-
inactive as amino group acceptor: 3-phenylpyruvate
-
-
?
additional information
?
-
-
inactive as amino group donor: putrescine
-
-
?
additional information
?
-
-
inactive as amino group donor: glycine
-
-
?
additional information
?
-
-
inactive as amino group acceptor: 2-oxobutanoate
-
-
?
additional information
?
-
-
inactive as amino group donor: L-valine
-
-
?
additional information
?
-
-
inactive as amino group donor: beta-alanine
-
-
?
additional information
?
-
-
inactive as amino group donor: D-ornithine
-
-
?
additional information
?
-
-
inactive as amino group donor: cadaverine
-
-
?
additional information
?
-
-
inactive as amino group acceptor: 2-oxopentanoate
-
-
?
additional information
?
-
-
inactive as amino group acceptor: 2-oxohexanoate
-
-
?
additional information
?
-
-
inactive as amino group donor: D-lysine
-
-
?
additional information
?
-
-
specific for 2-oxoglutarate
-
-
?
additional information
?
-
-
specific for ornithine
-
-
?
additional information
?
-
spontaneous cyclization of glutamate 5-semialdehyde (GSA) to form (S)-DELTA1-pyrroline-5-carboxylate (P5C), the aldehyde can spontaneously react to give a hydrated form of GSA, making the reaction almost irreversible in vitro
-
-
-
additional information
?
-
spontaneous cyclization of glutamate 5-semialdehyde (GSA) to form (S)-DELTA1-pyrroline-5-carboxylate (P5C), the aldehyde can spontaneously react to give a hydrated form of GSA, making the reaction almost irreversible in vitro
-
-
-
additional information
?
-
spontaneous cyclization of glutamate 5-semialdehyde (GSA) to form (S)-DELTA1-pyrroline-5-carboxylate (P5C), the aldehyde can spontaneously react to give a hydrated form of GSA, making the reaction almost irreversible in vitro
-
-
-
additional information
?
-
spontaneous cyclization of glutamate 5-semialdehyde (GSA) to form (S)-DELTA1-pyrroline-5-carboxylate (P5C), the aldehyde can spontaneously react to give a hydrated form of GSA, making the reaction almost irreversible in vitro
-
-
-
additional information
?
-
-
inactive as amino group acceptor: 2-oxoisohexanoate
-
-
?
additional information
?
-
-
inactive as amino group acceptor: 2-oxoisopentanoate
-
-
?
additional information
?
-
-
inactive as amino group acceptor: oxaloacetate
-
-
?
additional information
?
-
-
specific for ornithine
-
-
?
additional information
?
-
-
inactive as amino group acceptor: 2-oxobutanoate
-
-
?
additional information
?
-
-
inactive as amino group acceptor: 2-oxopentanoate
-
-
?
additional information
?
-
-
inactive as amino group acceptor: 2-oxohexanoate
-
-
?
additional information
?
-
spontaneous cyclization of glutamate 5-semialdehyde (GSA) to form (S)-DELTA1-pyrroline-5-carboxylate (P5C), the aldehyde can spontaneously react to give a hydrated form of GSA, making the reaction almost irreversible in vitro
-
-
-
additional information
?
-
spontaneous cyclization of glutamate 5-semialdehyde (GSA) to form (S)-DELTA1-pyrroline-5-carboxylate (P5C), the aldehyde can spontaneously react to give a hydrated form of GSA, making the reaction almost irreversible in vitro
-
-
-
additional information
?
-
the enzyme from Toxoplasma gondii does not show a specific ornithine aminotransferase activity like its human homologue, but exhibits both N-acetylornithine and gamma-aminobutyric acid (GABA) transaminase activity (EC 2.6.1.19) in vitro, suggesting a role in both arginine and GABA metabolism in vivo
-
-
-
additional information
?
-
-
the enzyme from Toxoplasma gondii does not show a specific ornithine aminotransferase activity like its human homologue, but exhibits both N-acetylornithine and gamma-aminobutyric acid (GABA) transaminase activity (EC 2.6.1.19) in vitro, suggesting a role in both arginine and GABA metabolism in vivo
-
-
-
additional information
?
-
the external aldimine hydrolysis is rate-limiting, and not its formation. The enzyme TgOAT also shows lyase activity with beta-chloro-L-alanine (BCA) performin g a beta-elimination reaction
-
-
-
additional information
?
-
-
the external aldimine hydrolysis is rate-limiting, and not its formation. The enzyme TgOAT also shows lyase activity with beta-chloro-L-alanine (BCA) performin g a beta-elimination reaction
-
-
-
additional information
?
-
the enzyme from Toxoplasma gondii does not show a specific ornithine aminotransferase activity like its human homologue, but exhibits both N-acetylornithine and gamma-aminobutyric acid (GABA) transaminase activity (EC 2.6.1.19) in vitro, suggesting a role in both arginine and GABA metabolism in vivo
-
-
-
additional information
?
-
the external aldimine hydrolysis is rate-limiting, and not its formation. The enzyme TgOAT also shows lyase activity with beta-chloro-L-alanine (BCA) performin g a beta-elimination reaction
-
-
-
additional information
?
-
the enzyme from Toxoplasma gondii does not show a specific ornithine aminotransferase activity like its human homologue, but exhibits both N-acetylornithine and gamma-aminobutyric acid (GABA) transaminase activity (EC 2.6.1.19) in vitro, suggesting a role in both arginine and GABA metabolism in vivo
-
-
-
additional information
?
-
the external aldimine hydrolysis is rate-limiting, and not its formation. The enzyme TgOAT also shows lyase activity with beta-chloro-L-alanine (BCA) performin g a beta-elimination reaction
-
-
-
additional information
?
-
spontaneous cyclization of glutamate 5-semialdehyde (GSA) to form (S)-DELTA1-pyrroline-5-carboxylate (P5C), the aldehyde can spontaneously react to give a hydrated form of GSA, making the reaction almost irreversible in vitro
-
-
-
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0.056 - 43.4
2-oxoglutarate
7.4 - 496
acetylornithine
4.2
D-ornithine
pH 8.0, 37°C, recombinant wild-type enzyme
1.4
DL-pyrroline-5-carboxylate
-
-
6.7
glyoxylate
-
pH 7.1, 37°C
1.53
N-acetylornithine
-
pH 7.4, 37°C
22
pyruvate
-
pH 7.1, 37°C
additional information
additional information
-
0.056
2-oxoglutarate
pH 8.0, 37°C, recombinant mutant V79Y
0.15
2-oxoglutarate
pH and temperature not specified in the publication, liver isolated mitochondria
0.191
2-oxoglutarate
-
gut, pH 7.5
0.23
2-oxoglutarate
-
kidney, pH 7.5
0.235
2-oxoglutarate
-
liver, pH 7.5
0.25
2-oxoglutarate
-
kidney, pH 7.5
0.28
2-oxoglutarate
-
pH 7.1, 37°C
0.3
2-oxoglutarate
wild-type with PfTrx, pH 7.4, 37°C
0.31
2-oxoglutarate
pH 8.0, 37°C, recombinant wild-type enzyme
0.337
2-oxoglutarate
-
AH 130 cells, pH 7.5
0.56
2-oxoglutarate
-
pH 7.4, 37°C
0.65
2-oxoglutarate
pH and temperature not specified in the publication
0.67
2-oxoglutarate
-
rhinopharyngeal tumor, pH 7.5
0.7
2-oxoglutarate
-
pH 7.8, 37°C
0.7
2-oxoglutarate
wild-type with PfGrx, pH 7.4, 37°C
0.72
2-oxoglutarate
pH and temperature not specified in the publication, liver enzyme
0.73
2-oxoglutarate
pH and temperature not specified in the publication, liver enzyme
0.75
2-oxoglutarate
25°C, pH 8.0
0.75
2-oxoglutarate
pH and temperature not specified in the publication
0.88
2-oxoglutarate
pH and temperature not specified in the publication, liver enzyme
0.9
2-oxoglutarate
wild-type, pH 7.4, 37°C
0.91
2-oxoglutarate
pH and temperature not specified in the publication, kidney enzyme
0.95
2-oxoglutarate
pH and temperature not specified in the publication, small intestine enzyme
1.1
2-oxoglutarate
-
pH 8, 37°C
1.136
2-oxoglutarate
-
well differentiated gastroadenocarcinoma, pH 7.5
1.2
2-oxoglutarate
wild-type (OAT in parasite cell extract), pH 7.4, 37°C
1.3
2-oxoglutarate
pH and temperature not specified in the publication, eye enzyme
2
2-oxoglutarate
pH and temperature not specified in the publication
2.17
2-oxoglutarate
-
wild-type, pH 7.5, 37°C
2.4
2-oxoglutarate
-
poorly differentiated gastroadenocarcinoma, pH 7.5
2.4
2-oxoglutarate
pH 8.0, 25°C, recombinant mutant R217A, 60 nM enzyme
2.6
2-oxoglutarate
pH and temperature not specified in the publication, brain enzyme
2.69
2-oxoglutarate
-
transgenic mouse, pH 7.5, 37°C
2.7
2-oxoglutarate
-
pH 8, 37°C
2.75
2-oxoglutarate
pH and temperature not specified in the publication, eye iris enzyme
3
2-oxoglutarate
-
pH 7.8, 37°C
3.2
2-oxoglutarate
-
pH 8, 37°C
3.6
2-oxoglutarate
-
pH 8, 37°C
3.9
2-oxoglutarate
recombinant wild-type enzyme, pH 8.0, 25°C
3.9
2-oxoglutarate
pH 8.0, 25°C, recombinant wild-type enzyme, 60 nM enzyme
4
2-oxoglutarate
pH 8.0, 15°C, recombinant wild-ype enzyme, 0.001 mM enzyme
4.4
2-oxoglutarate
pH 8.0, 15°C, recombinant mutant R217A, 0.001 mM enzyme
4.6
2-oxoglutarate
-
pH 8.5, 37°C
6.1
2-oxoglutarate
-
37°C
6.2
2-oxoglutarate
-
pH 7.6, 37°C
11.3
2-oxoglutarate
recombinant mutant R180T enzyme, pH 8.0, 25°C
7.4
acetylornithine
pH 8.0, 37°C, recombinant wild-type enzyme
496
acetylornithine
pH 8.0, 37°C, recombinant mutant V79Y
0.56 - 2.8
L-ornithine
pH and temperature not specified in the publication, liver enzyme
0.59
L-ornithine
pH and temperature not specified in the publication, kidney enzyme
0.6
L-ornithine
pH and temperature not specified in the publication, small intestine enzyme
0.8
L-ornithine
pH and temperature not specified in the publication, enzyme from cortical interneurons
0.9
L-ornithine
wild-type with PfTrx, pH 7.4, 37°C
1.1
L-ornithine
-
pH 8, 37°C
1.1
L-ornithine
pH and temperature not specified in the publication, brain enzyme
1.113
L-ornithine
-
gut, pH 7.5
1.2 - 4.8
L-ornithine
pH and temperature not specified in the publication, liver enzyme
1.282
L-ornithine
-
well differentiated gastroadenocarcinoma, pH 7.5
1.4
L-ornithine
-
kidney, pH 7.5
1.4
L-ornithine
-
liver, pH 7.5
1.5
L-ornithine
wild-type with PfGrx, pH 7.4, 37°C
1.6
L-ornithine
wild-type, pH 7.4, 37°C
1.7
L-ornithine
-
rhinopharyngeal tumor, pH 7.5
1.8
L-ornithine
-
pH 8.5, 37°C
1.8
L-ornithine
-
pH 8, 37°C
2
L-ornithine
-
AH 130 cells, pH 7.5
2
L-ornithine
25°C, pH 8.0
2
L-ornithine
pH and temperature not specified in the publication
2 - 37
L-ornithine
recombinant mutant R180Tenzyme, pH 8.0, 25°C
2.089
L-ornithine
-
in rat brain mitochondrial fraction, in absence of pyridoxal 5'-phosphate
2.3
L-ornithine
-
pH 8, 37°C
2.3
L-ornithine
wild-type (OAT in parasite cell extract), pH 7.4, 37°C
2.7
L-ornithine
-
pH 7.8, 37°C
2.9
L-ornithine
-
pH 8, 37°C
3.275
L-ornithine
-
poorly differentiated gastroadenocarcinoma, pH 7.5
3.3
L-ornithine
-
kidney, pH 7.5
3.7
L-ornithine
pH and temperature not specified in the publication, eye retina enzyme
3.95
L-ornithine
-
pH 7.4, 37°C
3.95
L-ornithine
pH and temperature not specified in the publication
4
L-ornithine
pH and temperature not specified in the publication, liver isolated mitochondria
4.3
L-ornithine
pH and temperature not specified in the publication, enzyme from astrocytes
4.7
L-ornithine
pH and temperature not specified in the publication, enzyme from cerebellar granule cells
4.8
L-ornithine
-
pH 7.8, 37°C
5.089
L-ornithine
-
in rat brain mitochondrial fraction, in presence of 0.05 mM pyridoxal 5'-phosphate
5.1
L-ornithine
pH 8.0, 25°C, recombinant mutant R217A, 60 nM enzyme
5.6
L-ornithine
pH and temperature not specified in the publication, eye enzyme
6.2
L-ornithine
-
pH 7.6, 37°C
6.5
L-ornithine
recombinant wild-type enzyme, pH 8.0, 25°C
6.5
L-ornithine
pH 8.0, 25°C, recombinant wild-type enzyme, 60 nM enzyme
6.9
L-ornithine
pH 8.0, 37°C, recombinant wild-type enzyme
6.9
L-ornithine
pH 8.0, 15°C, recombinant mutant R217A, 0.001 mM enzyme
7
L-ornithine
pH 8.0, 15°C, recombinant wild-type enzyme, 0.001 mM enzyme
7.5
L-ornithine
pH and temperature not specified in the publication, liver enzyme
8.97
L-ornithine
assay based on detection of L-glutamate, pH 8.0, 37°C
10.5
L-ornithine
assay based on reduction of DELTA1-pyrroline-5-carboxylate, pH 8.0, 37°C
13.94
L-ornithine
-
wild-type, pH 7.5, 37°C
15
L-ornithine
-
pH 8.0, 37°C
15
L-ornithine
pH and temperature not specified in the publication
15.32
L-ornithine
-
transgenic mouse, pH 7.5, 37°C
87
L-ornithine
-
salt stress conditions
91
L-ornithine
-
normal conditions
1.7
ornithine
-
with pyruvate as cosubstrate, pH 7.1, 37°C
2.8
ornithine
-
with 2-oxoglutarate as cosubstrate, pH 7.1, 37°C
2.9
ornithine
-
with glyoxylate as cosubstrate, pH 7.1, 37°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
aggregation results in increase of Km
-
additional information
additional information
-
Km for ornithine increases below pH 7.5, Km for 2-oxoglutarate decreases below pH 7
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
no Michaelis-Menten kinetics are obtained, possibly a positive cooperative behavior with kinetic values S0.5 of 0.8mM for 2-oxoglutarate and S0.5 of 6.3 mM for ornithine
-
additional information
additional information
-
no Michaelis-Menten kinetics are obtained, possibly a positive cooperative behavior with kinetic values S0.5 of 0.8mM for 2-oxoglutarate and S0.5 of 6.3 mM for ornithine
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics
-
additional information
additional information
steady-state and pre-steady state Michaelis-Menten kinetics, rapid-scanning stopped-flow kinetics, and transamination half-reaction kinetic parameters, overview
-
additional information
additional information
-
steady-state and pre-steady state Michaelis-Menten kinetics, rapid-scanning stopped-flow kinetics, and transamination half-reaction kinetic parameters, overview
-
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evolution
ornithine aminotransferase is a highly conserved enzyme present in all prokaryotes and eukaryotes, from unicellular bacteria to multicellular animals and plants. In Triticum aestivum, three homeologous OAT genes in wheat genome are found on chromosome group 5, named as TaOAT-5AL, TaOAT-5BL, and TaOAT-5DL. The phylogenetic tree indicates that OATs share highly conserved domains between monocotyledons and eudicotyledons
evolution
ornithine aminotransferase is a highly conserved enzyme present in all prokaryotes and eukaryotes, from unicellular bacteria to multicellular animals and plants. In Triticum aestivum, three homeologous OAT genes in wheat genome are found on chromosome group 5, named as TaOAT-5AL, TaOAT-5BL, and TaOAT-5DL. Two transcript variants of TaOAT-5AL are revealed, named TaOAT-5AL-1 and TaOAT-5AL-2 and characterized by 1497 bp and 1287 bp in cDNA length, respectively. Compared to TaOAT-5AL-2, TaOAT-5AL-1 contains an additional 120-bp insertion encompassing an in-frame stop codon, which resulted in a premature protein. The additional insertion is genotypically confirmed by sequencing results from six cultivars. The phylogenetic tree indicates that OATs share highly conserved domains between monocotyledons and eudicotyledons
malfunction
-
deltaOAT and proline dehydrogenases (ProDH1 and ProDH2) are involved in the defence against non-host pathogens. Mutants for these genes compromise non-host resistance and show a decrease in non-host pathogen-induced reactive oxygen species
malfunction
-
deltaOAT and proline dehydrogenases (ProDH1 and ProDH2) are involved in the defence against non-host pathogens. Silencing of these genes in Nicotina benthamiana delays occurrence of hypersensitive response and favours non-host pathogen growth
malfunction
-
the influence of OAT activity in a model of septic shock induced by intraperitoneal injection of lipopolysaccharide in wild-type and transgenic mice overexpressing OAT in the liver, kidney and intestine is analysed. OAT overexpression has only limited metabolic consequences, most probably because of compensatory mechanisms ensuring amino acid homeostasis. OAT overexpression brings a metabolic advantage in the response to stress. Results show an inhibition of OAT activity and expression in the liver following LPS treatment
malfunction
a deficit in ornithine aminotransferase (OAT) is associated with gyrate atrophy, a rare autosomal recessive disorder causing progressive blindness and chorioretinal degeneration
malfunction
mutation of Val79 to Tyr results in a change of substrate preference between GABA, N-acetylornithine and L-ornithine, suggesting a key role of Val79 in defining substrate specificity
malfunction
overexpression of OAT promotes the growth and metastasis of A-549 lung cancer cells, and overexpression of OAT also promotes the epithelial-mesenchymal transition (EMT) of OAT-overexpressing A549 cells. Knockdown of OAT inhibits the proliferation and metastasis of H-1299 cells
malfunction
selective inhibition of hOAT has been shown to effectively suppress hepatocellular carcinoma (HCC) tumor growth in vivo
malfunction
the R180T variant of delta-ornithine aminotransferase is associated with gyrate atrophy. Ornithine delta-aminotransferase deficiency is responsible for gyrate atrophy (GA), an autosomal recessive disorder causing a progressive degeneration of the choroid and retina epithelium leading to blindness in young adults
malfunction
toxic effect of elevated intraocular concentrations of ornithine and its metabolites in excess, such as spermine, on the retinal pigment epithelial cells, together with Pro deficiency in the choroid and retina
malfunction
transgenic plants overexpressing TaOAT show enhanced tolerance to drought stress by increasing proline accumulation. In addition, salt tolerance of the transgenic plants is also enhanced
malfunction
transgenic plants overexpressing TaOAT show enhanced tolerance to drought stress by increasing proline accumulation. In addition, salt tolerance of the transgenic plants is also enhanced. The TaOAT-5AL-1 gene transcript variant contains in-frame stop codon that causes the incomplete translation of protein
malfunction
-
mutation of Val79 to Tyr results in a change of substrate preference between GABA, N-acetylornithine and L-ornithine, suggesting a key role of Val79 in defining substrate specificity
-
malfunction
-
mutation of Val79 to Tyr results in a change of substrate preference between GABA, N-acetylornithine and L-ornithine, suggesting a key role of Val79 in defining substrate specificity
-
metabolism
-
catalyzes step 5 in the ornithine fermentation pathway
metabolism
-
OAT plays a different role in arginine, ornithine and proline metabolism depending on the tissue and their physiological needs
metabolism
-
the expression of the genes involved in the arginine operon (argCJBDFGH) for the control of the L-ornithine biosynthesis pathway that is regulated through the binding of ArgR to the so-called ARG operator sites preceding those relevant target genes
metabolism
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
-
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
the PLP-dependent enzyme is involved in the interconversion of ornithine and glutamyl-5-semialdehyde (GSA)
metabolism
-
the expression of the genes involved in the arginine operon (argCJBDFGH) for the control of the L-ornithine biosynthesis pathway that is regulated through the binding of ArgR to the so-called ARG operator sites preceding those relevant target genes
-
physiological function
-
enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate
physiological function
-
enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate
physiological function
enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate
physiological function
enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate
physiological function
enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate, OAT is essential for nitrogen recycling from arginine but not for the stress-induced proline accumulation, OAT probably links the degradation pathways for arginine and proline
physiological function
-
deltaOAT is involved in effector-triggered immunity (ETI) and plays a critical role in inducing early oxidative burst and other defence pathways in plants, conceivably by accumulating P5C in mitochondria
physiological function
-
deltaOAT is involved in effector-triggered immunity (ETI) and plays a critical role in inducing early oxidative burst and other defence pathways in plants, conceivably by accumulating P5C in mitochondria
physiological function
-
increased OAT activity and ornithine concentration can impact the supply of substrates for proline synthesis
physiological function
-
in the presence of arginine, Mycobacterium tuberculosis upregulates a gene cluster which includes ornithine aminotransferase (rocD) and Rv2323c, a gene of up to now unknown function. In Mycobacterium tuberculosis, arginine is not only used as nitrogen source but also as carbon source for the formation of amino acids, in particular of proline. RocD is naturally deleted in Mycobacterium tuberculosis, but not in non-tuberculous mycobacteria. Mycobacterium tuberculosis lacking gene Rv2323c shows a growth defect on arginine, does not produce proline from arginine, and incorporates less nitrogen derived from arginine in its core nitrogen metabolism
physiological function
ornithine-delta-aminotransferase OAT is essential for Xenopus embryonic development, and overexpression of OAT produces a ventralized phenotype characterized by a small head, lack of axial structure, and defective expression of neural developmental markers. Substitution of both Arg 180 and Leu 402 abrogates both OAT enzymatic activity and ability to modulate the developmental phenotype. Neurogenesis is inhibited by OAT during Xenopus embryonic development
physiological function
human ornithine aminotransferase (hOAT), a pyridoxal 5'-phosphate-dependent enzyme, plays a critical role in the progression of hepatocellular carcinoma (HCC) and in the metabolic reprograming of HCC via proline and glutamine metabolic pathways
physiological function
ornithine aminotransferase (OAT) promotes the proliferation, invasion, and migration, inhibits the apoptosis, and alters cell cycle of non-small cell lung cancer cells (NSCLC cells). Also the involvement of OAT-miR-21-glycogen synthase kinase-3beta signaling in the functional role of OAT in NSCLC is revealed. Glycogen synthase kinase-3beta (GSK-3beta) is a direct target of miR-21 in NSCLC
physiological function
ornithine delta-aminotransferase (OAT) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the delta-transamination of L-ornithine and 2-oxoglutarate to glutamic-gamma-semialdehyde (GSA) and L-glutamate in the mitochondrial matrix. GSA then spontaneously cyclizes forming pirroline-5-carboxylate (P5C), a proline precursor
physiological function
-
the Corynebacterium glutamicum ornithine acetyltransferase (OATase) ArgJ strongly influences the production of L-ornithine by OAT in Corynebacterium glutamicum
physiological function
the enzyme from Toxoplasma gondii does not show a specific ornithine aminotransferase activity like its human homologue, but exhibits both N-acetylornithine and ?-aminobutyric acid (GABA) transaminase activity in vitro, suggesting a role in both arginine and GABA metabolism in vivo
physiological function
the enzyme plays a role in proline biosynthesis through interactions with genes, such as delta 1-pyrroline-5-carboxylate synthetase (P5CS) and pyrroline-5-carboxylate reductase (P5CR), involved in the proline metabolic pathway, protein-protein interactions analysis, overview. Promoter analysis exposes the presence of several stress responsive elements, implying their involvement in stress regulation. Potential role of TaOAT genes during floret development. TaOATs genes are involved in proline synthesis and nitrogen remobilization because they interact with genes related to proline biosynthesis enzymes and arginine catabolism. The high expression observed in the stamen and low expression observed at the anthesis stage suggest that TaOATs are likely to be involved in anther dehiscence
physiological function
-
the enzyme from Toxoplasma gondii does not show a specific ornithine aminotransferase activity like its human homologue, but exhibits both N-acetylornithine and ?-aminobutyric acid (GABA) transaminase activity in vitro, suggesting a role in both arginine and GABA metabolism in vivo
-
physiological function
-
the Corynebacterium glutamicum ornithine acetyltransferase (OATase) ArgJ strongly influences the production of L-ornithine by OAT in Corynebacterium glutamicum
-
physiological function
-
in the presence of arginine, Mycobacterium tuberculosis upregulates a gene cluster which includes ornithine aminotransferase (rocD) and Rv2323c, a gene of up to now unknown function. In Mycobacterium tuberculosis, arginine is not only used as nitrogen source but also as carbon source for the formation of amino acids, in particular of proline. RocD is naturally deleted in Mycobacterium tuberculosis, but not in non-tuberculous mycobacteria. Mycobacterium tuberculosis lacking gene Rv2323c shows a growth defect on arginine, does not produce proline from arginine, and incorporates less nitrogen derived from arginine in its core nitrogen metabolism
-
physiological function
-
the enzyme from Toxoplasma gondii does not show a specific ornithine aminotransferase activity like its human homologue, but exhibits both N-acetylornithine and ?-aminobutyric acid (GABA) transaminase activity in vitro, suggesting a role in both arginine and GABA metabolism in vivo
-
additional information
the presence of Val79 in the active site of TgOAT in place of Tyr, as in its human counterpart, provides the necessary room to accommodate N-acetylornithine and GABA, resembling the active site arrangement of GABA transaminases. Contribution of active site Val79 to the specificity of the TgOAT enzym. The crystal structure of TgOAT in its internal aldimine form (PDB ID 4ZLV) is used to generate a structrue model of the V79Y mutant enzyme form, molecular modelling
additional information
-
the presence of Val79 in the active site of TgOAT in place of Tyr, as in its human counterpart, provides the necessary room to accommodate N-acetylornithine and GABA, resembling the active site arrangement of GABA transaminases. Contribution of active site Val79 to the specificity of the TgOAT enzym. The crystal structure of TgOAT in its internal aldimine form (PDB ID 4ZLV) is used to generate a structrue model of the V79Y mutant enzyme form, molecular modelling
additional information
-
the presence of Val79 in the active site of TgOAT in place of Tyr, as in its human counterpart, provides the necessary room to accommodate N-acetylornithine and GABA, resembling the active site arrangement of GABA transaminases. Contribution of active site Val79 to the specificity of the TgOAT enzym. The crystal structure of TgOAT in its internal aldimine form (PDB ID 4ZLV) is used to generate a structrue model of the V79Y mutant enzyme form, molecular modelling
-
additional information
-
the presence of Val79 in the active site of TgOAT in place of Tyr, as in its human counterpart, provides the necessary room to accommodate N-acetylornithine and GABA, resembling the active site arrangement of GABA transaminases. Contribution of active site Val79 to the specificity of the TgOAT enzym. The crystal structure of TgOAT in its internal aldimine form (PDB ID 4ZLV) is used to generate a structrue model of the V79Y mutant enzyme form, molecular modelling
-
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26
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19
674-681
2008
Homo sapiens
brenda
Wagemaker, M.J.; Eastwood, D.C.; Welagen, J.; van der Drift, C.; Jetten, M.S.; Burton, K.; Van Griensven, L.J.; Op den Camp, H.J.
The role of ornithine aminotransferase in fruiting body formation of the mushroom Agaricus bisporus
Mycol. Res.
111
909-918
2007
Agaricus bisporus (Q2Z0F8), Agaricus bisporus
brenda
Canas, R.A.; Villalobos, D.P.; Diaz-Moreno, S.M.; Canovas, F.M.; Canton, F.R.
Molecular and functional analyses support a role of Ornithine-delta-aminotransferase in the provision of glutamate for glutamine biosynthesis during pine germination
Plant Physiol.
148
77-88
2008
Pinus sylvestris (Q1RPP3), Pinus sylvestris
brenda
Ravikumar, H.; Devaraju, K.; Shetty, K.
Effect of pH on spectral characteristics of P5C-ninhydrin derivative: Application in the assay of ornithine amino transferase activity from tissue lysate
Indian J. Clin. Biochem.
23
117-122
2008
Homo sapiens
brenda
Ravi Kumar, H.; Ananda, S.; Devaraju, K.; Prakash, B.; Sampath Kumar, S.; Suresh Babu, S.; Ramachandraswamy, N.; Puttaraju, H.
A sensitive assay for ornithine amino transferase in rat brain mitochondria by ninhydrin method
Indian J. Clin. Biochem.
24
275-279
2009
Rattus norvegicus
brenda
Fonknechten, N.; Perret, A.; Perchat, N.; Tricot, S.; Lechaplais, C.; Vallenet, D.; Vergne, C.; Zaparucha, A.; Le Paslier, D.; Weissenbach, J.; Salanoubat, M.
A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine
J. Bacteriol.
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3162-3167
2009
Acetoanaerobium sticklandii
brenda
Stranska, J.; Kopecny, D.; Tylichova, M.; Snegaroff, J.; Sebela, M.
Ornithine delta-aminotransferase: An enzyme implicated in salt tolerance in higher plants
Plant Signal. Behav.
3
929-935
2008
Cucurbita pepo, Homo sapiens, Nicotiana plumbaginifolia, Oryza sativa, Pisum sativum (B1A0U3), Vigna aconitifolia (P31893), Arabidopsis thaliana (Q9FNK4)
brenda
Ventura, G.; Moinard, C.; Segaud, F.; Le Plenier, S.; Cynober, L.; De Bandt, J.P.
Adaptative response of nitrogen metabolism in early endotoxemia: role of ornithine aminotransferase
Amino Acids
39
1417-1426
2010
Homo sapiens
brenda
Stranska, J.; Tylichova, M.; Kopecny, D.; Snegaroff, J.; Sebela, M.
Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines
Biochimie
92
940-948
2010
Pisum sativum
brenda
Jortzik, E.; Fritz-Wolf, K.; Sturm, N.; Hipp, M.; Rahlfs, S.; Becker, K.
Redox regulation of Plasmodium falciparum ornithine delta-aminotransferase
J. Mol. Biol.
402
445-459
2010
Plasmodium falciparum (Q6LFH8)
brenda
da Rocha, I.M.; Vitorello, V.A.; Silva, J.S.; Ferreira-Silva, S.L.; Viegas, R.A.; Silva, E.N.; Silveira, J.A.
Exogenous ornithine is an effective precursor and the ?-ornithine amino transferase pathway contributes to proline accumulation under high N recycling in salt-stressed cashew leaves
J. Plant Physiol.
169
41-49
2012
Anacardium occidentale
brenda
Senthil-Kumar, M.; Mysore, K.S.
Ornithine-delta-aminotransferase and proline dehydrogenase genes play a role in non-host disease resistance by regulating pyrroline-5-carboxylate metabolism-induced hypersensitive response
Plant Cell Environ.
35
1329-1343
2012
Arabidopsis thaliana, Nicotiana benthamiana
brenda
Juncosa, J.I.; Lee, H.; Silverman, R.B.
Two continuous coupled assays for ornithine-delta-aminotransferase
Anal. Biochem.
440
145-149
2013
Homo sapiens (P04181)
brenda
da Silva, R.; Levillain, O.; Brosnan, J.T.; Araneda, S.; Brosnan, M.E.
The effect of portacaval anastomosis on the expression of glutamine synthetase and ornithine aminotransferase in perivenous hepatocytes
Can. J. Physiol. Pharmacol.
91
362-368
2013
Rattus norvegicus (P04182)
brenda
Peng, Y.; Cooper, S.K.; Li, Y.; Mei, J.M.; Qiu, S.; Borchert, G.L.; Donald, S.P.; Kung, H.F.; Phang, J.M.
Ornithine-delta-aminotransferase inhibits neurogenesis during Xenopus embryonic development
Invest. Ophthalmol. Vis. Sci.
56
2486-2497
2015
Xenopus laevis (Q98TS5)
brenda
Hampel, A.; Huber, C.; Geffers, R.; Spona-Friedl, M.; Eisenreich, W.; Bange, F.C.
Mycobacterium tuberculosis is a natural ornithine aminotransferase (rocD) mutant and depends on Rv2323c for growth on arginine
PLoS ONE
10
e0136914
2015
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Hao, N.; Mu, J.; Hu, N.; Xu, S.; Shen, P.; Yan, M.; Li, Y.; Xu, L.
Implication of ornithine acetyltransferase activity on L-ornithine production in Corynebacterium glutamicum
Biotechnol. Appl. Biochem.
63
15-21
2016
Corynebacterium glutamicum, Corynebacterium glutamicum 1006
brenda
Astegno, A.; Maresi, E.; Bertoldi, M.; La Verde, V.; Paiardini, A.; Dominici, P.
Unique substrate specificity of ornithine aminotransferase from Toxoplasma gondii
Biochem. J.
474
939-955
2017
Toxoplasma gondii (S8EY38), Toxoplasma gondii, Toxoplasma gondii ATCC 50611 (S8EY38), Toxoplasma gondii ME49 (S8EY38)
brenda
Ginguay, A.; Cynober, L.; Curis, E.; Nicolis, I.
Ornithine aminotransferase, an important glutamate-metabolizing enzyme at the crossroads of multiple metabolic pathways
Biology
6
18
2017
Bos taurus (Q3ZCF5), Geukensia demissa, Homo sapiens (P04181), Mus musculus (P29758), Oryctolagus cuniculus (A0A5F9CII4), Pisum sativum (B1A0U3), Plasmodium falciparum (Q6LFH8), Rattus norvegicus (P04182), Salmo trutta (A0A674DA32), Vigna aconitifolia (P31893)
brenda
Anwar, A.; She, M.; Wang, K.; Ye, X.
Cloning and molecular characterization of Triticum aestivum ornithine amino transferase (TaOAT) encoding genes
BMC Plant Biol.
20
187
2020
Triticum aestivum (A0A3B6KM96), Triticum aestivum (A0A3B6LSQ4), Triticum aestivum (A0A3B6MXE9), Triticum aestivum
brenda
Montioli, R.; Paiardini, A.; Giardina, G.; Zanzoni, S.; Cutruzzola, F.; Cellini, B.; Borri Voltattorni, C.
R180T variant of delta-ornithine aminotransferase associated with gyrate atrophy biochemical, computational, X-ray and NMR studies provide insight into its catalytic features
FEBS J.
286
2787-2798
2019
Homo sapiens (P04181)
brenda
Zhu, W.; Doubleday, P.F.; Catlin, D.S.; Weerawarna, P.M.; Butrin, A.; Shen, S.; Wawrzak, Z.; Kelleher, N.L.; Liu, D.; Silverman, R.B.
A remarkable difference that one fluorine atom confers on the mechanisms of inactivation of human ornithine aminotransferase by two cyclohexene analogues of gamma-aminobutyric Acid
J. Am. Chem. Soc.
142
4892-4903
2020
Homo sapiens (P04181), Homo sapiens
brenda
Liu, Y.; Wu, L.; Li, K.; Liu, F.; Wang, L.; Zhang, D.; Zhou, J.; Ma, X.; Wang, S.; Yang, S.
Ornithine aminotransferase promoted the proliferation and metastasis of non-small cell lung cancer via upregulation of miR-21
J. Cell. Physiol.
234
12828-12838
2019
Homo sapiens (P04181), Homo sapiens
brenda
Montioli, R.; Zamparelli, C.; Borri Voltattorni, C.; Cellini, B.
Oligomeric state and thermal stability of apo- and holo-human ornithine delta-aminotransferase
Protein J.
36
174-185
2017
Homo sapiens (P04181), Homo sapiens
brenda