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Information on EC 2.6.1.13 - ornithine aminotransferase
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2.6.1.13 ornithine aminotransferaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 2.6.1.13
- atrophy
-
gyrate
- arginase
- retina
- choroid
- pyridoxal
- polyamines
-
chorioretinal
-
hyperornithinemia
- citrulline
- putrescine
-
transamination
- aminotransferases
- delta1-pyrroline-5-carboxylate
- 1-pyrroline-5-carboxylate
- argininosuccinate
- gabaculine
-
hyperammonemias
- carbamoylphosphate
- biotechnology
- medicine
-
plp-dependent
- analysis
- drug development
- diagnostics
- agriculture
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
ornithine aminotransferase, ornithine-delta-aminotransferase, ornithine transaminase, ornithine delta-aminotransferase, psoat, delta-oat, ornithine amino transferase, l-ornithine:2-oxoacid aminotransferase, taoat, ornithine delta-transaminase, 
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topREACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
mechanism
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L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
mechanism
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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
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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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PATHWAY SOURCE
PATHWAYS
BRENDA