Literature summary for 2.6.1.13 extracted from

Ginguay, A.; Cynober, L.; Curis, E.; Nicolis, I.
Ornithine aminotransferase, an important glutamate-metabolizing enzyme at the crossroads of multiple metabolic pathways (2017), Biology, 6, 18 .

Application

Application	Comment	Organism
medicine	potential utility of OAT inhibitors for the treatment of cancer	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
it is believed that there is only one gene for OAT, pseudo-genes are not transcribed or lead to non-functional proteins, DNA and amino acid sequence comparisons and phylogenetic analysis	Pisum sativum
it is believed that there is only one gene for OAT, pseudo-genes are not transcribed or lead to non-functional proteins, DNA and amino acid sequence comparisons and phylogenetic analysis	Vigna aconitifolia
it is believed that there is only one gene for OAT, pseudo-genes are not transcribed or lead to non-functional proteins, DNA and amino acid sequence comparisons and phylogenetic analysis	Geukensia demissa
it is believed that there is only one gene for OAT, pseudo-genes are not transcribed or lead to non-functional proteins, DNA and amino acid sequence comparisons and phylogenetic analysis	Mus musculus
it is believed that there is only one gene for OAT, pseudo-genes are not transcribed or lead to non-functional proteins, DNA and amino acid sequence comparisons and phylogenetic analysis	Rattus norvegicus
it is believed that there is only one gene for OAT, pseudo-genes are not transcribed or lead to non-functional proteins, DNA and amino acid sequence comparisons and phylogenetic analysis	Plasmodium falciparum
it is believed that there is only one gene for OAT, pseudo-genes are not transcribed or lead to non-functional proteins, DNA and amino acid sequence comparisons and phylogenetic analysis	Bos taurus
it is believed that there is only one gene for OAT, pseudo-genes are not transcribed or lead to non-functional proteins, DNA and amino acid sequence comparisons and phylogenetic analysis	Oryctolagus cuniculus
it is believed that there is only one gene for OAT, pseudo-genes are not transcribed or lead to non-functional proteins, DNA and amino acid sequence comparisons and phylogenetic analysis	Salmo trutta
it is believed that there is only one gene for OAT, pseudo-genes are not transcribed or lead to non-functional proteins, DNA and amino acid sequence comparisons and phylogenetic analysis, genetic organization and localization of OAT genes, overview	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure analysis	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.15	-	2-oxoglutarate	pH and temperature not specified in the publication, liver isolated mitochondria	Rattus norvegicus
0.56	2.8	L-ornithine	pH and temperature not specified in the publication, liver enzyme	Rattus norvegicus
0.59	-	L-ornithine	pH and temperature not specified in the publication, kidney enzyme	Rattus norvegicus
0.6	-	L-ornithine	pH and temperature not specified in the publication, small intestine enzyme	Rattus norvegicus
0.65	-	2-oxoglutarate	pH and temperature not specified in the publication	Plasmodium falciparum
0.72	-	2-oxoglutarate	pH and temperature not specified in the publication, liver enzyme	Mus musculus
0.73	-	2-oxoglutarate	pH and temperature not specified in the publication, liver enzyme	Rattus norvegicus
0.75	-	2-oxoglutarate	pH and temperature not specified in the publication	Vigna aconitifolia
0.8	-	L-ornithine	pH and temperature not specified in the publication, enzyme from cortical interneurons	Mus musculus
0.88	-	2-oxoglutarate	pH and temperature not specified in the publication, liver enzyme	Salmo trutta
0.91	-	2-oxoglutarate	pH and temperature not specified in the publication, kidney enzyme	Rattus norvegicus
0.95	-	2-oxoglutarate	pH and temperature not specified in the publication, small intestine enzyme	Rattus norvegicus
1.1	-	L-ornithine	pH and temperature not specified in the publication, brain enzyme	Mus musculus
1.2	4.8	L-ornithine	pH and temperature not specified in the publication, liver enzyme	Mus musculus
1.3	-	2-oxoglutarate	pH and temperature not specified in the publication, eye enzyme	Bos taurus
2	-	2-oxoglutarate	pH and temperature not specified in the publication	Pisum sativum
2	-	L-ornithine	pH and temperature not specified in the publication	Vigna aconitifolia
2.6	-	2-oxoglutarate	pH and temperature not specified in the publication, brain enzyme	Mus musculus
2.75	-	2-oxoglutarate	pH and temperature not specified in the publication, eye iris enzyme	Homo sapiens
3.7	-	L-ornithine	pH and temperature not specified in the publication, eye retina enzyme	Homo sapiens
3.95	-	L-ornithine	pH and temperature not specified in the publication	Plasmodium falciparum
4	-	L-ornithine	pH and temperature not specified in the publication, liver isolated mitochondria	Rattus norvegicus
4.3	-	L-ornithine	pH and temperature not specified in the publication, enzyme from astrocytes	Mus musculus
4.7	-	L-ornithine	pH and temperature not specified in the publication, enzyme from cerebellar granule cells	Mus musculus
5.6	-	L-ornithine	pH and temperature not specified in the publication, eye enzyme	Bos taurus
7.5	-	L-ornithine	pH and temperature not specified in the publication, liver enzyme	Salmo trutta
15	-	L-ornithine	pH and temperature not specified in the publication	Pisum sativum

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	the mitochondrial localization may control the reaction kinetics, OAT activity being apparently limited by the rate of ornithine entry into the mitochondrion	Pisum sativum	5739	-
mitochondrion	the mitochondrial localization may control the reaction kinetics, OAT activity being apparently limited by the rate of ornithine entry into the mitochondrion	Vigna aconitifolia	5739	-
mitochondrion	the mitochondrial localization may control the reaction kinetics, OAT activity being apparently limited by the rate of ornithine entry into the mitochondrion	Geukensia demissa	5739	-
mitochondrion	the mitochondrial localization may control the reaction kinetics, OAT activity being apparently limited by the rate of ornithine entry into the mitochondrion	Homo sapiens	5739	-
mitochondrion	the mitochondrial localization may control the reaction kinetics, OAT activity being apparently limited by the rate of ornithine entry into the mitochondrion	Mus musculus	5739	-
mitochondrion	the mitochondrial localization may control the reaction kinetics, OAT activity being apparently limited by the rate of ornithine entry into the mitochondrion	Rattus norvegicus	5739	-
mitochondrion	the mitochondrial localization may control the reaction kinetics, OAT activity being apparently limited by the rate of ornithine entry into the mitochondrion	Plasmodium falciparum	5739	-
mitochondrion	the mitochondrial localization may control the reaction kinetics, OAT activity being apparently limited by the rate of ornithine entry into the mitochondrion	Bos taurus	5739	-
mitochondrion	the mitochondrial localization may control the reaction kinetics, OAT activity being apparently limited by the rate of ornithine entry into the mitochondrion	Oryctolagus cuniculus	5739	-
mitochondrion	the mitochondrial localization may control the reaction kinetics, OAT activity being apparently limited by the rate of ornithine entry into the mitochondrion	Salmo trutta	5739	-
additional information	OAT is a soluble, intracellular protein	Pisum sativum	-	-
additional information	OAT is a soluble, intracellular protein	Vigna aconitifolia	-	-
additional information	OAT is a soluble, intracellular protein	Geukensia demissa	-	-
additional information	OAT is a soluble, intracellular protein	Homo sapiens	-	-
additional information	OAT is a soluble, intracellular protein	Mus musculus	-	-
additional information	OAT is a soluble, intracellular protein	Rattus norvegicus	-	-
additional information	OAT is a soluble, intracellular protein	Plasmodium falciparum	-	-
additional information	OAT is a soluble, intracellular protein	Bos taurus	-	-
additional information	OAT is a soluble, intracellular protein	Oryctolagus cuniculus	-	-
additional information	OAT is a soluble, intracellular protein	Salmo trutta	-	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
L-ornithine + 2-oxoglutarate	Pisum sativum	-	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	Vigna aconitifolia	-	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	Geukensia demissa	-	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	Homo sapiens	-	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	Mus musculus	-	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	Rattus norvegicus	-	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	Plasmodium falciparum	-	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	Bos taurus	-	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	Oryctolagus cuniculus	-	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	Salmo trutta	-	L-glutamate 5-semialdehyde + L-glutamate	-	r

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	Q3ZCF5	-	-
Geukensia demissa	-	i.e. Modiolus demissus	-
Homo sapiens	P04181	-	-
Mus musculus	P29758	-	-
Oryctolagus cuniculus	A0A5F9CII4	-	-
Pisum sativum	B1A0U3	-	-
Plasmodium falciparum	Q6LFH8	-	-
Rattus norvegicus	P04182	-	-
Salmo trutta	A0A674DA32	-	-
Vigna aconitifolia	P31893	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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	Homo sapiens	a
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	Pisum sativum	a
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	Vigna aconitifolia	a
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	Geukensia demissa	a
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	Mus musculus	a
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	Rattus norvegicus	a
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	Plasmodium falciparum	a
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	Bos taurus	a
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	Oryctolagus cuniculus	a
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	Salmo trutta	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
astrocyte	-	Mus musculus	-
brain	-	Mus musculus	-
brain	enzyme localization in the tissues of the brain, overview	Homo sapiens	-
ciliary body	-	Homo sapiens	-
ciliary body	-	Rattus norvegicus	-
ciliary body	-	Bos taurus	-
ciliary body	-	Oryctolagus cuniculus	-
erythroblast	-	Homo sapiens	-
eye	-	Mus musculus	-
eye	-	Rattus norvegicus	-
eye	-	Bos taurus	-
eye	-	Oryctolagus cuniculus	-
eye	-	Salmo trutta	-
eye	enzyme localization in the tissues of the eye, overview	Homo sapiens	-
granule cell	cerebellar	Mus musculus	-
intestine	-	Homo sapiens	-
intestine	-	Mus musculus	-
intestine	-	Rattus norvegicus	-
intestine	-	Bos taurus	-
intestine	-	Oryctolagus cuniculus	-
intestine	-	Salmo trutta	-
iris	-	Homo sapiens	-
iris	-	Rattus norvegicus	-
iris	-	Bos taurus	-
iris	-	Oryctolagus cuniculus	-
keratinocyte	-	Homo sapiens	-
kidney	-	Homo sapiens	-
kidney	-	Mus musculus	-
kidney	-	Rattus norvegicus	-
kidney	-	Bos taurus	-
kidney	-	Oryctolagus cuniculus	-
kidney	-	Salmo trutta	-
liver	-	Homo sapiens	-
liver	-	Mus musculus	-
liver	-	Rattus norvegicus	-
liver	-	Bos taurus	-
liver	-	Oryctolagus cuniculus	-
liver	-	Salmo trutta	-
melanocyte	-	Homo sapiens	-
additional information	tissue expression profile, overview	Mus musculus	-
additional information	tissue expression profile, overview	Rattus norvegicus	-
additional information	tissue expression profile, overview	Bos taurus	-
additional information	tissue expression profile, overview	Oryctolagus cuniculus	-
additional information	tissue expression profile, overview. OAT can be found in almost all tissues, but its activity predominates in the liver, kidney, intestine, and retina	Homo sapiens	-
retina	-	Homo sapiens	-
retina	-	Mus musculus	-
retina	-	Rattus norvegicus	-
retina	-	Bos taurus	-
retina	-	Oryctolagus cuniculus	-
retina	-	Salmo trutta	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.00000055	-	pH and temperature not specified in the publication, partially purified liver enzyme	Salmo trutta
0.0000183	-	pH and temperature not specified in the publication, brain enzyme	Mus musculus
0.00018	-	pH and temperature not specified in the publication, liver enzyme	Mus musculus
0.00042	-	pH and temperature not specified in the publication, liver isolated mitochondria	Rattus norvegicus
0.00187	-	pH and temperature not specified in the publication, brain enzyme	Oryctolagus cuniculus
0.00275	-	pH and temperature not specified in the publication, eye iris enzyme	Homo sapiens
0.0036	-	pH and temperature not specified in the publication, eye iris, enzyme from calf	Bos taurus
0.00363	-	pH and temperature not specified in the publication, eye enzyme	Homo sapiens
0.0038	-	pH and temperature not specified in the publication, eye iris enzyme	Oryctolagus cuniculus
0.0039	-	pH and temperature not specified in the publication, eye retina, enzyme from calf	Bos taurus
0.004	-	pH and temperature not specified in the publication, eye retina enzyme	Oryctolagus cuniculus
0.0051	-	pH and temperature not specified in the publication, eye iris enzyme	Rattus norvegicus
0.0053	-	pH and temperature not specified in the publication, liver enzyme	Oryctolagus cuniculus
0.0054	-	pH and temperature not specified in the publication, eye retina enzyme	Rattus norvegicus
0.00763	-	pH and temperature not specified in the publication, liver enzyme	Rattus norvegicus
0.00813	-	pH and temperature not specified in the publication, brain enzyme	Rattus norvegicus
0.0112	-	pH and temperature not specified in the publication, kidney enzyme	Oryctolagus cuniculus
0.0153	-	pH and temperature not specified in the publication, kidney enzyme	Rattus norvegicus
3.624	-	pH and temperature not specified in the publication	Pisum sativum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
L-ornithine + 2-oxoglutarate	-	Pisum sativum	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	-	Vigna aconitifolia	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	-	Geukensia demissa	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	-	Homo sapiens	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	-	Mus musculus	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	-	Rattus norvegicus	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	-	Plasmodium falciparum	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	-	Bos taurus	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	-	Oryctolagus cuniculus	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	-	Salmo trutta	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	the forward reaction is favoured	Pisum sativum	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	the forward reaction is favoured	Vigna aconitifolia	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	the forward reaction is favoured	Geukensia demissa	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	the forward reaction is favoured	Homo sapiens	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	the forward reaction is favoured	Mus musculus	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	the forward reaction is favoured	Rattus norvegicus	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	the forward reaction is favoured	Plasmodium falciparum	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	the forward reaction is favoured	Bos taurus	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	the forward reaction is favoured	Oryctolagus cuniculus	L-glutamate 5-semialdehyde + L-glutamate	-	r
L-ornithine + 2-oxoglutarate	the forward reaction is favoured	Salmo trutta	L-glutamate 5-semialdehyde + L-glutamate	-	r
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	Pisum sativum	?	-	-
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	Vigna aconitifolia	?	-	-
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	Geukensia demissa	?	-	-
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	Homo sapiens	?	-	-
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	Mus musculus	?	-	-
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	Rattus norvegicus	?	-	-
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	Plasmodium falciparum	?	-	-
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	Bos taurus	?	-	-
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	Oryctolagus cuniculus	?	-	-
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	Salmo trutta	?	-	-

Synonyms

Synonyms	Comment	Organism
OAT	-	Pisum sativum
OAT	-	Vigna aconitifolia
OAT	-	Geukensia demissa
OAT	-	Homo sapiens
OAT	-	Mus musculus
OAT	-	Rattus norvegicus
OAT	-	Plasmodium falciparum
OAT	-	Bos taurus
OAT	-	Oryctolagus cuniculus
OAT	-	Salmo trutta
ornithine delta-aminotransferase	-	Pisum sativum
ornithine delta-aminotransferase	-	Vigna aconitifolia
ornithine delta-aminotransferase	-	Geukensia demissa
ornithine delta-aminotransferase	-	Homo sapiens
ornithine delta-aminotransferase	-	Mus musculus
ornithine delta-aminotransferase	-	Rattus norvegicus
ornithine delta-aminotransferase	-	Plasmodium falciparum
ornithine delta-aminotransferase	-	Bos taurus
ornithine delta-aminotransferase	-	Oryctolagus cuniculus
ornithine delta-aminotransferase	-	Salmo trutta
ornithine delta-transaminase	-	Pisum sativum
ornithine delta-transaminase	-	Vigna aconitifolia
ornithine delta-transaminase	-	Geukensia demissa
ornithine delta-transaminase	-	Homo sapiens
ornithine delta-transaminase	-	Mus musculus
ornithine delta-transaminase	-	Rattus norvegicus
ornithine delta-transaminase	-	Plasmodium falciparum
ornithine delta-transaminase	-	Bos taurus
ornithine delta-transaminase	-	Oryctolagus cuniculus
ornithine delta-transaminase	-	Salmo trutta

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
additional information	-	each half-reaction has its own kinetic profile with different effects of pH: for the first one, the reaction rate is maximal in the range pH 8.0-10.0, for the second one, it peaks at pH 6.0-8.5	Rattus norvegicus
7.3	-	liver enzyme	Salmo trutta
7.5	-	liver enzyme	Mus musculus
7.6	8	enzyme from eye retina	Homo sapiens
7.8	8.15	liver enzyme	Rattus norvegicus
8	-	-	Vigna aconitifolia
8	-	kidney enzyme and enzyme from small intestine	Rattus norvegicus
8.8	-	-	Pisum sativum

Cofactor

Cofactor	Comment	Organism
pyridoxal 5'-phosphate	PLP, dependent on	Pisum sativum
pyridoxal 5'-phosphate	PLP, dependent on	Vigna aconitifolia
pyridoxal 5'-phosphate	PLP, dependent on	Geukensia demissa
pyridoxal 5'-phosphate	PLP, dependent on	Homo sapiens
pyridoxal 5'-phosphate	PLP, dependent on	Mus musculus
pyridoxal 5'-phosphate	PLP, dependent on	Rattus norvegicus
pyridoxal 5'-phosphate	PLP, dependent on	Plasmodium falciparum
pyridoxal 5'-phosphate	PLP, dependent on	Bos taurus
pyridoxal 5'-phosphate	PLP, dependent on	Oryctolagus cuniculus
pyridoxal 5'-phosphate	PLP, dependent on	Salmo trutta

General Information

General Information	Comment	Organism
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	Homo sapiens
metabolism	the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview	Pisum sativum
metabolism	the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview	Vigna aconitifolia
metabolism	the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview	Geukensia demissa
metabolism	the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview	Homo sapiens
metabolism	the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview	Mus musculus
metabolism	the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview	Rattus norvegicus
metabolism	the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview	Plasmodium falciparum
metabolism	the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview	Bos taurus
metabolism	the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview	Oryctolagus cuniculus
metabolism	the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview	Salmo trutta