2.1.3.3: ornithine carbamoyltransferase
This is an abbreviated version!
For detailed information about ornithine carbamoyltransferase, go to the full flat file.
Word Map on EC 2.1.3.3
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2.1.3.3
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coherence
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tomography
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eyes
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retinal
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macular
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acuity
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angiography
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nerve
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fiber
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vessel
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fundus
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choroid
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vision
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fluorescein
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coronary
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posterior
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spectral-domain
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edema
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modal
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glaucoma
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foveal
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retinopathy
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refract
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intraocular
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multimodal
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plexiform
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quadrant
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photography
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corneal
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autofluorescence
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best-corrected
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intravitreal
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neovascularization
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ophthalmic
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peripapillary
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glaucomatous
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stent
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ophthalmology
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ganglion
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subretinal
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vitrectomy
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analysis
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myopia
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biotechnology
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angiogram
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drug-eluting
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ellipsoid
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vitreous
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phantom
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medicine
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diagnostics
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traction
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anti-vegf
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indocyanine
- 2.1.3.3
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coherence
-
tomography
- eyes
- retinal
-
macular
-
acuity
-
angiography
- nerve
- fiber
- vessel
-
fundus
- choroid
- vision
- fluorescein
- coronary
-
posterior
-
spectral-domain
- edema
-
modal
- glaucoma
-
foveal
- retinopathy
-
refract
-
intraocular
-
multimodal
-
plexiform
-
quadrant
-
photography
- corneal
-
autofluorescence
-
best-corrected
-
intravitreal
- neovascularization
-
ophthalmic
-
peripapillary
-
glaucomatous
-
stent
-
ophthalmology
- ganglion
-
subretinal
-
vitrectomy
- analysis
- myopia
- biotechnology
-
angiogram
-
drug-eluting
-
ellipsoid
- vitreous
-
phantom
- medicine
- diagnostics
-
traction
-
anti-vegf
-
indocyanine
Reaction
Synonyms
anabolic ornithine carbamoyltransferase, anabolic ornithine transcarbamoylase, AOTC, arcB gene product, ArgF, ArgK, aTtOTCase, carbamoyltransferase, carbamoyltransferase, ornithine, carbamylphosphate-ornithine transcarbamylase, catabolic ornithine carbamoyltransferase, catabolic ornithine transcarbamylase, citrulline phosphorylase, cOTC, L-ornithine carbamoyltransferase, L-ornithine carbamyltransferase, L-ornithine transcarbamylase, Lmo0036, MB1684, Mtb OTC, OCT, ornithine carbamoyltransferase, ornithine carbamoytransferase, ornithine carbamyl transferase, ornithine carbamyltransferase, ornithine transcarbamoylase, ornithine transcarbamylase, ornithine transcarbamylase 3, OTC, otcase, ROTCase
ECTree
2.1.3.3 ornithine carbamoyltransferaseAdvanced search results
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results (Application
Application on EC 2.1.3.3 - ornithine carbamoyltransferase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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after administration of carbon tetrachloride, allyl alcohol, D-galactosamine, lipopolysaccharide, and concanavalin A, the significant increase in the serum levels of the markers is faster in type-I arginase and ornithine carbamoyltransferase than aspartate aminotransferase and alanine aminotransferase. The extent of the increase at the peak is always higher in type-I arginase and ornithine carbamoyltransferase than in spartate aminotransferase and alanine aminotransferase
biotechnology
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HepG2 is an immortalized human hepatoma cell line that has been used for research into bioartificial liver systems. However, a low level of ammonia detoxification is its biggest drawback. Stable overexpression of arginase I and ornithine transcarbamylase in HepG2 cells improves its ammonia detoxification
diagnostics
medicine
diagnostics
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the enzyme alone or in combination with other markers is a useful indicator for Kupffer cell activation as well as for mitochondrial damage in hepatic cells
diagnostics
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ornithine carbamoyltransferase is one promising blood-based biomarker candidate for liver injury examination
diagnostics
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the enzyme can be used as biomarker for early stage of hepatic injury induced by CCl4, diagnostics values are best in combination with total bile acid and phosphorylase measurements
diagnostics
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ornithine carbamoyltransferase is one promising blood-based biomarker candidate for liver injury examination
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diagnostics
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the enzyme can be used as biomarker for early stage of hepatic injury induced by CCl4, diagnostics values are best in combination with total bile acid and phosphorylase measurements
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medicine
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after administration of carbon tetrachloride, allyl alcohol, D-galactosamine, lipopolysaccharide, and concanavalin A, the significant increase in the serum levels of the markers is faster in type-I arginase and ornithine carbamoyltransferase than aspartate aminotransferase and alanine aminotransferase. The extent of the increase at the peak is always higher in type-I arginase and ornithine carbamoyltransferase than in spartate aminotransferase and alanine aminotransferase
medicine
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in patients with Alzheimer's disease, ornithine carbamoyltransferase is expressed in brain, but not in controls. Ornithine carbamoyltransferase expression is strictly restricted to vascular endothelial cells. Ornithine carbamoyltransferase activity is 880% increased in the cerebrospinal fluid of probable Alzheimer's disease cases compared with controls. Rare haplotypes may be associated with the risk of Alzheimer's disease through a possible modulation of the methylation of the ornithine carbamoyltransferase promoter
medicine
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in patients with non-alcoholic steatohepatitis, the serum levels of ornithine carbamoyltransferase and the ratios of ornithine carbamoyltransferase:alanine amino transferase and ornithine carbamoyltransferase:aspartate amino transferase are increased in parallel with the progression of on-alcoholic steatohepatitis. Especially, ornithine carbamoyltransferase and both ratios are markedly increased in hepatocellular carcinoma. As for the relationship between fibrosis grade and ornithine carbamoyxltransferase, the serum ornthine carbamoyltransferase levels and theratio of ornithine carbamoyltransferase:alanine amino transferase levels are increased in parallel with liver fibrosis. In non-alcoholic steatohepatitis patients with alanine amino transferase within normal range, about 30% show elevation of ornithine carbamoyltransferase
medicine
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ornithine carbamoyltransferase is acetylated at lysine resiudes, including K88, which is also mutated in ornithine carbamoyltransferase-deficient patients. K88 acetylation decreases the affinity for carbamoyl phosphate, and the maximum velocity, whereas the Km for ornithine is not affected
medicine
ornithine carbamyltransferase is present in urine of patients with pulmonary tuberculosis. Recombinant ornithine carboamyltransferase produced in Escherichia coli is recognized by immunoglobulin G antibodies from patients with active tuberculosis but not by IgG from uninfected healthy subjects. Protein is strongly recognized by peripheral blood mononuclear cells from both healthy tuberculin purified protein derivative-positive individuals and patients with pulmonary tuberculosis
medicine
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the serum activities of ornithine carbamoyltransferase and glutamate dehydrogenase increase significantly by chronic ethanol feeding while other markers do not. Although the hepatic content of ornithine carbamoyltransferase and glutamate dehydrogenase also increase, the serum activities do not correlate with the hepatic activities and the extent of increase in the liver is much less than in serum
medicine
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use of multiplex ligation-dependent probe amplification methodology to three ornithine transcarbamylase deficiency patients, two females and one male, reveals copy number alterations of ornithine transcarbamylase exons in all of them. The two females are heterozygous for deletions of either exon 2 or exons 6-9, and the male is confirmed to lack all exons. Females' characterization of the deletion breakpoints reveal mutations corresponding to exon 2 and exon 6-9 deletions, respectively. Exon 2 deletion probably results from replication slippage facilitated by a secondary structure formed by two inverted Alu repeats, whereas an Alu-Alu homologous recombination is probably responsible for the exon 6_9 deletion
medicine
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enzyme downregulation is associated with poor prognosis in hepatocellular carcinoma
medicine
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measurement of serum enzyme concentration is a useful marker of disease severity, and thus can be a useful marker for a high risk of hepatocellular carcinoma occurrence
medicine
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ornithine carbamyltransferase is present in urine of patients with pulmonary tuberculosis. Recombinant ornithine carboamyltransferase produced in Escherichia coli is recognized by immunoglobulin G antibodies from patients with active tuberculosis but not by IgG from uninfected healthy subjects. Protein is strongly recognized by peripheral blood mononuclear cells from both healthy tuberculin purified protein derivative-positive individuals and patients with pulmonary tuberculosis
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