Information on EC 2.1.3.3 - ornithine carbamoyltransferase

New: Word Map on EC 2.1.3.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
2.1.3.3
-
RECOMMENDED NAME
GeneOntology No.
ornithine carbamoyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
-
-
-
-
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
mechanism
-
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
mechanism
-
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
mechanism; ping pong mechanism
-
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
mechanism
-
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
ordered mechanism, carbamoylphosphate binds first
-
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
ordered sequential mechanism, carbamoylphosphate binds first, followed by L-ornithine, L-citrulline leaves first, followed by phosphate
-
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
mechanism
-
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
ordered bi-bi-sequential reaction mechanism, carbamoylphosphate binds first followed by L-ornithine, L-citrulline leaves first followed by phosphate
-
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
ordered mechanism with carbamoyl phosphate first substrate to bind
-
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
ping-pong reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carbamoyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-arginine biosynthesis I (via L-ornithine)
-
-
L-arginine biosynthesis II (acetyl cycle)
-
-
L-arginine biosynthesis IV (archaebacteria)
-
-
L-citrulline biosynthesis
-
-
L-citrulline degradation
-
-
L-proline biosynthesis II (from arginine)
-
-
urea cycle
-
-
urea cycle
-
-
Arginine biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
carbamoyl-phosphate:L-ornithine carbamoyltransferase
The plant enzyme also catalyses the reactions of EC 2.1.3.6 putrescine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
anabolic ornithine carbamoyltransferase
-
-
anabolic ornithine transcarbamoylase
-
anabolic ornithine transcarbamoylase
Campylobacter jejuni NCTC11168
-
-
AOTC
Campylobacter jejuni NCTC11168
-
-
arcB gene product
-
-
arcB gene product
Lactobacillus hilgardii CETC4786T
-
-
-
carbamoyltransferase, ornithine
-
-
-
-
carbamylphosphate-ornithine transcarbamylase
-
-
-
-
catabolic ornithine carbamoyltransferase
-
-
catabolic ornithine carbamoyltransferase
-
-
-
catabolic ornithine transcarbamylase
-
-
catabolic ornithine transcarbamylase
Lactobacillus hilgardii CETC4786T
-
-
-
citrulline phosphorylase
-
-
-
-
cOTC
Lactobacillus hilgardii CETC4786T
-
-
-
L-ornithine carbamoyltransferase
-
-
-
-
L-ornithine carbamyltransferase
-
-
-
-
L-ornithine transcarbamylase
-
-
-
-
ornithine carbamoyltransferase
-
ornithine carbamoyltransferase
Campylobacter jejuni NCTC11168
-
-
ornithine carbamoyltransferase
-
-
ornithine carbamoyltransferase
-
-
-
ornithine carbamoyltransferase
-
-
ornithine carbamoyltransferase
-
-
ornithine carbamoyltransferase
Sulfolobus solfataricus P1
-
-
-
ornithine carbamyltransferase
-
-
-
-
ornithine transcarbamoylase
-
-
-
-
ornithine transcarbamoylase
-
-
ornithine transcarbamoylase
-
-
ornithine transcarbamylase
-
ornithine transcarbamylase
-
-
ornithine transcarbamylase
-
ornithine transcarbamylase
-
-
ornithine transcarbamylase
Lactobacillus plantarum Lp60
-
-
-
ornithine transcarbamylase 3
-
OTC
-
-
-
-
OTC
Campylobacter jejuni NCTC11168
-
-
otcase
-
-
otcase
Lactobacillus plantarum Lp60
-
-
-
otcase
Pseudomonas aeruginosa PAO, Pseudomonas aeruginosa PAO532
-
-
-
otcase
Pyrococcus furiosus GE5
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-69-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoenzyme 1
-
-
Manually annotated by BRENDA team
3'-hydroxymethylcephem O-carbamoyltransferase
-
-
Manually annotated by BRENDA team
Arundinaria sp.
sugar cane, cytoplasmic and mitochondrial enzyme form
-
-
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
-
-
Manually annotated by BRENDA team
subsp. jejuni, gene argF
UniProt
Manually annotated by BRENDA team
Campylobacter jejuni NCTC11168
subsp. jejuni, gene argF
UniProt
Manually annotated by BRENDA team
2 isoforms
-
-
Manually annotated by BRENDA team
loggerhead turtle
-
-
Manually annotated by BRENDA team
carrot
-
-
Manually annotated by BRENDA team
blue-green alga
-
-
Manually annotated by BRENDA team
strain W
-
-
Manually annotated by BRENDA team
also known as Halobacterium salinarium, catabolic ornithine carbamoyltransferase
SwissProt
Manually annotated by BRENDA team
mRNA isoforms OTC-t1, OTC-t2, and OTC-t3 are transcribed from the OTC gene
UniProt
Manually annotated by BRENDA team
normal liver enzyme and enzyme from a liver of a patient with Reye's syndrome
-
-
Manually annotated by BRENDA team
ornithine transcarbamoyltransferase deficiency is the most common cause of inherited urea cycle disorders
-
-
Manually annotated by BRENDA team
patients with Alzheimer's disease
-
-
Manually annotated by BRENDA team
patients with non-alcoholic steatohepatitis
-
-
Manually annotated by BRENDA team
patients with ornithine transcarbamylase deficiency
-
-
Manually annotated by BRENDA team
strain CETC4786T, ATCC 8290
-
-
Manually annotated by BRENDA team
Lactobacillus hilgardii CETC4786T
strain CETC4786T, ATCC 8290
-
-
Manually annotated by BRENDA team
strain Lp60, high assimilation of citrulline, low ornithine transcarbamylase activity
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum Lp60
strain Lp60, high assimilation of citrulline, low ornithine transcarbamylase activity
-
-
Manually annotated by BRENDA team
putrescine synthase has inherent activities of agmatine iminohydrolase, putrescine carbamoyltransferase, ornithine carbamoyltransferase and carbamate kinase
-
-
Manually annotated by BRENDA team
gene lmo0036
-
-
Manually annotated by BRENDA team
BCG cells
-
-
Manually annotated by BRENDA team
catabolic ornithine carbamoyltransferase
-
-
Manually annotated by BRENDA team
strain PAO and mutants from strain PAO
-
-
Manually annotated by BRENDA team
strain PAO532
-
-
Manually annotated by BRENDA team
strains PAO1 and PTO6095
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa PAO
strain PAO
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa PAO532
strain PAO532
-
-
Manually annotated by BRENDA team
pv. phaseolicola
-
-
Manually annotated by BRENDA team
pv. phaseolicola
-
-
Manually annotated by BRENDA team
pv. phaseolicola, induction of enzyme expression by carbamoylphosphate, enzyme expression is independent of temperature and regulated directly by a compound resembling the inorganic moiety of phaseolotoxin
-
-
Manually annotated by BRENDA team
male 9-weeks-old Wistar rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
plasmid-containing enzyme-overproducing strain
-
-
Manually annotated by BRENDA team
shark
-
-
-
Manually annotated by BRENDA team
Streptococcus sp. D10
D10
-
-
Manually annotated by BRENDA team
3'-hydroxymethylcephem O-carbamoyltransferase
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus P1
-
-
-
Manually annotated by BRENDA team
house musk shrew
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
aOTC is a widespread enzyme that is found in a large variety of organisms from bacteria to mammals
evolution
Campylobacter jejuni NCTC11168
-
aOTC is a widespread enzyme that is found in a large variety of organisms from bacteria to mammals
-
malfunction
-
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
-
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
-
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
-
metabolism
-
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
-
ArgF is involved in the biosynthesis of L-arginine, overview
metabolism
-
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
-
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
Campylobacter jejuni NCTC11168
-
anabolic ornithine transcarbamoylase is involved in the urea cycle and L-arginine biosynthesis
-
metabolism
-
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
-
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
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
-
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
-
Lmo0036 is responsible for acid tolerance at both sublethal and lethal pH levels and plays a possible role in Listeria virulence
physiological function
the OTC activity of the enzyme is involved in arginine biosynthesis
physiological function
-
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
Campylobacter jejuni NCTC11168
-
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
-
Lmo0036 is responsible for acid tolerance at both sublethal and lethal pH levels and plays a possible role in Listeria virulence
-
physiological function
Pyrococcus furiosus GE5
-
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
-
metabolism
Sulfolobus solfataricus P1
-
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
-
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
-
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
sequence 230YGLY233 is the putrescine signature sequence
additional information
Campylobacter jejuni NCTC11168
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-hydroxymethylcephem + carbamoyl phosphate
cephamycin C + phosphate
show the reaction diagram
-
-
-
?
arsenate + L-citrulline
carbamoylarsenate + L-ornithine
show the reaction diagram
-
pseudo-reverse reaction, arsenate is first coupled to citrulline, followed by elimination of carbamoylarsenate
-
r
carbamoyl phosphate + canaline
O-ureidohomoserine + phosphate
show the reaction diagram
-
66fold higher activity with canaline than with ornithine
-
?
carbamoyl phosphate + canaline
O-ureidohomoserine + phosphate
show the reaction diagram
-
isoform 2 shows 13times higher canaline-dependent transcarbamoylase activity than ornithine-dependent transcarbamoylase activity
-
-
carbamoyl phosphate + canaline
O-ureidohomoserine + phosphate
show the reaction diagram
-
66fold higher activity with canaline than with ornithine, enzyme may play a role in canavanine synthesis
-
?
carbamoyl phosphate + diaminobutane
phosphate + ?
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-lysine
phosphate + ?
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?, r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
-
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
-
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
ir
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
shark
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
Arundinaria sp.
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
highly specific for L-ornithine at pH 8.0
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
enzyme also catalyzes the reactions of EC 2.1.3.6, EC 2.7.2.2 and EC 3.5.3.12, thus acting as putrescine synthase converting agmatine and ornithine into putrescine and citrulline
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
very low activity with canaline
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
catabolic ornithine carbamoyltransferase, catalyzes the reverse reaction, i.e. the cleavage of citrulline
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
catabolic ornithine carbamoyltransferase, catalyzes the reverse reaction, i.e. the cleavage of citrulline
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
isoform 1 shows 14times higher ornithine-dependent transcarbamoylase activity than canaline-dependent transcarbamoylase activity
-
-
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
enzyme catalyzes the synthesis of delta-acetyl ornithine at 0.3-0.5% the rate of citrulline synthesis at pH 8.5 when acetyl phosphate replaces carbamoyl phosphate
-
-
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
anabolic function
-
ir
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
anabolic function
-
-
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
enzyme belongs to the arginine biosynthesis pathway
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
Arundinaria sp.
-
cytoplasmic form has predominantly catabolic function, mitochondrial form has anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
catalyzes the last step of mitochondrial citrulline synthesis
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
first step in arginine biosynthesis
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
enzyme is involved in the biosynthesis of arginine in many organisms and participates in the urea cycle of mammals
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
enzyme seems to be involved in a bicarbonate-fixing pathway
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
ornithine transcarbamylase deficiency is the most common inherited disorder of the urea cycle and is transmitted as an X-linked trait, defects in the OTC gene, especially at clusters of the substrate binding sites, cause a block in ureagenesis resulting in hyperammonemia, which can lead to brain damage and death, the carbamoyl phosphate binding site contains the highly conserved motif Ser90-Thr91-Arg92-Thr93-Arg94, the ornithine binding site contains the His302-Cys303-Leu304-Pro305 motif
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
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
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
Bacillus subtilis 168
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
Streptococcus sp. D10
-
enzyme catalyzes the synthesis of delta-acetyl ornithine at 0.3-0.5% the rate of citrulline synthesis at pH 8.5 when acetyl phosphate replaces carbamoyl phosphate
-
-
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
Sulfolobus solfataricus P1
-
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
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
catalyzes the sixth step in arginine biosynthesis
-
r
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
Pseudomonas aeruginosa PAO532
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
Pseudomonas aeruginosa PAO
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
-
-
-
r
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
-
-
r
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
the mechanism of the aOTC-catalyzed reaction involves nucleophilic attack of the electron pair of the epsilon-amino group of L-ornithine on the carbonyl group of carbamoyl phosphate
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
-
-
-
r
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
Campylobacter jejuni NCTC11168
the mechanism of the aOTC-catalyzed reaction involves nucleophilic attack of the electron pair of the epsilon-amino group of L-ornithine on the carbonyl group of carbamoyl phosphate
-
?
carbamoyl phosphate + lysine
phosphate + homocitrulline
show the reaction diagram
-
4.3% of the rate with ornithine
-
?
phosphate + L-citrulline
carbamoylphosphate + L-ornithine
show the reaction diagram
-
-
-
?
phosphate + L-citrulline
carbamoylphosphate + L-ornithine
show the reaction diagram
-
catabolic carbamoyltransferase
-
?
phosphate + L-citrulline
carbamoyl phosphate + L-ornithine
show the reaction diagram
-
-
-
r
carbamoyl phosphate + lysine
phosphate + homocitrulline
show the reaction diagram
-
at alkaline pH
-
?
additional information
?
-
-
involved in arginine metabolism
-
-
-
additional information
?
-
-
key protein involved in the degradation of arginine during malolactic fermentation
-
-
-
additional information
?
-
-
Lmo0036 is an ornithine carbamoyltransferase and also a putrescine carbamoyltransferase, EC 2.1.3.6, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
-
-
-
additional information
?
-
in addition to using putrescine, see EC 2.1.3.6, the enzyme can utilize L-ornithine as a poor substrate. Differences between the respective 230 and SMG loops of putrescine transcarbamoylase PTC and OTC appear to account for the differential preference of these enzymes for putrescine and ornithine, active center and the discrimination mechanism between putrescine and ornithine, overview
-
-
-
additional information
?
-
OTC-t1 and OTC-t2 transcripts display heterogeneity at the cleavage sites in a tissue-dependent manner
-
-
-
additional information
?
-
-
Lmo0036 is an ornithine carbamoyltransferase and also a putrescine carbamoyltransferase, EC 2.1.3.6, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
-
-
-
additional information
?
-
Lactobacillus plantarum Lp60
-
involved in arginine metabolism
-
-
-
additional information
?
-
Lactobacillus hilgardii CETC4786T
-
key protein involved in the degradation of arginine during malolactic fermentation
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + canaline
O-ureidohomoserine + phosphate
show the reaction diagram
-
66fold higher activity with canaline than with ornithine, enzyme may play a role in canavanine synthesis
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
anabolic function
-
ir
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
anabolic function
-
-
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
enzyme belongs to the arginine biosynthesis pathway
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
Arundinaria sp.
-
cytoplasmic form has predominantly catabolic function, mitochondrial form has anabolic function
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
catalyzes the last step of mitochondrial citrulline synthesis
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
first step in arginine biosynthesis
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
enzyme is involved in the biosynthesis of arginine in many organisms and participates in the urea cycle of mammals
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
enzyme seems to be involved in a bicarbonate-fixing pathway
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
ornithine transcarbamylase deficiency is the most common inherited disorder of the urea cycle and is transmitted as an X-linked trait, defects in the OTC gene, especially at clusters of the substrate binding sites, cause a block in ureagenesis resulting in hyperammonemia, which can lead to brain damage and death
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
O93656
there is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Channeling must occur during the dynamic association of coupled enzymes pairs
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
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
-
?
carbamoyl phosphate + L-ornithine
phosphate + citrulline
show the reaction diagram
P9WIT9
catalyzes the sixth step in arginine biosynthesis
-
r
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
-
-
-
r
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
Q9PNU6
-
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
Q837U7
-
-
r
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
-
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
Sulfolobus solfataricus P1
-
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
-
?
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
Campylobacter jejuni NCTC11168
Q9PNU6
-
-
?
additional information
?
-
-
involved in arginine metabolism
-
-
-
additional information
?
-
-
key protein involved in the degradation of arginine during malolactic fermentation
-
-
-
additional information
?
-
-
Lmo0036 is an ornithine carbamoyltransferase and also a putrescine carbamoyltransferase, EC 2.1.3.6, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
-
-
-
additional information
?
-
Lactobacillus plantarum Lp60
-
involved in arginine metabolism
-
-
-
additional information
?
-
Lactobacillus hilgardii CETC4786T
-
key protein involved in the degradation of arginine during malolactic fermentation
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
structure reveals a metal-binding site located at the 3fold molecular symmetry axis of each trimer within the hexamer
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,4-diaminobutane
-
100 mM, 50% inhibition
1,4-diaminobutane
-
10 mM; 10 mM, 45% inhibition
2,4,6-Trinitrobenzenesulfonate
-
-
2,4,6-Trinitrobenzenesulfonate
-
10 mM, almost complete inactivation
2,4-diaminobutyrate
-
-
2-mercaptoethanol
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
complete inactivation at alkaline pH
5-hydroxy-2-aminovaleric acid
-
competitive vs. ornithine, uncompetitive vs. carbamoylphosphate
Acetylimidazole
-
50 mM, 95% inhibition at 25C in 100 mM imidazole-HCl, pH 7.5
ADP
5 mM, 90% inhibition
agmatine
-
13 mM, 50% inhibition
AMP
5 mM, 90% inhibition
arginase
-
500 units, 14% remaining activity
-
arginine
-
several arginine analogs have no effect
arginine
-
L-isomer, 8 mM, 50% inhibition
arsenate
-
competitive vs. carbamoylphosphate, noncompetitive vs. ornithine
ATP
5 mM, 90% inhibition
Carbamoyl phosphate
-
-
Carbamoyl phosphate
-
-
Cd2+
-
1 mM, 99% inhibition
Chlorosis-inducing toxin of Pseudomonas phaseolicola
-
no more than 85% inhibition
-
citrulline
-
competitive to carbamoyl phosphate
CTP
5 mM, 90% inhibition
Cu2+
-
1 mM, 75% inhibition
cystamine
-
complete inactivation, activity is completely recovered by incubation with 20 mM dithiothreitol
delta-N-(phosphonacetyl)-L-ornithine
-
-
delta-N-(phosphonacetyl)-L-ornithine
-
-
delta-N-(phosphonoacetyl)-L-ornithine
bisubstrate analogue inhibitor
Delta-N-Phosphonoacetyl-L-ornithine
-
0.001 mM, 86% inhibition, 0.0025 mM, 95% inhibition
Delta-N-Phosphonoacetyl-L-ornithine
-
competitive vs. carbamoylphosphate; transition state analogue
Delta-N-Phosphonoacetyl-L-ornithine
-
transition state analogue
Delta-N-Phosphonoacetyl-L-ornithine
-
synthesis and properties
Delta-N-Phosphonoacetyl-L-ornithine
-
-
Delta-N-Phosphonoacetyl-L-ornithine
-
-
Delta-N-Phosphonoacetyl-L-ornithine
-
-
Delta-N-Phosphonoacetyl-L-ornithine
-
-
Delta-N-Phosphonoacetyl-L-ornithine
-
weak
diaminobutyric acid
-
-
dithiodiglycol
-
100 mM, inactivation at pH 9,0
dithiothreitol
-
-
DL-2-Amino-5-hydroxypentanoic acid
-
-
DL-2-Amino-5-hydroxypentanoic acid
-
-
glutamine
-
-
glycine
-
-
GTP
5 mM, 90% inhibition
histidine
-
-
L-2,4-diaminobutyric acid
-
-
L-2,4-diaminobutyric acid
-
-
L-2,4-diaminobutyric acid
-
-
L-2-Amino-4-pentenoic acid
-
-
L-2-aminobutyrate
-
L-isomer
L-2-aminobutyrate
-
5-20 mM; L-isomer
L-2-aminobutyrate
-
-
L-2-aminobutyrate
-
L-isomer
L-alanine
-
-
L-asparagine
-
weak
L-cysteine
-
10 mM, 90% inhibition, noncompetitive vs. ornithine
L-isoleucine
-
-
L-isoleucine
-
-
L-leucine
-
-
L-leucine
-
-
L-leucine
-
-
L-lysine
-
weak
L-lysine
-
weak
L-norvaline
-
competitive vs. ornithine
L-norvaline
-
-
L-norvaline
-
competitive vs. ornithine, uncompetitive vs. carbamoylphosphate
L-norvaline
-
2 mM, 50% inhibition
L-norvaline
-
-
L-norvaline
-
-
L-norvaline
-
-
L-norvaline
-
-
L-norvaline
-
competitive
L-ornithine
-
-
L-ornithine
-
-
L-serine
-
weak
L-valine
-
-
L-valine
-
-
methionine
-
L-isomer
methionine
-
-
N-delta-(phosphosulfamyl)ornithylalanylhomoarginine
-
inhibition of isoform 1 only
N-delta-(phosphosulfamyl)ornithylalanylhomoarginine
-
trivial name phaseolotoxin, 0.1 mM, 93% inhibition
NaCl
-
50 mM, 25% inhibition
ornithine
-
at high concentrations
ornithine
-
at high concentrations
ornithine
-
at high concentrations
ornithine
-
at high concentrations; noncompetitive substrate inhibition vs. carbamoylphosphate
ornithine
-
above 10 mM
ornithine
-
above 8 mM
ornithine
-
-
ornithine
-
-
ornithine
-
recombinant wild-type enzyme
ornithine
-
competitive vs. carbamoylphosphate in the presence of phosphate
ornithine-delta-P(O)(NH2)-NH-SO3H
-
inhibition of isoform 1 only
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
inhibition is completely reversed by 2-mercaptoethanol
Phenylglyoxal
-
complete inactivation after 1 h incubation
phosphate
-
competitive vs. carbamoylphosphate, noncompetitive vs. ornithine
phosphate
-
-
phosphate
-
competitive vs. carbamoylphosphate, uncompetitive vs. ornithine
phosphate
-
competitive vs. carbamoylphosphate
phosphate
-
competitive vs. carbamoylphosphate
phosphate
-
-
phosphate
slight inhibition
phosphate
-
competitive
S-carbamoyl cysteine
-
10 mM, 90% inhibition
spermidine
-
10 mM, 93% inhibition, 3.7 mM, 50% inhibition
spermidine
-
E105G mutant enzyme, competitive vs. carbamoylphosphate
spermidine
-
10 mM, more than 98% inhibition of arsenolytic cleavage activity
Tris
-
50 mM, more than 80% inhibition
UTP
5 mM, 90% inhibition
Zn2+
-
1 mM, 44% inhibition
Zn2+
-
5-20 mM
Zn2+
-
-
MgCl2
-
10 mM, 14% inhibition
additional information
-
effects of chemical modifications of specific residues on ligand binding and enzymatic activity
-
additional information
-
not inhibited by 10 mM 2-oxoglutarate, proline, glutamate, aspartate, acetylglutamate, pyruvate, oxaloacetate, glycine, acetylornithine, ATP, GTP, CTP, L-asparagine, arginine and glutamine
-
additional information
-
isoform 2 is not inhibited by phaseolotoxin and ornithine-delta-P(O)(NH2)-NH-SO3H
-
additional information
-
not inhibited by lysine and alpha-methyl-L-ornithine
-
additional information
-
not inhibited by arginine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
10 mM, 350% arsenolytic cleavage activity
AMP
-
strong allosteric activator, 1.5 mM, half-maximal activation
AMP
-
10 mM, 550% arsenolytic cleavage activity, activation by phosphate and AMP correspond to different mechanisms
arginine
50 mM, 2fold activatin
arsenate
-
potent activator in the concentration range of 0-10 mM
CMP
-
strong allosteric activator
CMP
-
10 mM, 340% arsenolytic cleavage activity
CTP
-
10 mM, 340% arsenolytic cleavage activity
GMP
-
allosteric activator
phosphate
-
presumably via interaction with the carbamoyl phosphate-binding site
phosphate
-
potent activator in the concentration range of 0-10 mM
phosphate
-
10 mM, 225% arsenolytic cleavage activity
UMP
-
allosteric activator
UMP
-
10 mM, 600% arsenolytic cleavage activity
GMP
-
10 mM, 340% arsenolytic cleavage activity
additional information
-
activity increases with ionic strength up to 100 mM
-
additional information
-
elevation in enzyme activity with increased duration of crowding is observed for all four ornithine-urea cycle enzymes examined, i.e. carbamoyl phosphate synthetase, ornithine carbamoyl transferase, argininosuccinate synthetase, argininosuccinate lyase, and arginase. By contrast, mRNA expression is variable for the ornithine-urea cycle enzymes. Results suggest that the activities of ornithine-urea cycle enzymes are better predictors for urea production than ornithine-urea cycle enzyme mRNA expression levels
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0008
Carbamoyl phosphate
-
liver enzyme, presence of putrescine, pH 7.0
0.00176
Carbamoyl phosphate
-
liver enzyme, pH 7.0
0.008
Carbamoyl phosphate
pH 8.0, 37C
0.06
Carbamoyl phosphate
-
Q106E
0.09
Carbamoyl phosphate
-
pH 8.5, 37C
0.13
Carbamoyl phosphate
-
wild-type, pH 7.7, 37C
0.13
Carbamoyl phosphate
-
pH 8.0, 37C
0.15
Carbamoyl phosphate
-
mutant K88R, pH 7.7, 37C
0.36
Carbamoyl phosphate
-
wild type
0.625
Carbamoyl phosphate
-
pH 8.5, 10 mM fixed substrate
0.9
Carbamoyl phosphate
-
pH 9.0, 30C
1
Carbamoyl phosphate
-
pH 9.0, 20C
1.1
Carbamoyl phosphate
-
pH 9.0, 5C
1.24
Carbamoyl phosphate
-
mutant K88Q, pH 7.7, 37C
0.033
Carbamoylphosphate
-
37C, pH 8.6
0.087
Carbamoylphosphate
-
37C, pH 8.2
0.25
Carbamoylphosphate
-
37C, pH 9.0
43.5
Diaminobutane
-
pH 8.5, 37C
10.4
L-citrulline
-
pH 8.0, 37C
25
L-lysine
-
pH 8.5, 37C
0.001
L-ornithine
-
liver enzyme, presence of putrescine, pH 7.0
0.00232
L-ornithine
-
liver enzyme, pH 7.0
0.0285
L-ornithine
pH 8.0, 37C
0.05
L-ornithine
-
mutant K268A, pH 8.0, 30C
0.11
L-ornithine
-
pH 8.0, 37C
0.25
L-ornithine
-
37C, pH 8.6
0.33
L-ornithine
-
37C, pH 8.2
0.36
L-ornithine
-
wild-type, pH 7.7, 37C
0.42
L-ornithine
-
mutant K88R, pH 7.7, 37C
0.45
L-ornithine
-
37C, pH 9.0
0.55
L-ornithine
-
mutant K88Q, pH 7.7, 37C
1
L-ornithine
-
mutant K260A, pH 8.0, 30C
1.1
L-ornithine
-
pH 8.5, 37C
1.1
L-ornithine
-
mutant K265R, pH 8.0, 30C; mutant K268R, pH 8.0, 30C
1.2
L-ornithine
-
mutant E256Q, pH 8.0, 30C; mutant K260R, pH 8.0, 30C; mutant K265A, pH 8.0, 30C
1.3
L-ornithine
-
mutant Q294P, pH 8.0, 30C
1.6
L-ornithine
-
wild-type, pH 8.0, 30C
1.78
L-ornithine
-
pH 9.0, 5C
2
L-ornithine
-
mutant L290Q, pH 8.0, 30C; mutant L290S, pH 8.0, 30C
2.1
L-ornithine
-
mutant E123S, pH 8.0, 30C
2.6
L-ornithine
-
mutant E123A, pH 8.0, 30C
2.8
L-ornithine
-
mutant C191M/C194N/F197V, pH 8.0, 30C
3.34
L-ornithine
-
pH 9.0, 10C
3.4
L-ornithine
-
mutant T68G, pH 8.0, 30C
5.67
L-ornithine
-
pH 9.0, 15C
8
L-ornithine
-
pH 9.0, 20C
10
L-ornithine
-
mutant E256A, pH 8.0, 30C; mutant K289S, pH 8.0, 30C
20
L-ornithine
-
mutant K263R, pH 8.0, 30C
22.49
L-ornithine
-
pH 9.0, 25C
30
L-ornithine
-
mutant K263A, pH 8.0, 30C
32
L-ornithine
recombinant enzyme mutant Y230V/G231S/L232M/Y233G, pH 8.5, 37C
34
L-ornithine
-
mutant N184Q, pH 8.0, 30C
36.4
L-ornithine
recombinant wild-type enzyme, pH 8.5, 37C
45
L-ornithine
-
pH 9.0, 30C
49
L-ornithine
-
mutant D182N, pH 8.0, 30C
350
L-ornithine
-
mutant N185Q, pH 8.0, 30C
0.8
ornithine
-
wild type, pH 7.25
0.85
ornithine
-
-
0.85
ornithine
-
pH 8.5, 10 mM fixed substrate
1.8
ornithine
-
mutant arcB6254, pH 7.25
1.85
ornithine
-
mutant arcB6240, pH 7.25
2.3
phosphate
-
pH 8.0, 37C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
82
Carbamoyl phosphate
Giardia intestinalis
-
pH 8.0, 37C
0.025
Diaminobutane
Pseudomonas savastanoi
-
pH 8.5, 37C
8.1
L-citrulline
Giardia intestinalis
-
pH 8.0, 37C
90
L-citrulline
Enterococcus faecalis
-
-
0.0036
L-lysine
Pseudomonas savastanoi
-
pH 8.5, 37C
49
L-ornithine
Pseudomonas savastanoi
-
pH 8.5, 37C
94.2
L-ornithine
Giardia intestinalis
-
pH 8.0, 37C
235
L-ornithine
Moritella abyssi
-
pH 9.0, 5C
382
L-ornithine
Moritella abyssi
-
pH 9.0, 10C
546
L-ornithine
Moritella abyssi
-
pH 9.0, 15C
690
L-ornithine
Moritella abyssi
-
pH 9.0, 30C
694
L-ornithine
Moritella abyssi
-
pH 9.0, 20C
750
L-ornithine
Moritella abyssi
-
pH 9.0, 25C
18
ornithine
Alnus glutinosa
-
-
187
ornithine
Bos taurus
-
-
370
ornithine
Pyrococcus furiosus
-
at 30C
500
ornithine
Pyrococcus furiosus
-
at 55C
2200
ornithine
Pyrococcus furiosus
-
Y227C/E277G double mutant, at 30C
2900
ornithine
Pyrococcus furiosus
-
A240D/E277G double mutant, at 30C
3400
ornithine
Enterococcus faecalis
-
-
3500
ornithine
Pyrococcus furiosus
-
Y227C/E277G double mutant, at 55C
4300
ornithine
Pyrococcus furiosus
-
A240D/E277G double mutant, at 55C
7.9
phosphate
Giardia intestinalis
-
pH 8.0, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
650000
Carbamoyl phosphate
Giardia intestinalis
-
pH 8.0, 37C
440
780
L-citrulline
Giardia intestinalis
-
pH 8.0, 37C
938
880000
L-ornithine
Giardia intestinalis
-
pH 8.0, 37C
192
3400
phosphate
Giardia intestinalis
-
pH 8.0, 37C
16
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7
2,4-diaminobutyrate
-
-
8.2
arginine
-
determined in the presence of 0.5 mM ornithine and 0.5 mM carbamoylphosphate
0.012
Carbamoyl phosphate
-
at 25C and pH 8.4
0.151
Carbamoyl phosphate
-
pH 8.5, 37C
0.00001
delta-N-(phosphonacetyl)-L-ornithine
-
-
0.000025
delta-N-(phosphonacetyl)-L-ornithine
-
pH 8.0, 37C
0.27
delta-N-(phosphonoacetyl)-L-ornithine
-
at 30C and pH 7.4, competitive vs. carbamoyl phosphate, noncompetitive vs. ornithine
0.0000047
Delta-N-Phosphonoacetyl-L-ornithine
-
at pH 8.5
0.000007
Delta-N-Phosphonoacetyl-L-ornithine
-
at pH 7.2
0.00013
Delta-N-Phosphonoacetyl-L-ornithine
-
-
0.00025
Delta-N-Phosphonoacetyl-L-ornithine
-
-
0.01
Delta-N-Phosphonoacetyl-L-ornithine
-
-
0.0115
Delta-N-Phosphonoacetyl-L-ornithine
-
pH 9.0, 20C
1.1
diaminobutyric acid
-
pH 8.5, 37C
15
glycine
-
-
13
L-alanine
-
-
0.58
L-alpha-aminobutyrate
-
-
110
L-asparagine
-
-
40
L-histidin
-
-
10.5
L-isoleucine
-
-
14
L-isoleucine
-
-
1.2
L-leucine
-
-
5.5
L-leucine
-
-
40
L-methionine
-
-
0.071
L-norvaline
-
-
0.4
L-norvaline
-
-
1.7
L-norvaline
-
pH 8.5, 37C
1.9
L-ornithine
-
pH 8.5, 37C
63.5
L-serine
-
-
12.5
L-valine
-
-
0.0002
N-delta-(phosphosulfamyl)ornithylalanylhomoarginine
-
mixed or competitive vs. carbamoyl phosphate
0.0009
N-delta-(phosphosulfamyl)ornithylalanylhomoarginine
-
noncompetitive vs. ornithine
0.06
ornithine
-
-
1.7
ornithine
-
at 2 mM carbamoyl phosphate
3.6
ornithine
-
at 10 mM carbamoyl phosphate
0.25
phosphate
-
-
1.1 - 1.3
phosphate
-
chloroplast enzyme
3.8
phosphate
-
pH 8.5, 37C
8
phosphate
-
at 25C and pH 7.1
0.01
phosphonacetyl-L-ornithine
-
between pH 7.5-9.0
-
13.5
L-valine
-
-
additional information
additional information
-
Ki for norvaline varies with pH, carbamoyl phosphate or phosphate concentration
-
additional information
additional information
-
approximate Ki of 1.0-2.0 mM for phosphate in permeabilized mitochondria
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00058
-
crude cell extract
0.0657
-
purified enzyme
0.0928
-
isoenzyme 2 with ornithine
0.12
-
catabolic reaction, pH 5.0-6.0, 37C
0.12
-
pH 8.0, 55C, activity in cell culture in growth medium with 0.2% yeast extract
0.255
-
pH 8.0, 55C, activity in cell culture in minimal growth medium with 20 mM glucose and 5 mM NH4+
0.43
-
pH 8.0, 55C, activity in cell culture in growth medium with 0.5% peptone and 0.1% yeast extract
0.47
-
multifunctional enzyme
0.574
-
isoenzyme 1 with canaline
1.24
-
isoenzyme 2 with canaline
1.28
-
mutant T68G, pH 8.0, 30C
2.33
-
extracts prepared from Escherichia coli CM236 carrying pME178
2.83
-
mutant K289S, pH 8.0, 30C
3.33
-
recombinant enzyme
3.59
-
anabolic reaction, pH 10.0, 37C
4.16
-
mutant C191M/C194N/F197V, pH 8.0, 30C
4.66
-
mutant L290S, pH 8.0, 30C
5.56
-
isoenzyme 1
7.5
-
mutant K263A, pH 8.0, 30C
8.31
-
isoenzyme 1 with ornithine
12.33
-
mutant N184Q, pH 8.0, 30C
12.66
-
mutant E256Q, pH 8.0, 30C
12.67
-
pH 7.5, crude cell exstract
13.3
-
mutant L290Q, pH 8.0, 30C
14.83
-
mutant K263R, pH 8.0, 30C
15
-
mutant E256A, pH 8.0, 30C
16.16
-
mutant D182N, pH 8.0, 30C
16.83
-
mutant K265A, pH 8.0, 30C
23.38
-
mutant E123S, pH 8.0, 30C
23.63
-
mutant K265R, pH 8.0, 30C
24
recombinant wild-type enzyme, substrate L-ornithine, pH 8.5, 37C
25
-
mutant K268A, pH 8.0, 30C; mutant N185Q, pH 8.0, 30C
25.16
-
mutant K260R, pH 8.0, 30C
25.3
-
mutant E123A, pH 8.0, 30C
25.73
-
mutant K268R, pH 8.0, 30C
25.83
-
mutant K260A, pH 8.0, 30C
26.12
-
wild-type, pH 8.0, 30C
26.4
-
-
40.2
-
recombinant enzyme
48.66
-
mutant Q294P, pH 8.0, 30C
82
recombinant enzyme mutant Y230V/G231S/L232M/Y233G, substrate L-ornithine, pH 8.5, 37C
83.3
-
enzyme from a liver of a Reye's syndrome patient
86.5
-
enzyme from normal liver
157.8
-
-
250 - 260
-
-
450
-
pH 7.5, purified enzyme
780
-
-
additional information
highest activity at 4 M KCl
additional information
-
enzyme activity during mechanical jaundice in the rat model
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
-
catabolic reaction
6.7
-
in potassium phosphate buffer 5 mM ornithine, pH optimum shifts to more alkaline values with decreasing ornithine concentrations
7
-
ornithine synthesis
7
-
enzyme 2
7.1
-
ornithine synthesis
7.2
-
at 10 mM carbamoyl phosphate, sharp decrease of activity above
7.25
-
wild type
7.3
-
catabolic ornithine carbamoyltransferase
7.4
-
assay at
7.5
-
half-maximal activity at pH 9.0
7.5
-
in triethanolamine-HCl
7.6
-
triethanolamine/acetate buffer
7.7
-
triethanolamine buffer, 85% of maximal activity at pH 8.5, 25% of maximal activity at pH 6.8
7.9
-
HEPES/NaOH buffer
8
-
sharp decrease in activity between pH 8.4 and 8.8
8
-
gradual loss of activity above pH 8.5 or below pH 6.5
8
-
at an ornithine concentration around the Km value, at higher concetration the pH optimum shifts to pH 7.0
8
-
with canaline
8.2
-
at 10 mM ornithine
8.2
-
mutant arcB6240
8.2
-
strain PAO524
8.3
-
bicine-NaOH buffer
8.4
-
phaseolotoxin insensitive isoform 2
8.4 - 8.8
-
-
8.5
-
-
8.5
-
citrulline synthesis
8.5
-
citrulline synthesis
8.5
-
with ornithine
8.5
-
mutant arcB6254
8.5
-
in 50 mM EDTA/NaOH buffer
8.5 - 9.5
-
phaseolotoxin sensitive isoform 1
8.6
-
at 0.025 mM ornithine
8.8
30% of maximal activity at pH 7.0
9
-
enzyme 1
9.5
-
citrulline synthesis
10
-
anabolic reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
-
activity range, anabolic and catabolic reactions
6 - 7.2
-
at 10 mM carbamoyl phosphate, sharp decrease in activity above
6 - 8.3
-
approx. 50% of maximal activity at pH 6.0
6.7 - 8.5
-
approx. 50% of maximal activity at pH 6.7 and 8.5, triethanolamine/acetate buffer
6.8 - 8.5
-
approx. 85% of maximal activity at pH 6.8, approx. 25% of maximal activity at pH 8.5
7 - 10
-
sharp decrease in activity below pH 9.0
7 - 9
-
50% of maximal activity at pH 9.0, 70% at pH 7.0
7.2 - 8.3
-
71% of maximal activity at pH 7.2, 94% of maximal activity at pH 8.3, HEPES/NaOH buffer
7.5 - 10
-
nearly constant activity in this range, half-maximal activity at pH 7.0, negliable activity at pH 6.0
7.5 - 9
-
approx. 50% of maximal activity at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 45
-
-
37
-
assay at
38 - 40
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23 - 25
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
i.e. a larval salmonid that has hatched but has not fully absorbed its yolk sac
Manually annotated by BRENDA team
-
enzyme activity during mechanical jaundice in the rat model, overview
Manually annotated by BRENDA team
-
high content
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
-
serum level of the enzyme, leakage and clearance, is influenced by the activation state of Kupffer cells, overview
Manually annotated by BRENDA team
additional information
-
ornthine carbamoyltransferase is present in all developmental phases
Manually annotated by BRENDA team
additional information
two major transcripts, OTC-t1 and OTC-t2, are more highly expressed than any of the other isoforms in all the tissues analyzed
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Arundinaria sp.
-
2 enzyme forms in sugar cane: cytoplasmic and mitochondrial
Manually annotated by BRENDA team
-
serum, from leakage of liver
-
Manually annotated by BRENDA team
Arundinaria sp.
-
2 enzyme forms in sugar cane: cytoplasmic and mitochondrial
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Brucella melitensis biotype 2 (strain ATCC 23457)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Coccidioides immitis (strain RS)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Gloeobacter violaceus (strain PCC 7421)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycoplasma penetrans (strain HF-2)
Mycoplasma penetrans (strain HF-2)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio vulnificus (strain CMCP6)
Vibrio vulnificus (strain CMCP6)
Vibrio vulnificus (strain CMCP6)
Vibrio vulnificus (strain CMCP6)
Vibrio vulnificus (strain CMCP6)
Vibrio vulnificus (strain CMCP6)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38000
-
-
719326
56000
-
multifunctional enzyme with agmatine iminohydrolase, putrescine carbamoyltransferase, ornithine carbamoyltransferase and carbamate kinase activity, gel filtration
209399
75000
-
-
485896
77600
-
gel filtration
485906
79000
Arundinaria sp.
-
cytoplasmic form
485895
87000
-
gel filtration
485907
90000
-
dimeric aggregation state, sucrose density gradient centrifugation
485921
90000
-
gel filtration
701115
95000
-
gel filtration
485920
98000
-
sedimentation equilibrium
485912
102000
-
gel filtration
660046
105000
-
-
485898
107000
-
gel filtration, sedimentation equilibrium
485928
108000
-
sedimentation equilibrium measurement
485890
108000
-
high performance hydrophobic interaction chromatography
485917
108200
-
gel filtration
485903
109000
-
-
485935
109000
-
gel filtration
485935
109000
-
-
485941
110000
-
gel filtration
485904
110000
-
gel filtration
485915
110000
-
SDS-PAGE of dimethyl suberimidate cross-linked enzyme
485918
110000
-
gel filtration
485919
110000
-
equilibrium sedimentation
485925
110000
-
gel filtration
485926
110000
-
gel filtration
485934
110000
-
gel filtration
666362
112000
-
sedimentation equilibrium analysis
485923
112000
-
gel filtration
485945
113000
-
gel filtration
485922
114000
-
gel filtration, glycerol density gradient centrifugation
485927
115000
-
gel filtration
485918
116000
-
-
485893
116000
-
sucrose density gradient ultracentrifugation
485911
118000
-
gel filtration
485946
120300
trimeric enzyme, gel filtration
720853
125000
-
gel filtration
485899
125000
-
gel filtration
665351
158000
-
gel filtration
485916
167000
-
tetrameric aggregation state, sucrose density gradient centrifugation
485921
200000
-
gradient PAGE
485913
200000
gel filtration
485930
223000
-
sedimentation equilibrium measurement
485890
224000
Arundinaria sp.
-
mitochondrial enzyme
485895
230000
hexameric enzyme, gel filtration
720853
230600
gel filtration
699590
236000
-
hexameric aggregation state, sucrose density gradient centrifugation
485921
240000
-
gel filtration
690247
260000
-
gel filtration
485921
400000
-
gel filtration
485932
420000
-
gel filtration
485929, 664807
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 35000, SDS-PAGE
?
-
x * 40000, enzyme may be a dimer, SDS-PAGE
?
-
x * 44000, SDS-PAGE, enzyme exists as a mixture of dimeric, tetrameric and hexameric forms, enzyme is converted to a dimer in presence of 2-mercaptoethanol
?
-
x * 57148, deduced from nucleotide sequence
?
Bacillus subtilis 168
-
x * 44000, SDS-PAGE, enzyme exists as a mixture of dimeric, tetrameric and hexameric forms, enzyme is converted to a dimer in presence of 2-mercaptoethanol
-
dodecamer
-
12 * 38000, SDS-PAGE
dodecamer
-
four catalytic trimers disposed in a tetrahedral manner, crystallization data
dodecamer
-
-
dodecamer
-
X-ray diffraction
hexamer
-
6 * 39600, SDS-PAGE
hexamer
6 * 32000, deduced from nucleotide sequence
hexamer
-
6 * 40000, recombinant enzyme, calculated from the deduced amino acid sequence
hexamer
-
crystal structure analysis, possibly a crystallization artifact
hexamer
6 * 40000, SDS-PAGE
hexamer
two trimer structure
hexamer
Lactobacillus hilgardii CETC4786T
-
6 * 40000, recombinant enzyme, calculated from the deduced amino acid sequence
-
trimer
-
3 * 37800, SDS-PAGE
trimer
-
3 * 35000, SDS-PAGE
trimer
-
3 * 37500, SDS-PAGE
trimer
-
3 * 36500, SDS-PAGE
trimer
-
3 * 35300, SDS-PAGE
trimer
-
3 * 36500, SDS-PAGE
trimer
-
3 * 37000, SDS-PAGE
trimer
-
3 * 36000, SDs-PAGE
trimer
-
3 * 37500, SDS-PAGE
trimer
-
3 * 38000, SDS-PAGE
trimer
-
3 * 39600, SDS-PAGE, sedimentation equilibrium analysis in 6 M guanidine-HCl; 3 * 39900, amino acid sequence
trimer
-
3 * 37000, SDS-PAGE
trimer
-
3 * 36500, SDS-PAGE
trimer
-
SDS-PAGE under reducing conditions
trimer
-
3 * 37000, SDS-PAGE
trimer
-
3 * 36000, SDs-PAGE
trimer
-
3 * 36000, SDs-PAGE
trimer
-
3 * 36000, SDs-PAGE
trimer
-
3 * 38000, SDS-PAGE
trimer
-
3 * 40000, SDS-PAGE
trimer
-
3 * 34000, SDS-PAGE
trimer
-
3 * 40000, aggregating to form nonamers or dodecamers, SDS-PAGE
trimer
-
3 * 36000, SDs-PAGE
trimer
-
crystal structure determination
trimer
-
3 * 38000, PAGE
trimer
-
3 * 33000, crystal structure analysis
trimer
-
3 * 36494, calculated
trimer
forms a head-to-head pseudohexamer in the asymmetric unit, each monomer is composed of an N-terminal CP-binding domain and a C-terminal ORN-binding domain joined by two interdomain helices. Conformation of the B2-H3 loop, residues 68-78, is involved in binding CP in an adjacent subunit of the trimer, overview
trimer
-
-
trimer
Campylobacter jejuni NCTC11168
-
forms a head-to-head pseudohexamer in the asymmetric unit, each monomer is composed of an N-terminal CP-binding domain and a C-terminal ORN-binding domain joined by two interdomain helices. Conformation of the B2-H3 loop, residues 68-78, is involved in binding CP in an adjacent subunit of the trimer, overview
-
trimer
Pseudomonas aeruginosa PAO
-
3 * 36000, SDs-PAGE
-
monomer
-
1 * 55000, multifunctional enzyme, SDS-PAGE
additional information
-
structural properties
additional information
-
in presence of up to 1 M Nacl, amount of dodecamer increases
additional information
-
in presence of ornitthine and arginine, enzyme forms a complex with arginase of 200 kDa
additional information
presence or absence of supratrimeric oligomerization, structure comparison and analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
ornithine carbamoyltransferase is acetylated at lysine residues, 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. K88 acetylation is regulated by both extracellular glucose and amino acid availabilit
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
unliganded aOTC, hanging drop vapor diffusion method, mixing of 500 nl 10 mg/ml protein solution with 500 nl well solution containing 25% PEG 3350, 0.2 M NaCl, 0.1 M HEPES, pH 8.0, room temperature, 1 week, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement and modeling
purified full-length enzyme or in complex with inhibitors N-(phosphonoacetyl)-putrescine or N-(phosphonoacetyl)-L-ornithine, and trunacted enzyme in complex with N-(phosphonoacetyl)-L-ornithine, hanging drop vapor diffusion technique, mixing of 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5 containing 0.43 mM ligand with 0.001 ml of crystallization solution composed of 125 mM (NH4)2SO4, 17% PEG 3350, 0.1 M Bis-Tris, pH 5.5, 21C, X-ray diffraction structure determination and analysis at 2.5 A, 2.0 A, and 1.59 A resolution, respectively, modeling
ornithine carbamoyltransferase-Ndelta-(N'-sulfodiaminophosphinyl)-L-ornithine complex, hanging-drop vapour diffusion, equal volumes of protein are combined with a solution containing 17.8% polyethylene glycol 8000 and 2.2% polyethylene glycol 1000, pyramidal crystals after 1-2 weeks
one protein molecule per asymmetric unit, trimeric structure
-
complexed with the bisubstrate analog N-phosphoacetyl-L-ornithine
-
ornithine transcarbamoylase-carbamoylphosphate complex, X-ray structure at 2.4-2.6 A resolution
-
hanging drop vapor diffusion method
-
to 2.1 A resolution. enzyme forms a homohexamer with 32 point group symmetry. The C-terminal end from each subunit constitutes a key structural element for the stabilization of the hexameric assembly in solution
hanging drop vapor diffusion method, crystal structures of Mtb OTC in orthorhombic and hexagonal form hexagonal form crystals complexed with carbamoyl phosphate and L-norvaline
-
crystal structure determination of the E105G mutant at 3.0 A resolution
-
T allosteric form, hanging-drop vapour diffusion against a reservoir solution containing 100 mM glycylglycin, pH 9, 12% polyethylene glycol 6000 and 1 mM dithiothreitol, X-ray analysis, 4.5 A resolution, R allosteric form, hanging-drop vapour diffusion against a reservoir solution containing 1.9 M ammonium sulfate, 50 mM HEPES, pH 7.2, 1 mM DTT, 1 mM EDTA, 3% polyethylene glycol 400 and 10 mM spermidine
-
dodecamer, four catalytic trimers disposed in a tetrahedral manner
-
hanging-drop vapor diffusion, 1/1 mixture of 12 mg/ml enzyme solution and a reservoir solution containing 1 M NaCl, 100 mM acetate buffer, pH 4.0, crystals are obtained after 7-10 days, X-ray structure at 2.7 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8 - 8.2
-
120 min, 37C, stable
485927
6.8 - 9
-
60 min, stable
485923
8.3
-
highest stability, bicine-NaOH buffer
485921
9
-
stable at low ionic strength, gradual loss of activity in 1 M KCl
485890
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-50 - 60
-
stable
485927
5
-
37% residual activity
659020
45
-
rapid inactivation above
485905
50
-
potassium phosphate pH 7.0, half-life 60 min, PIPES-NaOH pH 7.0, half-life 14 min, Tris-HCl, pH 7.5, half-life 9 min
659020
50
-
41 min, 50% residual activity
660046
51
-
R277W mutant enzyme, 50% loss of activity
485933
55
-
potassium phosphate pH 7.0, half-life 40 min, PIPES-NaOH pH 7.0, half-life 4.5 min, Tris-HCl, pH 7.5, half-life 3 min
659020
55
-
16 min, 50% residual activity
660046
56
-
recombinant enzyme, 50% loss of activity
485933
56
-
half-live: 99 min
485946
57
-
melting temperature, in absence and presence of carbamoyl phosphate
700959
58
-
half-life: 60 min
485946
60
-
half-life: 116 min
485945
60
-
potassium phosphate pH 7.0, half-life 2 min
659020
62.9
-
melting temperature
698036
63
-
presence of 20 mM carbamoylphosphate, 15 min, 50% residual activity; presence of 20 mM carbamoylphosphate plus 20 mM L-norvaline, stable; presence of 20 mM ornithine, 3 min, 50% residual activity
660046
64
-
half-life: 39 min
485945
64
-
half-life: 11 min
485946
64.9
-
melting temperature, presence of NaCl
698036
66
-
half-life: 10 min
485945
66.3
-
melting temperature, presence of ornithine
698036
67
-
half-life: 7 min
485945
67.2
-
melting temperature, presence of phosphate
698036
68
-
half-life: 5 min, 8 min with 500 mM KCl, 10 min with 10 mM citrulline, 20 min with 100 mM citrulline, 43 min with 20 mM phosphate, 48 min with 100 mM ornithine, 108 min with 100 mM phosphate, 120 min with 10 mM phosphate and 10 mM ornithine, 122 min with 10 mM phosphate and 100 mM citrulline, more than 200 min with 100 mM phosphate and 100 mM citrulline or with 10 mM phosphate and 100 mM ornithine
485898
68
-
half-life: 10.5 min, half-life increases to 45 min in the presence of 50 mM ornithine
485946
69.7
-
melting temperature, presence of sulfate
698036
70
-
half-life: 5 min
485945
70
-
melting temperature, presence of trehalose
698036
85
-
half-life: 18 min, 10 mM ornithine and phosphate increase half-life 5fold and 7fold respectively
485934
100
-
half-life, 30-40 min, presence of ornithine and/or phosphate protects
485932
additional information
-
extremely thermostable, result of strengthening of the intersubunit interactions in a trimer and oligomerization of trimers into dodecamer
657450
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in the presence of trehalose the enzyme is stabilized and it also inhibits the combined denaturation effect induced by urea and high temperature.Trehalose avoids the denaturation process through a process preserving the tertiary and secondary structures and it decreases the exposure of SH-group essential for enzymatic activity maintenance
-
unstable below 1 M KCl
cetyltrimethylammonium stabilizes enzyme in crude extract against heat inactivation in presence of the detergent
-
loss of activity after the second thawing
-
prolonged dialysis and freeze-thawing causes loss of activity
-
purified enzyme is highly unstable even in the presence of glycerol, dithiothreitol and Mg2+
-
1 mM carbamoyl phosphate or 20% glycerol stabilize the enzyme in cell-free extracts, a minimal enzyme concentration of 0.2 mg/ml is obligatory for stability
-
glycerol, 20% v/v, stabilizes during freeze-thawing
-
in Saccharomyces cerevisiae extracts the enzyme remains as stable as in Pyrococcus furiosus extracts
loss of activity by freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, protein concentration 1-2 mg/ml, several months, no loss of activity after repeated freezing and thawing
-
enzyme suspension in 3.0 M ammonium sulfate, pH 5.0, 3 years, no loss of activity
-
-80C, prolonged storage, no loss of activity
-
25C, high-salt solution, 1 year, no loss of activity
-20C, 20 mM Tris acetate, 2 mM EDTA, pH 7.4, 50% glycerol, no loss of activity
-
-20C, 50% glycerol, 10 mM potassium phosphate, pH 7.0, 1 mM 2-mercaptoethanol, 4 months, no loss of activity
-
-50C, indefinitely
-
4C, 48 h, complete loss of activity
-
-20C, 25 mM sodium phosphate, 10 mM carbamoylphosphate, 25 mM norvalien, pH 7.0, stable for months
-
-20C or 4C, no loss of activity
-
-70C, 2% loss of activity per month
-
-20C, 0.05 potassium phosphate buffer, pH 7.6, 1 month, no loss of activity
-
0-4C, 2 months, no loss of activity
-
-20C, several weeks, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sephacel, hydroxylapatite, preparative PAGE, isoenzyme 1
-
heat, ammonium sulfate, DEAE-cellulose, hydroxylapatite, DEAE-Sephacel, Bio-Gel A 1.5
-
ammonium sulfate
-
gene argF, expression of His-tagged aOTC in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
heat treatment, delta-N-(phosphonacetyl)-L-ornithine affinity chromatography
-
ammonium sulfate, streptomycin, DEAE-cellulose, heating, DEAE-Sephadex
-
heat, ammonium sulfate, DEAE-Sephadex, Sephadex G-200, aminohexyl-Sepharose
-
N-delta-(phosphonoacetyl)ornithine affinity chromatography, Sephadex G-100
-
recombinant enzyme
60-65C for 5 min, ammonium sulfate, DEAE-cellulose, Bio-Gel P-300
-
gel filtration, ammonium sulfate-mediated hydrophobic chromatography
enzyme from normal liver and liver of a Reye's syndrome patient, DEAE-cellulose, hydroxylapatite, Sephadex G-200
-
recombinant wild-type and R277W mutant enzyme, ammonium sulfate, delta-N-(phosphonacetyl)-L-ornithine affinity chromatography
-
recombinant protein using His-tag
-
putrescine synthase has inherent activities of agmatine iminohydrolase, putrescine carbamoyltransferase, ornithine carbamoyltransferase and carbamate kinase, ammonium sulfate, putrescine-Sepharose affinity column
-
DEAE-cellulose, isoelectric focusing
-
ammonium sulfate, 70C for 25 min, gel filtration, ion-exchange chromatography
-
delta-N-(phosphonoacetyl)-L-ornithine-Sepharose 6B affinity chromatography
-
partially purified
-
ammonium sulfate, DEAE-cellulose, isoforms 1 and 2
-
ammonium sulfate, heat treatment, celite, DEAE-Sephadex A-50, Sephacryl S-200, partial purification
-
single step procedure using delta-N-(phosphonoacetyl)-L-ornithine-Sepharose 6B affinity chromatography
-
isoforms 1 and 2
-
ammonium sulfate, DEAE-Sepharose, ornithine[AcPO(OH)2]-Sepharose
-
recombinant enzyme, Mono Q, arginine-Sepharose column
-
affinity chromatography on delta-N-(phosphonacetyl)-L-ornithine, Sephacryl S-200
-
high-performance hydrophobic interaction chromatography
-
native enzyme from liver mitochondria by anion exchange chromatography, ultrafiltration, and gel filtration, to about 50% purity
-
ammonium sulfate, DEAE-Sephadex, Sephadex G-200
-
plasmid-containing enzyme-overproducing strain
-
protamine sulfate, ammonium sulfate, diethylaminoethyl-cellulose, Sephadex G-150, hydroxylapatite
-
ammonium sulfate, heat, activated charcoal, delta-N-(phosphonacetyl)-L-ornithine affinity chromatography
-
DEAE-Sephadex, hydoxyapatite C, delta-N-(phosphonacetyl)-L-ornithine affinity chromatography
-
ammonium sulfate, DEAE-cellulose, aminohexyl-agarose
-
immunoadsorbent column
-
ammonium sulfate, Sephacryl S-200, delta-N-phosphonoacetyl-L-ornithine affinity chromatography
-
recombinant enzyme, thermodenaturation at 85C, delta-N-(phosphonacetyl)-L-ornithine affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene argF, expression of His-tagged aOTC in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
expression of isoform 1 and 2 in Escherichia coli
-
enzyme protomer structure, overview
expression in Escherichia coli
-
expression in Escherichia coli
-
coexpression with GroES and GroEL in Escherichia coli
-
stable overexpression of arginase I and ornithine transcarbamylase in HepG2 cells using a eukaryotic dual gene expression vector pBudCE4.1, the co-expression improves ammonia detoxification of the cells, improvement of HepG2 cell function, overview
-
three different splicing isoforms, OTC-t1, OTC-t2, and OTC-t3, all three isoforms use a canonical AAUAAA hexamer that is predicted to fold into a hairpin secondary structure which might be exposed to the cleavage and polyadenylation specificity factor. In addition, the OTC-t1 and OTC-t2 transcripts display heterogeneity at the cleavage sites in a tissue-dependent manner. Secondary structure of the OTC mRNA polyA signals, overview
His-tag fusion protein expressed in Escherichia coli JM109(DE3) (pLys), recombinant protein is fully active
-
gene lmo0036, phylogenetic tree, quantitative real-time PCR expresion analysis at different acidic conditions, overview
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Pseudomonas aeruginosa
-
expression in Escherichia coli and in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae
-
expression of wild-type, Y227C, A240D, E277G, Y227C/E277G and A240D/E277G mutant enzyme in Saccharomyces cerevisiae
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
elevation in enzyme activity with increased duration of crowding is observed for all four ornithine-urea cycle enzymes examined, i.e. liver glutamine synthetase, carbamoyl phosphate synthetase III, ornithine carbamoyl transferase and arginase. By contrast, mRNA expression is variable for the ornithine-urea cycle enzymes. Results suggest that the activities of ornithine-urea cycle enzymes are better predictors for urea production than ornithine-urea cycle enzyme mRNA expression levels
-
threefold repression of enzyme formation by arginine
-
threefold repression of enzyme formation by arginine
Sulfolobus solfataricus P1
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H121R
-
isoform 2, 80% increase in ornithine dependent activity, 64% decrease in canaline-dependent activity
R54G
site-directed mutagenesis, inactive mutant, not exhibiting any PTC or OTC activity
Y230V/G231S/L232M/Y233G
engineering of the 230-loop of the enzyme, by replacing the sequence 230YGLY233 of the putrescine signature by its OTC counterpart VSMG, favors the use of ornithine and impairs that of putrescine
Q106E
-
mutant to study the carbamoyl phosphate cooperativity on the anabolic OTCase
K88Q
-
less than 1% of wild-type activity
E105G
-
no cooperativity towards carbamoyl phosphate, follows Michaelis-Menten kinetics
E105G
-
mutant blocked in the active R (relaxed) state
E106A
-
mutant arcB6240, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
E106G
-
mutant arcB6254, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
E106A
Pseudomonas aeruginosa PAO532
-
mutant arcB6240, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
-
A240D
-
10fold increase of Km at 55C
E277G
-
14fold increase of Km at 55C
Y227D
-
slight increase of Km at 55C
D182N
-
greatly reduced affinity for L-ornithine, no interaction with arginase
E123A
-
little change in activity, or in sensitivity to arginase
E123S
-
little change in activity, or in sensitivity to arginase
E256A
-
greatly reduced affinity for L-ornithine, impaired interaction with arginase
E256Q
-
greatly reduced affinity for L-ornithine, impaired interaction with arginase
G181R
-
no residual activity
K260A
-
important in mediating sensitivity to L-ornithine and arginase
K260R
-
important in mediating sensitivity to L-ornithine and arginase
K263R
-
important in mediating sensitivity to L-ornithine and arginase
K265A
-
important in mediating sensitivity to L-ornithine and arginase
K265R
-
important in mediating sensitivity to L-ornithine and arginase
K268A
-
important in mediating sensitivity to L-ornithine and arginase
K268R
-
important in mediating sensitivity to L-ornithine and arginase
K289S
-
greatly reduced affinity for L-ornithine, impaired interaction with arginase
L290Q
-
reduced activity, little change in sensitivity to arginase
L290S
-
reduced activity, little change in sensitivity to arginase
N184Q
-
greatly reduced affinity for L-ornithine, impaired interaction with arginase
N185Q
-
greatly reduced affinity for L-ornithine, impaired interaction with arginase
Q294P
-
little change in activity, or in sensitivity to arginase
T68G
-
greatly reduced activity, no change in sensitivity to arginase
L118M
-
isoform 2, 515% increase in ornithine dependent activity, 54% decrease in canaline-dependent activity; isoform 2, 617% increase in ornithine dependent activity, 55% decrease in canaline-dependent activity
additional information
-
construction of the putrescine-producing strain PUT1 by deletion of argF, the gene for ornithine transcarbamoylase, and argR, encoding the L-arginine repressor, combined with heterologous expression of the Escherichia coli gene for L-ornithine decarboxylase SpeC. The strain requires supplementation of L-arginine and shows growth-decoupled putrescine production. By fine-tuning argF expression through modifications of the promoter, the translational start codon and/or the ribosome binding site, high productivity and titer can be obtained, optimization of putrescine production by mutant strains, overview
additional information
confirmation of decreased stability of the trimer of the enzyme lacking the C-terminal helix by deleting this helix
K88R
-
mutant retains substantial enzymatic activity
additional information
-
screening and analysis of naturally occuring mutations and polymorphisms in the OTC gene, defects in the OTC gene cause a block in ureagenesis resulting in hyperammonemia, which can lead to brain damage and death, phenotypes of mutated individuals, overview
additional information
-
computer model of molecular dynamic
R277W
-
shows no substrate inhibition by ornithine, 70fold lower affinity for L-ornithine
additional information
-
construction of a lmo0036 knockout mutant by homologous recombination using for in-frame deletion of the whole length of lmo0036
additional information
-
construction of a lmo0036 knockout mutant by homologous recombination using for in-frame deletion of the whole length of lmo0036
-
E106G
Pseudomonas aeruginosa PAO532
-
mutant arcB6254, with strongly reduced cooperativity for carbamoyl phosphate and anabolic activity
-
additional information
-
null mutant of argK encoding phaseolotoxin resistant isozyme, enzyme expression is independent of temperature and regulated directly by a compound resembling the inorganic moiety of phaseolotoxin
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
effect of pH and temperature on the rate of renaturation of guanidine-HCl dissociated enzyme, approx. 90% recovery at 25C and pH 7.0
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
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
medicine
-
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
-
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
-
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
-
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
-
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
-
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
-
analysis
-
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
diagnostics
-
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
medicine
-
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
-
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