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evolution
aOTC is a widespread enzyme that is found in a large variety of organisms from bacteria to mammals
evolution
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aOTC is a widespread enzyme that is found in a large variety of organisms from bacteria to mammals
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malfunction
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absence of this enzyme impairs the growth of Listeria under mild acidic conditions at pH 4.8 and reduced its survival in synthetic human gastric fluid at pH 2.5, corresponding to a loss in ammonia production
malfunction
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inborn deficiency of OTC causes mainly urea cycle-related disorders and leads to hyperammonemic states that may become lethal. Some states of hepatotoxicity are associated woth hepatocyte disruption and release of OTC into the bloodstream
malfunction
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absence of this enzyme impairs the growth of Listeria under mild acidic conditions at pH 4.8 and reduced its survival in synthetic human gastric fluid at pH 2.5, corresponding to a loss in ammonia production
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metabolism
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the binding of carbamoyl phosphate to the enzymes aspartate and ornithine transcarbamoylase reduces the rate of thermal decomposition of carbamoyl phosphate by a factor of >5000. Both of these transcarbamoylases use an ordered-binding mechanism in which carbamoyl phosphate binds first, allowing the formation of an enzyme-carbamoyl phosphate complex. The critical step in the thermal decomposition of carbamoyl phosphate in aqueous solution, in the absence of enzyme, involves the breaking of the C-O bond facilitated by intramolecular proton transfer from the amine to the phosphate. The binding of carbamoyl phosphate to the active sites of the enzymes significantly inhibits this process by restricting the accessible conformations of the bound ligand to those disfavoring the reactive geometry
metabolism
anabolic ornithine transcarbamoylase is involved in the urea cycle and L-arginine biosynthesis
metabolism
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ArgF is involved in the biosynthesis of L-arginine, overview
metabolism
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catabolic ornithine and putrescine carbamoyltransfer reactions constitute the second step of arginine deiminase and agmatine deiminase pathways. However, the equilibrium of in vitro carbamoyltransfer reactions is overwhelmingly towards the anabolic direction, suggesting that catabolic carbamoyltransferase is probably the limiting step of the pathways. lmo0036 is induced at the transcriptional level when Listeria monocytogenes is subjected to low-pH stress. Its expression product in Escherichia coli exhibits higher catabolic carbamoyltransfer activities under acidic conditions
metabolism
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Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
metabolism
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the enzyme is a mitochondria matrix urea cycle enzyme that is primarily expressed in hepatocyte
metabolism
carbamoyl-phosphate synthetase and ornithine carbamoyltransferase form an efficient channeling cluster for carbamoyl phosphate, an extremely thermolabile and potentially toxic metabolic intermediate. Therefore, by physically interacting with each other, carbamoyl-phosphate synthetase and ornithine carbamoyltransferase prevent the thermodenaturation of carbamoyl phosphate in the aqueous cytoplasmic environment
metabolism
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the enzyme activity supports nitric oxide production in nitrergic neurons
metabolism
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the enzyme is a mitochondria matrix urea cycle enzyme that is primarily expressed in hepatocyte
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metabolism
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Sulfolobus solfataricus lacks ornithine acetyltransferase and thus forms N-acetylglutamate exclusively via the energetically less favourable reaction catalysed by N-acetylglutamate synthase, investing 1 mol of acetyl CoA per mol of N-acetyl intermediate synthesized
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metabolism
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anabolic ornithine transcarbamoylase is involved in the urea cycle and L-arginine biosynthesis
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metabolism
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catabolic ornithine and putrescine carbamoyltransfer reactions constitute the second step of arginine deiminase and agmatine deiminase pathways. However, the equilibrium of in vitro carbamoyltransfer reactions is overwhelmingly towards the anabolic direction, suggesting that catabolic carbamoyltransferase is probably the limiting step of the pathways. lmo0036 is induced at the transcriptional level when Listeria monocytogenes is subjected to low-pH stress. Its expression product in Escherichia coli exhibits higher catabolic carbamoyltransfer activities under acidic conditions
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physiological function
insertion mutant shows arginine auxotrophy and formes infection threads for symbiosis with Lotus japonicus, but the nodules formed have few infected cells filled with bacteroids
physiological function
arginine biosynthesis
physiological function
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Lmo0036 is responsible for acid tolerance at both sublethal and lethal pH levels and plays a possible role in Listeria virulence
physiological function
OTC catalyzes the reversible transfer of the carbamoyl group from carbamoyl phosphate to the Nepsilon atom of L-ornithine to produce L-citrulline. There are two types of enzyme: anabolic, aOTC, and catabolic, cOTC. Anabolic OTCs catalyze the forward reaction and participate in the urea cycle and L-arginine biosynthesis
physiological function
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OTC is involved in the metabolic transformation of arginine and proline and participates in the urea cycle. OTC is regulated by glucocorticoids and other transcriptional factors, such as C/EFP and HNF-4. OTC is released into the blood stream from liver in case of liver regeneration cell proliferation, extracellular might play a role as signaling molecule
physiological function
the OTC activity of the enzyme is involved in arginine biosynthesis
physiological function
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physically interacting with each other, carbamate kinase and ornithine carbamoyltransferase prevent thermodenaturation of carbamoyl phosphate (a precursor of pyrimidines and arginine, which is an extremely labile and potentially toxic intermediate) in the aqueous cytoplasmic environment. The carbamoyl phosphate channelling complex involves carbamate kinase, ornithine carbamoyltransferase and aspartate carbamoyltransferase
physiological function
the enzyme ArgK in Pseudomona syringae pv. phaseolicola is resonsible for self-defense in the antimetabolic phytotoxin phaseolotoxin, a sulfodiaminophosphinyl tripeptide produced to inhibit plant host cell's ornithine transcarbamylase activity and induce arginine auxotrophic phenotype. Phaseolotoxin-resistant OTCase ArgK acts as a functional replacement of housekeeping OTCase ArgF, which is the acting target of phaseolotoxin, to confer phaseolotoxin producers with self-resistance. But neither transcriptional regulator nor thermal regulation related protein encoding gene is detected from PHT biosynthetic gene cluster
physiological function
the enzyme induces proinflammatory cytokine gene expression by activating NF-kappaB in macrophages of the bovine host. The enzyme plays a role in induction of upregulation of interferon-gamma and proinflammatory cytokines (interleukin-1beta, IL-6, and tumor necrosis factor-alpha) in Bos taurus Ana-1 macrophages
physiological function
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the enzyme which is involved in bacterial adherence, may efficiently stimulate an immune response conferring protection against Streptococcus suis infections
physiological function
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the enzyme ArgK in Pseudomona syringae pv. phaseolicola is resonsible for self-defense in the antimetabolic phytotoxin phaseolotoxin, a sulfodiaminophosphinyl tripeptide produced to inhibit plant host cell's ornithine transcarbamylase activity and induce arginine auxotrophic phenotype. Phaseolotoxin-resistant OTCase ArgK acts as a functional replacement of housekeeping OTCase ArgF, which is the acting target of phaseolotoxin, to confer phaseolotoxin producers with self-resistance. But neither transcriptional regulator nor thermal regulation related protein encoding gene is detected from PHT biosynthetic gene cluster
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physiological function
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OTC catalyzes the reversible transfer of the carbamoyl group from carbamoyl phosphate to the Nepsilon atom of L-ornithine to produce L-citrulline. There are two types of enzyme: anabolic, aOTC, and catabolic, cOTC. Anabolic OTCs catalyze the forward reaction and participate in the urea cycle and L-arginine biosynthesis
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physiological function
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Lmo0036 is responsible for acid tolerance at both sublethal and lethal pH levels and plays a possible role in Listeria virulence
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physiological function
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the enzyme which is involved in bacterial adherence, may efficiently stimulate an immune response conferring protection against Streptococcus suis infections
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physiological function
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physically interacting with each other, carbamate kinase and ornithine carbamoyltransferase prevent thermodenaturation of carbamoyl phosphate (a precursor of pyrimidines and arginine, which is an extremely labile and potentially toxic intermediate) in the aqueous cytoplasmic environment. The carbamoyl phosphate channelling complex involves carbamate kinase, ornithine carbamoyltransferase and aspartate carbamoyltransferase
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additional information
sequence 230YGLY233 is the putrescine signature sequence
additional information
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stochastic simulations of coarse-grained protein models used to investigate the propensity to form knots in early stages of protein folding, comparison of natively-knotted N-acetylornithine carbamoyltransferase, AOTCase, EC 2.1.3.9, and an unknotted ornithine carbamoyltransferase, OTCase, protein and amino acid interactions, mechanism, overview. The different entanglement of the two transcarbamylases follows from the tendency of the C-terminal to point away from (for OTCase) or approach and eventually thread (for AOTCase) other regions of partly-folded protein. The analysis of the OTCase/AOTCase pair clarifies that natively-knotted proteins can spontaneously knot during early folding stages and that non-native sequence-dependent interactions are important for promoting and disfavouring early knotting events. Knotting usually results from the threading of the C-terminal through loops present in the loose protein globule. Simulation of the early folding process of the two transcarbamylases, non-native interactions, kinetics, and modeling, overview
additional information
the conserved active site of Campylobacter jejuni aOTC consists of residues from both carbamoyl phosphate binding and L-ornithine-binding domains of the subunit and the B2-H3 loop, residues 68-78, from an adjacent subunit of the trimer, active site structure, overview
additional information
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the conserved active site of Campylobacter jejuni aOTC consists of residues from both carbamoyl phosphate binding and L-ornithine-binding domains of the subunit and the B2-H3 loop, residues 68-78, from an adjacent subunit of the trimer, active site structure, overview
additional information
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the enzyme is released in response to drugs
additional information
the putative L-ornithine binding residues in aTtOTCase are Asn164, Asn165, Asp220, Ser224 and Met225. The active site geometry of the enzyme is unique among its homologs where the side chain of certain residues (Leu57, Arg58 and Arg288) is oriented differently, substrate binding in the enzyme, docking of carbamoyl phosphate (CP) and ornithine, structure analysis, overview
additional information
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the putative L-ornithine binding residues in aTtOTCase are Asn164, Asn165, Asp220, Ser224 and Met225. The active site geometry of the enzyme is unique among its homologs where the side chain of certain residues (Leu57, Arg58 and Arg288) is oriented differently, substrate binding in the enzyme, docking of carbamoyl phosphate (CP) and ornithine, structure analysis, overview
additional information
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the enzyme is released in response to drugs
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additional information
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the conserved active site of Campylobacter jejuni aOTC consists of residues from both carbamoyl phosphate binding and L-ornithine-binding domains of the subunit and the B2-H3 loop, residues 68-78, from an adjacent subunit of the trimer, active site structure, overview
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additional information
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the putative L-ornithine binding residues in aTtOTCase are Asn164, Asn165, Asp220, Ser224 and Met225. The active site geometry of the enzyme is unique among its homologs where the side chain of certain residues (Leu57, Arg58 and Arg288) is oriented differently, substrate binding in the enzyme, docking of carbamoyl phosphate (CP) and ornithine, structure analysis, overview
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