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Information on EC 2.6.1.13 - ornithine aminotransferase and Organism(s) Rattus norvegicus and UniProt Accession P04182

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.13 ornithine aminotransferase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Rattus norvegicus
UNIPROT: P04182
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
ornithine aminotransferase, ornithine-delta-aminotransferase, ornithine transaminase, ornithine delta-aminotransferase, psoat, delta-oat, ornithine amino transferase, l-ornithine:2-oxoacid aminotransferase, ornithine delta-transaminase, taoat, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ornithine delta-aminotransferase
-
ornithine delta-transaminase
-
aminotransferase, ornithine-keto acid
-
-
-
-
L-ornithine 5-aminotransferase
-
-
-
-
L-ornithine aminotransferase
-
-
-
-
L-ornithine:alpha-ketoglutarate delta-aminotransferase
-
-
-
-
ornithine 5-aminotransferase
-
-
-
-
ornithine aminotransferase
ornithine delta-transaminase
-
-
-
-
ornithine transaminase
-
-
-
-
ornithine-2-oxoacid aminotransferase
-
-
-
-
ornithine-alpha-ketoglutarate aminotransferase
-
-
-
-
ornithine-keto acid aminotransferase
-
-
-
-
ornithine-keto acid transaminase
-
-
-
-
ornithine-ketoglutarate aminotransferase
-
-
-
-
ornithine-oxo acid aminotransferase
-
-
-
-
ornithine-oxo-acid transaminase
-
-
-
-
ornithine:alpha-oxoglutarate transaminase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-ornithine + a 2-oxo carboxylate = L-glutamate 5-semialdehyde + an L-amino acid
show the reaction diagram
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-ornithine:2-oxo-acid aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-42-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
show the reaction diagram
L-ornithine + glyoxylate
DELTA1-pyrroline-5-carboxylate + glycine
show the reaction diagram
-
-
-
-
?
L-ornithine + pyruvate
DELTA1-pyrroline-5-carboxylate + L-alanine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
-
-
-
r
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
PLP, dependent on
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-aminooxyacetic acid
-
almost complete inhibition at 0.2 mM
2-oxobutanoate
-
-
2-oxoglutarate
-
alpha-keto acid acceptor, inhibitor at high concentrations
2-Oxohexanoate
-
-
2-oxoisopentanoate
-
-
4-aminobutanoate
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5-Aminopentanoate
5-Fluoromethylornithine
Butanoate
-
-
Butyrate
-
27% inhibition at 25 mM
cadaverine
-
-
caproate
-
34% inhibition at 25 mM
DL-norvaline
glyoxylate
-
alpha-keto acid acceptor, inhibitor at high concentrations
hexanoate
-
-
hydroxylamine
-
reversible, noncompetitive
iodoacetamide
-
-
Isocaproate
-
41% inhibition at 25 mM
Isohexanoate
-
-
Isopentanoate
-
-
Isovalerate
-
41% inhibition at 25 mM
L-canaline
L-canavanine
L-isoleucine
L-leucine
L-valine
N2-Acetyl-L-ornithine
-
competitive with L-ornithine
norvaline
-
inhibitory action largely depends on the branched structure of the hydrophobic residue
ornithine
-
at high concentrations
p-chloromercuribenzoate
-
-
putrescine
-
-
pyridoxal 5'-phosphate
-
in excess: partial inactivation, 70% inactivation at 0.75 and 7.5 mM/g enzyme
pyruvate
-
alpha-keto acid acceptor, inhibitor at high concentrations
valerate
-
38% inhibition at 25 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 0.95
2-oxoglutarate
0.56 - 4
L-ornithine
0.191 - 3
2-oxoglutarate
1.4
DL-pyrroline-5-carboxylate
-
-
6.7
glyoxylate
-
pH 7.1, 37°C
25
L-glutamate
-
-
1.1 - 5.089
L-ornithine
1.7 - 2.9
ornithine
22
pyruvate
-
pH 7.1, 37°C
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017
5-Aminopentanoate
-
pH 8, 37°C
0.07
5-Fluoromethylornithine
-
37°C, pH 8
0.00043
hydroxylamine
-
pH 8, 37°C
2 - 20
L-valine
0.0088
N2-L-acetyl ornithine
-
pH 8, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00042
pH and temperature not specified in the publication, liver isolated mitochondria
0.0051
pH and temperature not specified in the publication, eye iris enzyme
0.0054
pH and temperature not specified in the publication, eye retina enzyme
0.00763
pH and temperature not specified in the publication, liver enzyme
0.00813
pH and temperature not specified in the publication, brain enzyme
0.0153
pH and temperature not specified in the publication, kidney enzyme
0.0052
-
muscle tissue, 35 mM L-ornithine, 5 mM 2-oxoglutarate and cofactor 0.05 mM pyridoxal 5'-phosphate in 50 mM Tris-HCl (pH-8.0)
0.0168
-
heart tissue, 35 mM L-ornithine, 5 mM 2-oxoglutarate and cofactor 0.05 mM pyridoxal 5'-phosphate in 50 mM Tris-HCl (pH-8.0)
0.02
-
brain tissue, 35 mM L-ornithine, 5 mM 2-oxoglutarate and cofactor 0.05 mM pyridoxal 5'-phosphate in 50 mM Tris-HCl (pH-8.0)
0.0225
-
spleen tissue, 35 mM L-ornithine, 5 mM 2-oxoglutarate and cofactor 0.05 mM pyridoxal 5'-phosphate in 50 mM Tris-HCl (pH-8.0)
0.0284
-
lung tissue, 35 mM L-ornithine, 5 mM 2-oxoglutarate and cofactor 0.05 mM pyridoxal 5'-phosphate in 50 mM Tris-HCl (pH-8.0)
0.0483
-
small intestine tissue, 35 mM L-ornithine, 5 mM 2-oxoglutarate and cofactor 0.05 mM pyridoxal 5'-phosphate in 50 mM Tris-HCl (pH-8.0)
0.0721
-
kidney tissue, 35 mM L-ornithine, 5 mM 2-oxoglutarate and cofactor 0.05 mM pyridoxal 5'-phosphate in 50 mM Tris-HCl (pH-8.0)
0.1156
-
liver tissue, 35 mM L-ornithine, 5 mM 2-oxoglutarate and cofactor 0.05 mM pyridoxal 5'-phosphate in 50 mM Tris-HCl (pH-8.0)
0.184
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8 - 8.15
liver enzyme
8
kidney enzyme and enzyme from small intestine
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
OAT is a soluble, intracellular protein
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the ornithine delta-transaminase, OAT, stands at the crossroads of several metabolic pathways. The role of enzyme OAT in ornithine fluxes, overview
metabolism
-
OAT plays a different role in arginine, ornithine and proline metabolism depending on the tissue and their physiological needs
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OAT_RAT
439
0
48333
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
132000
-
equilibrium ultracentrifugation
161000
-
equilibrium sedimentation analysis
256000
-
equilibrium sedimentation
33000
-
4 * 33000, empirical weight determined from the values for the thiol and half-cystine content
43000
-
4 * 43000, SDS-PAGE
45000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
6 * 45000, SDS-PAGE and equilibrium sedimentation in presence of 6 M guanidine-HCl
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8
-
equally stable at pH 6.8 and pH 8.0
637123
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66
-
pH 7.5, 15 min, 85% loss of activity, 60 min, 96% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity of the purified enzyme is preserved by addition of pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, pH 6-8, 0.01 M potassium phosphate buffer, about 20% loss of activity after 4 months
-
-15°C, rat liver homogenate in sucrose or phosphate solution, stable for some weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
in rats, a liver portacaval shunt causes a marked decrease in glutamine synthetase activity and an increase in ornithine aminotransferase activity. The glutamine synthetase and ornithine aminotransferase proteins maintain their location in the perivenous cells, indicating that there is no generalized loss of perivenous hepatocytes, but rather, there is a significant alteration in the expression of these proteins and hence metabolism in this cell population
diagnostics
-
the standardization of the enzyme kinetics can be extended to detect enzyme activity in patients of gyrate atrophy of choroid and retina with hyperornithinemia by studying the OAT activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Strecker, H.J.
Purification and properties of rat liver ornithine DELTA-transaminase
J. Biol. Chem.
240
1225-1230
1965
Rattus norvegicus
Manually annotated by BRENDA team
Peraino, C.; Bunville, L.G.; Tahmisian, T.N.
Chemical, physical, and morphological properties of ornithine aminotransferase from rat liver
J. Biol. Chem.
244
2241-2249
1969
Rattus norvegicus
Manually annotated by BRENDA team
Peraino, C.
Functional properties of ornithine-ketoacid aminotransferase from rat liver
Biochim. Biophys. Acta
289
117-127
1972
Rattus norvegicus
Manually annotated by BRENDA team
Daune, G.; Gerhart, F.; Seiler, N.
5-Fluoromethylornithine, an irreversible and specific inhibitor of L-ornithine:2-oxo-acid aminotransferase
Biochem. J.
253
481-488
1988
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Matsuzawa, T.
Characteristics of the inhibition of ornithine-delta-aminotransferase by branched-chain amino acids
J. Biochem.
75
601-609
1974
Rattus norvegicus
Manually annotated by BRENDA team
Marcovic-Housley, Z.; Kania, M.; Lustig, A.; Vincent, M.G.; Jansonius, J.N.; John, R.A.
Quaternary structure of ornithine aminotransferase in solution and preliminary crystallographic data
Eur. J. Biochem.
162
345-350
1987
Rattus norvegicus
Manually annotated by BRENDA team
Boernke, W.E.; Stevens, F.J.; Peraino, C.
Effects of self-association of ornithine aminotransferase on its physicochemical characteristics
Biochemistry
20
115-121
1981
Rattus norvegicus
Manually annotated by BRENDA team
Matsuzawa, T.; Sugimoto, N.; Sobue, M.; Ishiguro, I.
Ornithine oxoacid aminotransferase found in AH 130 ascites hepatoma cells
Biochim. Biophys. Acta
714
356-360
1982
Homo sapiens, Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Williams, J.A.; Bridge, G.; Fowler, L.J.; John, R.A.
The reaction of ornithine aminotransferase with ornithine
Biochem. J.
201
221-225
1982
Rattus norvegicus
Manually annotated by BRENDA team
Ohura, T.; Kominami, E.; Tada, K.; Katunuma, N.
Crystallization and properties of human liver ornithine aminotransferase
J. Biochem.
92
1785-1792
1982
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kalita, C.; Kerman, J.D.; Strecker, H.J.
Preparation and properties of ornithine-oxo-acid aminotransferase of rat kidney. Comparison with the liver enzyme
Biochim. Biophys. Acta
429
780-797
1976
Rattus norvegicus
Manually annotated by BRENDA team
Burcham, J.M.; Giometti, C.S.; Tollaksen, S.L.; Peraino, C.
Comparison of rat and mouse ornithine aminotransferase with respect to molecular properties and regulation of synthesis
Arch. Biochem. Biophys.
262
501-507
1988
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Kito, K.; Sanada, Y.; Katunuma, N.
Mode of inhibition of ornithine aminotransferase by L-canaline
J. Biochem.
83
201-206
1978
Rattus norvegicus
Manually annotated by BRENDA team
Cooper, A.J.L.
Glutamate-ornithine transaminases
Methods Enzymol.
113
76-79
1985
Neurospora crassa, Rattus norvegicus
Manually annotated by BRENDA team
Roschinger, W.; Endres, W.; Shin, Y.S.
Characteristics of L-ornithine: 2-oxoacid aminotransferase and potential prenatal diagnosis of gyrate atrophy of the choroid and retina by first trimester chorionic villus sampling
Clin. Chim. Acta
296
91-100
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Seiler, N.
Ornithine aminotransferase, a potential target for the treatment of hyperammonemias
Curr. Drug Targets
1
119-153
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Levillain, O.; Hus-Citharel, A.; Garvi, S.; Peyrol, S.; Reymond, I.; Mutin, M.; Morel, F.
Ornithine metabolism in male and female rat kidney: mitochondrial expression of ornithine aminotransferase and arginase II
Am. J. Physiol. Renal. Physiol.
286
F727-738
2004
Rattus norvegicus (P04182)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Geukensia demissa, Oryctolagus cuniculus (A0A5F9CII4), Salmo trutta (A0A674DA32), Pisum sativum (B1A0U3), Homo sapiens (P04181), Rattus norvegicus (P04182), Mus musculus (P29758), Vigna aconitifolia (P31893), Bos taurus (Q3ZCF5), Plasmodium falciparum (Q6LFH8)
Manually annotated by BRENDA team