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Information on EC 2.1.3.3 - ornithine carbamoyltransferase and Organism(s) Pyrococcus furiosus and UniProt Accession Q51742

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IUBMB Comments
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.
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Pyrococcus furiosus
UNIPROT: Q51742
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
oct, ornithine transcarbamylase, ornithine carbamoyltransferase, otcase, ornithine transcarbamoylase, carbamoyltransferase, ornithine carbamyl transferase, ornithine carbamyltransferase, catabolic ornithine carbamoyltransferase, rotcase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbamoyltransferase, ornithine
-
-
-
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carbamylphosphate-ornithine transcarbamylase
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-
-
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citrulline phosphorylase
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-
-
-
L-ornithine carbamoyltransferase
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-
-
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L-ornithine carbamyltransferase
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-
-
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L-ornithine transcarbamylase
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-
-
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ornithine carbamoyltransferase
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ornithine carbamyltransferase
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-
-
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ornithine transcarbamoylase
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-
-
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OTC
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbamoyl group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-69-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Delta-N-Phosphonoacetyl-L-ornithine
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
370 - 4300
ornithine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
Delta-N-Phosphonoacetyl-L-ornithine
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.43
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pH 8.0, 55°C, activity in cell culture in growth medium with 0.5% peptone and 0.1% yeast extract
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
at 55°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
400000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
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four catalytic trimers disposed in a tetrahedral manner, crystallization data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
dodecamer, four catalytic trimers disposed in a tetrahedral manner
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A240D
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10fold increase of Km at 55°C
E277G
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14fold increase of Km at 55°C
Y227D
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slight increase of Km at 55°C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
half-life, 30-40 min, presence of ornithine and/or phosphate protects
additional information
-
extremely thermostable, result of strengthening of the intersubunit interactions in a trimer and oligomerization of trimers into dodecamer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in Saccharomyces cerevisiae extracts the enzyme remains as stable as in Pyrococcus furiosus extracts
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-Sepharose, ornithine[AcPO(OH)2]-Sepharose
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recombinant enzyme, Mono Q, arginine-Sepharose column
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae
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expression of wild-type, Y227C, A240D, E277G, Y227C/E277G and A240D/E277G mutant enzyme in Saccharomyces cerevisiae
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
threefold repression of enzyme formation by arginine
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Legrain, C.; Villeret, V.; Roovers, M.; Gigot, D.; Dideberg, O.; Pierard, A.; Glansdorff, N.
Biochemical characterization of ornithine carbamoyltransferase from Pyrococcus furiosus
Eur. J. Biochem.
247
1046-1055
1997
Pyrococcus furiosus
Manually annotated by BRENDA team
Villeret, V.; Clantin, B.; Tricot, C.; Legrain, C.; Roovers, M.; Stalon, V.; Glansdorff, N.; Van Beeumen, J.
The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures
Proc. Natl. Acad. Sci. USA
95
2801-2806
1998
Pyrococcus furiosus
Manually annotated by BRENDA team
Roovers, M.; Sanchez, R.; Legrain, C.; Glansdorff, N.
Experimental evolution of enzyme temperature activity profile: selection in vivo and characterization of low-temperature-adapted mutants of Pyrococcus furiosus ornithine carbamoyltransferase
J. Bacteriol.
183
1101-1105
2001
Pyrococcus furiosus
Manually annotated by BRENDA team
Massant, J.; Wouters, J.; Glansdorff, N.
Refined structure of Pyrococcus furiosus ornithine carbamoyltransferase at 1.87 A
Acta Crystallogr. Sect. D
59
2140-2149
2003
Pyrococcus furiosus
Manually annotated by BRENDA team
Massant, J.; Glansdorff, N.
Metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus: dynamic enzyme-enzyme interactions involved in the formation of the channelling complex
Biochem. Soc. Trans.
32
306-309
2004
Pyrococcus furiosus
Manually annotated by BRENDA team
Roovers, M.; Hethke, C.; Legrain, C.; Thomm, M.; Glansdorff, N.
Isolation of the gene encoding Pyrococcus furiosus ornithine carbamoyltransferase and study of its expression profile in vivo and in vitro
Eur. J. Biochem.
247
1038-1045
1997
Pyrococcus furiosus (Q51742), Pyrococcus furiosus
Manually annotated by BRENDA team
Van de Casteele, M.; Demarez, M.; Legrain, C.; Glansdorff, N.; Pierard, A.
Pathways of arginine biosynthesis in extreme thermophilic archaeo- and eubacteria
J. Gen. Microbiol.
136
1177-1183
1990
Pyrococcus furiosus, Saccharolobus solfataricus, Saccharolobus solfataricus P1
-
Manually annotated by BRENDA team
Massant, J.; Verstreken, P.; Durbec, V.; Kholti, A.; Legrain, C.; Beeckmans, S.; Cornelis, P.; Glansdorff, N.
Metabolic channeling of carbamoyl phosphate, a thermolabile intermediate Evidence for physical interaction between carbamate kinase-like carbamoyl-phosphate synthetase and ornithine carbamoyltransferase from the hyperthermophile Pyrococcus furiosus
J. Biol. Chem.
277
18517-18522
2002
Pyrococcus furiosus (Q51742), Pyrococcus furiosus
Manually annotated by BRENDA team