2.6.1.13: ornithine aminotransferase
This is an abbreviated version!
For detailed information about ornithine aminotransferase, go to the full flat file.
Word Map on EC 2.6.1.13
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2.6.1.13
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atrophy
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gyrate
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arginase
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retina
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choroid
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pyridoxal
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polyamines
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chorioretinal
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hyperornithinemia
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citrulline
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putrescine
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transamination
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aminotransferases
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delta1-pyrroline-5-carboxylate
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1-pyrroline-5-carboxylate
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argininosuccinate
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gabaculine
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hyperammonemias
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carbamoylphosphate
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biotechnology
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medicine
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plp-dependent
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analysis
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drug development
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diagnostics
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agriculture
- 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
Reaction
Synonyms
aminotransferase, ornithine-keto acid, delta OAT, delta-OAT, delta-ornithine aminotransferase, deltaOAT, EC 2.6.1.68, hOAT, L-ornithine 5-aminotransferase, L-ornithine aminotransferase, L-ornithine:2-oxoacid aminotransferase, L-ornithine:alpha-ketoglutarate delta-aminotransferase, OAT, Orn-AT, ornithine 5-aminotransferase, ornithine amino transferase, ornithine aminotransferase, ornithine delta aminotransferase, ornithine delta-amino transferase, ornithine delta-aminotransferase, ornithine delta-transaminase, ornithine transaminase, ornithine-2-oxoacid aminotransferase, ornithine-alpha-ketoglutarate aminotransferase, ornithine-delta-aminotransferase, ornithine-keto acid aminotransferase, ornithine-keto acid transaminase, ornithine-ketoglutarate aminotransferase, ornithine-oxo acid aminotransferase, ornithine-oxo-acid transaminase, ornithine: 2-oxo-glutarate aminotransferase, ornithine:alpha-oxoglutarate transaminase, PsOAT, RocD, TaOAT, TaOAT-5AL, TaOAT-5B, TaOAT-5BL, TaOAT-5DL, TaOAT-AL-2, TgOAT
ECTree
2.6.1.13 ornithine aminotransferaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 2.6.1.13 - ornithine aminotransferase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid
a nonselective aminotransferase inactivator
(1S,3S)-3-amino-4-(1,1,1,3,3,3-hexafluoropropan-2-ylidene)cyclopentane-1-carboxylic acid
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(2S,5S)-5-fluoromethylornithine
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it blocks the enzyme by a suicide reaction (mechanism-based inhibition) leading to a covalent adduct with the cofactor
3-Methyl-2-benzothiazolone hydrazone hydrochloride
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fully reversed by addition of pyridoxal phosphate
4-Amino-5-hexynoic acid
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synonym: AHA, irreversible, pretreatment with ornithine protects
carboxylmethoxyamine
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fully reversed by addition of pyridoxal phosphate
L-arginine
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fully reversed by addition of pyridoxal phosphate, 28% inhibition at 10 mM after 20 min
norvaline
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inhibitory action largely depends on the branched structure of the hydrophobic residue
phenylhydrazine
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fully reversed by addition of pyridoxal phosphate
pyridoxal 5'-phosphate
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in excess: partial inactivation, 70% inactivation at 0.75 and 7.5 mM/g enzyme
testosterone
ornithine aminotransferase is naturally downregulated in the presence of testosterone
2-oxoglutarate
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alpha-keto acid acceptor, inhibitor at high concentrations
2-oxoglutarate
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alpha-keto acid acceptor, inhibitor at high concentrations
5-Fluoromethylornithine
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specific irreversible inhibitor in vivo and in vitro
cadaverine
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fully reversed by addition of pyridoxal phosphate, 57% inhibition at 10 mM after 20 min
gabaculine
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synonym: 5-amino-1,3-cyclohexadienyl carboxylate, irreversible inactivation of the holo form, but not the apo form
gabaculine
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almost complete irreversible inhibition at 0.001 mM within a few hours, pretreatment with ornithine protects
L-canaline
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binds covalently to enzyme forming a canaline-pyridoxal phosphate oxime, dialysis against free pyridoxal phosphate slowly reactivates the enzyme as the oxime is replaced by pyridoxal phosphate
L-canaline
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i.e. 2-amino-4-(aminooxy)-n-butanoic acid, irreversible, forms oxime-type compound with pyridoxal 5'-phosphate
L-isoleucine
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inhibitory action largely depends on the branched structure of the hydrophobic residue
L-leucine
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inhibitory action largely depends on the branched structure of the hydrophobic residue
L-valine
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fully reversed by addition of pyridoxal phosphate, 35% inhibition at 10 mM after 20 min
L-valine
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competitive with L-ornithine; inhibitory action largely depends on the branched structure of the hydrophobic residue
putrescine
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fully reversed by addition of pyridoxal phosphate, 63% inhibition at 10 mM after 20 min
additional information
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by substrate analogs and pyridoxal phosphate inhibitors
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additional information
design, synthesis, and evaluation of a series of fluorine-substituted cyclohexene analogues, as selective hOAT inhibitors, overview. Molecular dynamics simulations and electrostatic potential charge calculations are conducted to elucidated the significant influence of the one-fluorine difference on the corresponding intermediates, leading to two totally different inactivation pathways. Binding analysis of inhibitors 8 and 9 using the structure of hOAT (PDB ID 1OAT); inactivation mechanism, detailed overview. The compound shows enhanced potency, along with excellent selectivity over other aminotransferases. Enzyme binding structure analysis
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additional information
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design, synthesis, and evaluation of a series of fluorine-substituted cyclohexene analogues, as selective hOAT inhibitors, overview. Molecular dynamics simulations and electrostatic potential charge calculations are conducted to elucidated the significant influence of the one-fluorine difference on the corresponding intermediates, leading to two totally different inactivation pathways. Binding analysis of inhibitors 8 and 9 using the structure of hOAT (PDB ID 1OAT); inactivation mechanism, detailed overview. The compound shows enhanced potency, along with excellent selectivity over other aminotransferases. Enzyme binding structure analysis
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additional information
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by substrate analogs and pyridoxal phosphate inhibitors
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