Information on EC 2.6.1.13 - ornithine aminotransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.6.1.13
-
RECOMMENDED NAME
GeneOntology No.
ornithine aminotransferase
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-arginine degradation I (arginase pathway)
-
-
L-arginine degradation VI (arginase 2 pathway)
-
-
L-citrulline biosynthesis
-
-
L-Ndelta-acetylornithine biosynthesis
-
-
L-ornithine biosynthesis II
-
-
L-ornithine degradation II (Stickland reaction)
-
-
L-proline biosynthesis II (from arginine)
-
-
L-proline biosynthesis III
-
-
Metabolic pathways
-
-
proline metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-ornithine:2-oxo-acid aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-42-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
hookworm parasite
-
-
Manually annotated by BRENDA team
YM-2
-
-
Manually annotated by BRENDA team
YM-2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gramicidin S-producing
-
-
Manually annotated by BRENDA team
Erwinia aroidea
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
tobacco hornworm
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
radish
-
-
Manually annotated by BRENDA team
Wistar
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-lysine + 2-oxoglutarate
glutamate + 3-amino-7-oxooctanoic acid
show the reaction diagram
D-ornithine + 2-oxoglutarate
glutamate + DELTA1-pyrroline-5-carboxylate
show the reaction diagram
L-lysine + 2-oxoglutarate
glutamate + 2-amino-7-oxooctanoic acid
show the reaction diagram
-
weak
-
-
?
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + glutamate
show the reaction diagram
L-ornithine + 2-oxoglutarate
DELTA1-pyrroline-5-carboxylate + L-glutamate
show the reaction diagram
L-ornithine + 2-oxoglutarate
glutamate + DELTA1-pyrroline-5-carboxylate
show the reaction diagram
L-ornithine + 2-oxoglutarate
L-glutamate + DELTA1-pyrroline-5-carboxylate
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
N-acetylornithine + 2-oxoglutarate
glutamate + N-acetyl-glutamate-gammasemialdehyde
show the reaction diagram
-
-
-
-
?
ornithine + oxaloacetate
DELTA1-pyrroline-5-carboxylate + L-aspartate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
DELTA1-pyrroline-5-carboxylate + L-glutamate
show the reaction diagram
additional information
?
-
-
ornithine aminotransferase feeds pyrroline-5-carboxylate exclusively into the catabolic branch of proline metabolism, which yields glutamate as an end product. Proline biosynthesis occurs predominantly or exclusively via the glutamate pathway in Arabidopsis thaliana and does not depend on glutamate produced by arginine and ornithine catabolism
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S,5S)-5-fluoromethylornithine
-
it blocks the enzyme by a suicide reaction (mechanism-based inhibition) leading to a covalent adduct with the cofactor
1,3-Diaminopropane
-
-
2-aminooxyacetic acid
2-oxobutanoate
-
-
2-oxoglutarate
2-Oxohexanoate
-
-
2-oxoisopentanoate
-
-
3-Methyl-2-benzothiazolone hydrazone hydrochloride
-
fully reversed by addition of pyridoxal phosphate
4-Amino-5-hexynoic acid
-
synonym: AHA, irreversible, pretreatment with ornithine protects
4-aminobutanoate
-
-
4-Aminohex-5-ynoic acid
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5-amino-1,3-cyclohexadienyl carboxylic acid
5-Aminopentanoate
5-Fluoromethylornithine
beta-Lysine
-
80% inhibition at 10 mM after 20 min
Butanoate
-
-
Butyrate
-
27% inhibition at 25 mM
cadaverine
caproate
-
34% inhibition at 25 mM
carboxylmethoxyamine
-
fully reversed by addition of pyridoxal phosphate
diethylenetriamine
-
-
DL-norvaline
gabaculine
glyoxylate
hexanoate
-
-
hydroxylamine
iodoacetamide
-
-
Isocaproate
-
41% inhibition at 25 mM
Isohexanoate
-
-
isoleucine
-
-
Isonicotinylhydrazide
-
-
Isopentanoate
-
-
Isovalerate
-
41% inhibition at 25 mM
L-arginine
-
fully reversed by addition of pyridoxal phosphate, 28% inhibition at 10 mM after 20 min
L-canaline
L-canavanine
L-Cycloserine
-
fully reversed by addition of pyridoxal phosphate
L-isoleucine
L-leucine
L-lysine
-
35% inhibition at 10 mM after 20 min
L-norvaline
-
-
L-ornithine
-
slight inhibition above 40 mM
L-serine
-
-
L-valine
N-ethylmaleimide
-
complete inactivation at 0.1 and 1 mM after 20 min
N2-Acetyl-L-ornithine
-
competitive with L-ornithine
norspermidine
-
-
norvaline
-
inhibitory action largely depends on the branched structure of the hydrophobic residue
ornithine
oxaloacetate
-
-
p-chloromercuribenzoate
-
-
p-Chloromercuriphenylsulfonic acid
-
-
phenylhydrazine
-
fully reversed by addition of pyridoxal phosphate
putrescine
pyridoxal 5'-phosphate
-
in excess: partial inactivation, 70% inactivation at 0.75 and 7.5 mM/g enzyme
pyruvate
spermidine
-
-
spermine
-
-
testosterone
ornithine aminotransferase is naturally downregulated in the presence of testosterone
triethylenetetramine
-
-
valerate
-
38% inhibition at 25 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
omission from the reaction mixture reduces the activity by 60%
retinoic acid
-
treatment of cells induces increase in ornithine aminotransferase expression and activity which results in decreased intracellular concentrations of ornithine and polyamines putrescine, spermidine and spermine. Changes occur concomitantly with a decrease in the total number of cells, and the increase in ornithine aminotransferase activity is due to increased mRNA expression. In cells treated with 1 microM retinoic acid, addition of 10 microM putrescine to culture medium restores both cellular levels of polyamines and cell numbers to the values for the control group
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.191 - 43.4
2-oxoglutarate
1.4
DL-pyrroline-5-carboxylate
-
-
6.7
glyoxylate
-
pH 7.1, 37C
25
L-glutamate
-
-
0.9 - 91
L-ornithine
1.53
N-acetylornithine
-
pH 7.4, 37C
1.7 - 2.9
ornithine
22
pyruvate
-
pH 7.1, 37C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0333
2-oxoglutarate
Manduca sexta
-
-
0.0333 - 4.3
L-ornithine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2867 - 7.7
L-ornithine
192
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
35
1,3-Diaminopropane
-
pH 8.0, 37C
0.0017
5-Aminopentanoate
-
pH 8, 37C
0.07
5-Fluoromethylornithine
-
37C, pH 8
3
diethylenetriamine
-
pH 8.0, 37C
0.00043
hydroxylamine
-
pH 8, 37C
0.000492
L-canaline
-
pH 7.4, 37C
7
L-norvaline
-
pH 8.0, 37C
2 - 20
L-valine
0.0088
N2-L-acetyl ornithine
-
pH 8, 37C
13
norspermidine
-
pH 8.0, 37C
90
putrescine
-
pH 8.0, 37C
2 - 5
spermidine
-
pH 8.0, 37C
17
spermine
-
pH 8.0, 37C
0.8
triethylenetetramine
-
pH 8.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000184
-
healthy patients
0.00024
-
DELTA1-pyrroline-5-carboxylate is formed per mg enzyme per minute in lysates from platelets, without cofactor pyridoxal 5'-phosphate, in 50 mM Tris-HCl, pH 8.0; DELTA1-pyrroline-5-carboxylate is formed per mg enzyme per minute in lysates from white blood cells, without cofactor pyridoxal 5'-phosphate, in 50 mM Tris-HCl, pH 8.0
0.0011 - 0.0072
-
fibroblast
0.0011
-
native chorionic villi
0.00133
-
DELTA1-pyrroline-5-carboxylate is formed per mg enzyme per minute in lysates from white blood cells, with 0.05 mM pyridoxal 5'-phosphate, in 50 mM Tris-HCl, pH 8.0
0.00228
-
DELTA1-pyrroline-5-carboxylate is formed per mg enzyme per minute in lysates from platelets, with 0.05 mM pyridoxal 5'-phosphate, in 50 mM Tris-HCl, pH 8.0
0.0026 - 0.228
-
depending on gestational age
0.0052
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)
0.3
wild-type (OAT in parasite cell extract), pH 7.4, 37C
1.9
wild-type with PfGrx, pH 7.4, 37C
2
wild-type, pH 7.4, 37C
4.01
-
assay based on detection of L-glutamate, pH 8.0, 37C
5.22
-
assay based on reduction of DELTA1-pyrroline-5-carboxylate, pH 8.0, 37C
19.08
-
-
20.9
wild-type with PfTrx, pH 7.4, 37C
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
pH 7.0: about 50% of activity maximum, pH 9.0: about 60% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
expression is undetectable in the embryo, but increase of activity is observed in germinating embryos and seedlings
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
decrease in transcription during the first stages of fruitbody development
Manually annotated by BRENDA team
-
well and poorly differentiated
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
lysate from human blood
Manually annotated by BRENDA team
highest expression in male mice
Manually annotated by BRENDA team
expression is highly induced at early stages of germination and seedling development in all different organs. An increase of activity is observed in germinating embryos and seedlings
Manually annotated by BRENDA team
increase in transcript level in lignified stems of 90-d-old plants
Manually annotated by BRENDA team
-
lysate from human blood
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Toxoplasma gondii (strain ATCC 50611 / Me49)
Toxoplasma gondii (strain ATCC 50611 / Me49)
Toxoplasma gondii (strain ATCC 50611 / Me49)
Toxoplasma gondii (strain ATCC 50611 / Me49)
Toxoplasma gondii (strain ATCC 50611 / Me49)
Toxoplasma gondii (strain ATCC 50611 / Me49)
Toxoplasma gondii (strain ATCC 50611 / Me49)
Toxoplasma gondii (strain ATCC 50611 / Me49)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
4 * 33000, empirical weight determined from the values for the thiol and half-cystine content
36000
-
4 * 36000, SDS-PAGE
42000
-
2 * 42000, SDS-PAGE
43000
-
4 * 43000, SDS-PAGE
44000
-
4 * 44000, SDS-PAGE
46000 - 47000
-
SDS-PAGE
46000
-
2 * 46000, SDS-PAGE
48100
-
x * 48100, calculated
49000
x * 51200, calculated, x * 49000, SDS-PAGE
50700
x * 50700, calculated
51200
x * 51200, calculated, x * 49000, SDS-PAGE
62000
-
1 * 62000, SDS-PAGE
63000
-
gel filtration
74000
-
-
80000 - 85000
-
sedimentation equilibrium method, gel filtration
82000
-
gel filtration
88000
-
gel filtration
90000
-
gel filtration
92000
-
gel filtration
109000
-
gel filtration
132000
-
equilibrium ultracentrifugation
148000 - 152000
-
nondenaturing PAGE, gel filtration
161000
-
equilibrium sedimentation analysis
177000
-
sucrose density gradient centrifugation
256000
-
equilibrium sedimentation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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
monomer
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complexed to gabaculine and L-canaline, hanging drop vapor diffusion method
-
complexed with 5-fluoromethylornithine, hanging drop vapor diffusion method
-
hanging drop vapor diffusion method
-
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
-
the three-dimensional crystal structure of Plasmodium falciparum OAT at 2.3 A resolution is reported. The overall structure is very similar to that of the human OAT. In plasmodial OAT, the loop involved in substrate binding contains two cysteine residues, which are lacking in human OAT
hanging drop vapor diffusion method
-
homology modeling of crystal structure and flexible docking studies. G106 and K256 are the important residues in binding
-
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
58
-
temperature at which 50% of the activity is retained upon 30 min
66
-
pH 7.5, 15 min, 85% loss of activity, 60 min, 96% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol or DTT stabilizes
-
activity of the purified enzyme is preserved by addition of pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate is required during solubilization and purification
-
pyridoxal 5'-phosphate slightly increases heat stability
-
pyridoxal 5'-phosphate stabilizes
-
stability enhanced by presence of DTT and glycerol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, pH 6-8, 0.01 M potassium phosphate buffer, about 20% loss of activity after 4 months
-
-15C, rat liver homogenate in sucrose or phosphate solution, stable for some weeks
-
-20C, 50 mM potassium phosphate buffer, pH 8, 5 mM 2-oxoglutarate, 0.02 mM pyridoxal phosphate, 90-100% retention of activity after 1 month
-
-60C, long-term storage is best as a pellet under liquid-saturated ammonium sulfate
-
1C, sharp loss in activity, especially in absence of free pyridoxal phosphate and mercaptans
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hitrap Q anion exchange chromatography
homogeneity
partial
recombinant protein
-
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
calmodulin-binding peptide fusion protein
-
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli
expression of the entire human gene in Escherichia coli
-
fusion with maltose binding protein
-
mothbean enzyme is expressed in Escherichia coli
-
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
delta OAT and proline dehydrogenases are induced upon non-host pathogen infection
-
deltaOAT and proline dehydrogenases are induced upon non-host pathogen infection
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E235A
-
mutant retains its regiospecificity for the gamma-amino group of ornithine, but the glutamate reaction is enhanced 650fold, whereas only a 5fold enhancement of the ketoglutarate reaction rate results
E235S
-
mutation leads to a lowering of the apparent rate and an increase of the dissociation constant
G237D
-
patient with gyrate atrophy of the choroid and retina, mutation of both alleles, no enzymic activity in white blood cells. Son of patient is heterozygous for the mutation and has 45% of normal values for enzyme activity
Y85L
-
significant decrease in reactivity toward ornithine
C154S
mutant shows drastically reduced activity. Activity can be activated by Trx but not to the same extent as wild-type
C154S/C163S
double mutant shows the same phenotype as mutant C154S
C163S
mutant degrades ornithine with the same specific activity as the wild-type, and the Trx-mediated activation occurres at higher Trx concentrations when compared to OAT wild-type
C316S
transamination of ornithine and 2-oxoglutarate with an activity is reduced to 25-35% of the wild-type. Mutants can be activated by Trx and reaches a specific activity comparable to PfOAT wild-type with Trx
C350S
transamination of ornithine and 2-oxoglutarate with an activity is reduced to 25-35% of the wild-type. Mutants can be activated by Trx and reaches a specific activity comparable to PfOAT wild-type with Trx
C390S
transamination of ornithine and 2-oxoglutarate with an activity is reduced to 25-35% of the wild-type. Mutants can be activated by Trx and reaches a specific activity comparable to PfOAT wild-type with Trx
L402P
mutation based on mutant identified in humans, abrogates both OAT enzymatic activity and ability to modulate the developmental phenotype
R180T
mutation based on mutant identified in humans, abrogates both OAT enzymatic activity and ability to modulate the developmental phenotype
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
expression of enzyme in Oryza sativa, transgenic plants are significantly taller than control, and more resistant to high salinity and drought
analysis
-
development of two new continuous, coupled assays for ornithine-delta-aminotransferase (OAT) that are more sensitive than previous methods, measure activity in real time, and can be carried out in multi-well plates for convenience and high throughput. The first assay is based on the reduction of DELTA1-pyrroline-5-carboxylate (P5C), generated from ornithine by OAT, using human pyrroline 5-carboxylate reductase 1, which results in the concomitant oxidation of NADH to NAD+. This procedure is three times more sensitive than previous methods, and is suitable for the study of small molecules as inhibitors or inactivators of OAT or as a method to determine OAT activity in unknown samples. The second method involves the detection of L-glutamate, produced during the regeneration of the cofactor PLP of OAT by an unamplified modification of the commercially available Amplex Red L-glutamate detection kit (Life Technologies). This assay is recommended for the determination of the substrate activity of small molecules against OAT
biotechnology
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
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; 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
medicine
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