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Literature summary for 2.6.1.13 extracted from

  • Stranska, J.; Kopecny, D.; Tylichova, M.; Snegaroff, J.; Sebela, M.
    Ornithine delta-aminotransferase: An enzyme implicated in salt tolerance in higher plants (2008), Plant Signal. Behav., 3, 929-935.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.13

Activating Compound

Activating Compound Comment Organism Structure
additional information in rice, cycloheximide, a protein synthesis inhibitor, has no effect on OAT activity induced by water stress Oryza sativa
additional information OAT activity increases by salt-stress treatment in Arabidopsis thaliana Arabidopsis thaliana

Application

Application Comment Organism
biotechnology genetic engineering of plants for increased production of the osmoprotectant proline, transgenic plants overexpressing OAT display enhanced tolerance to salt and drought due to increased proline content Cucurbita pepo
biotechnology genetic engineering of plants for increased production of the osmoprotectant proline, transgenic plants overexpressing OAT display enhanced tolerance to salt and drought due to increased proline content Oryza sativa
biotechnology genetic engineering of plants for increased production of the osmoprotectant proline, transgenic plants overexpressing OAT display enhanced tolerance to salt and drought due to increased proline content Nicotiana plumbaginifolia
biotechnology genetic engineering of plants for increased production of the osmoprotectant proline, transgenic plants overexpressing OAT display enhanced tolerance to salt and drought due to increased proline content Pisum sativum
biotechnology genetic engineering of plants for increased production of the osmoprotectant proline, transgenic plants overexpressing OAT display enhanced tolerance to salt and drought due to increased proline content Arabidopsis thaliana
biotechnology genetic engineering of plants for increased production of the osmoprotectant proline, transgenic plants overexpressing OAT display enhanced tolerance to salt and drought due to increased proline content Vigna aconitifolia
drug development human OAT as a potential target for development of new therapeutic drugs, OAT holds a significant scientific interest because of its association with gyrate atrophy, a recessive hereditary genetic dissorder leading to progressive loss of vision and eventually blindness in humans Homo sapiens
drug development human OAT is recognized as a potential target for chemotherapeutic drug development, in a study performed to evaluate the effect of selective blocking of mitosis in human cancer cells, OAT is identified as a protein, which binds the antimitotic drug diazonamide A and it has a role in regulating mitotic cell division Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
a recombinant seedling OAT is obtained by cDNA expression in Escherichia coli and its substrate specificity is measured, the enzyme is found to be strictly specific for L-ornithine showing practically no activity with putrescine, 1,3-diamimopropane and 4-aminobutyrate Pisum sativum
expression of the entire human gene in Escherichia coli Homo sapiens
mothbean enzyme is expressed in Escherichia coli Vigna aconitifolia
Nicotiana plumbaginifolia plants overexpressing OAT from Arabidopsis synthesize more proline than the control plants and show a higher biomass and a higher germination rate under osmotic stress conditions Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
human OAT is crystallized as a recombinant protein obtained by expression of the entire gene in Escherichia coli, the packing of the dimers in the crystal yields a hexameric quaternary structure in which 3 dimers are arranged to form about one turn of a right-handed superhelix, OAT is also crystallized in the presence of L-canaline and gabaculine, co-crystallization of OAT with (2S, 5S)-5-fluoromethylornithine Homo sapiens

Protein Variants

Protein Variants Comment Organism
Y85I mutation of Tyr85 in human OAT to Ile decreases the rate of the reaction of the enzyme with ornithine 1000fold and increases that with 4-aminobutyrate 16fold, indicating that Tyr85 is a major determinant of specificity toward ornithine Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
(2S,5S)-5-fluoromethylornithine it blocks the enzyme by a suicide reaction (mechanism-based inhibition) leading to a covalent adduct with the cofactor Homo sapiens
5-amino-1,3-cyclohexadienyl carboxylic acid gabaculine Arabidopsis thaliana
5-amino-1,3-cyclohexadienyl carboxylic acid gabaculine Cucurbita pepo
5-amino-1,3-cyclohexadienyl carboxylic acid gabaculine Homo sapiens
5-amino-1,3-cyclohexadienyl carboxylic acid gabaculine Nicotiana plumbaginifolia
5-amino-1,3-cyclohexadienyl carboxylic acid gabaculine Oryza sativa
5-amino-1,3-cyclohexadienyl carboxylic acid gabaculine Pisum sativum
5-amino-1,3-cyclohexadienyl carboxylic acid gabaculine Vigna aconitifolia

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.75
-
 2-oxoglutarate
-
 Vigna aconitifolia
2
-
 L-ornithine
-
 Vigna aconitifolia
4.7
-
 L-ornithine
-
 Cucurbita pepo
6.3
-
 2-oxoglutarate
-
 Cucurbita pepo

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-
mitochondrion
-
 Cucurbita pepo 5739
-
mitochondrion
-
 Oryza sativa 5739
-
mitochondrion
-
 Nicotiana plumbaginifolia 5739
-
mitochondrion
-
 Pisum sativum 5739
-
mitochondrion
-
 Arabidopsis thaliana 5739
-
mitochondrion
-
 Vigna aconitifolia 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 mothbean enzyme, 1 * 50000 Vigna aconitifolia

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-ornithine + 2-oxoglutarate Homo sapiens
-
 DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate Cucurbita pepo
-
 DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate Oryza sativa
-
 DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate Nicotiana plumbaginifolia
-
 DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate Pisum sativum
-
 DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate Arabidopsis thaliana
-
 DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate Vigna aconitifolia
-
 DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9FNK4
-
-
Cucurbita pepo
-
-
-
Homo sapiens
-
-
-
Nicotiana plumbaginifolia
-
-
-
Oryza sativa
-
-
-
Pisum sativum B1A0U3
-
-
Vigna aconitifolia P31893
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-ornithine + 2-oxoglutarate
-
 Homo sapiens DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate
-
 Cucurbita pepo DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate
-
 Oryza sativa DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate
-
 Nicotiana plumbaginifolia DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate
-
 Pisum sativum DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate
-
 Arabidopsis thaliana DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?
L-ornithine + 2-oxoglutarate
-
 Vigna aconitifolia DELTA1-pyrroline-5-carboxylate + L-glutamate
-
 ?

Subunits

Subunits Comment Organism
homodimer the crystal structure of the human enzyme is determined, the functional unit of the protein consists of a dimer built from 2 identical subunits, each monomer contains 12 alpha-helices and 14 beta-strands and can be structurally divided into 3 domains: a large 249 residue domain (PLP-binding domain), a small C-terminal domain of 95 residues and an N-terminal segment of 42 residues Homo sapiens
monomer mothbean enzyme, 1 * 50000 Vigna aconitifolia

Synonyms

Synonyms Comment Organism
L-ornithine:2-oxoacid aminotransferase
-
 Homo sapiens
L-ornithine:2-oxoacid aminotransferase
-
 Cucurbita pepo
L-ornithine:2-oxoacid aminotransferase
-
 Oryza sativa
L-ornithine:2-oxoacid aminotransferase
-
 Nicotiana plumbaginifolia
L-ornithine:2-oxoacid aminotransferase
-
 Pisum sativum
L-ornithine:2-oxoacid aminotransferase
-
 Arabidopsis thaliana
L-ornithine:2-oxoacid aminotransferase
-
 Vigna aconitifolia
OAT
-
 Homo sapiens
OAT
-
 Cucurbita pepo
OAT
-
 Oryza sativa
OAT
-
 Nicotiana plumbaginifolia
OAT
-
 Pisum sativum
OAT
-
 Arabidopsis thaliana
OAT
-
 Vigna aconitifolia
ornithine delta-aminotransferase
-
 Homo sapiens
ornithine delta-aminotransferase
-
 Cucurbita pepo
ornithine delta-aminotransferase
-
 Oryza sativa
ornithine delta-aminotransferase
-
 Nicotiana plumbaginifolia
ornithine delta-aminotransferase
-
 Pisum sativum
ornithine delta-aminotransferase
-
 Arabidopsis thaliana
ornithine delta-aminotransferase
-
 Vigna aconitifolia

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Cucurbita pepo
8
-
-
 Vigna aconitifolia

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Homo sapiens
pyridoxal 5'-phosphate
-
 Cucurbita pepo
pyridoxal 5'-phosphate
-
 Oryza sativa
pyridoxal 5'-phosphate
-
 Nicotiana plumbaginifolia
pyridoxal 5'-phosphate
-
 Pisum sativum
pyridoxal 5'-phosphate
-
 Arabidopsis thaliana
pyridoxal 5'-phosphate
-
 Vigna aconitifolia

General Information

General Information Comment Organism
physiological function enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate Cucurbita pepo
physiological function enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate Oryza sativa
physiological function enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate Pisum sativum
physiological function enzyme is implicated in salt tolerance in higher plants, enzyme is implicated in proline biosynthesis and accumulation via pyrroline-5-carboxylate Vigna aconitifolia
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 Arabidopsis thaliana