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Information on EC 2.1.3.3 - ornithine carbamoyltransferase and Organism(s) Escherichia coli and UniProt Accession P04391

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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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This record set is specific for:
Escherichia coli
UNIPROT: P04391
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The taxonomic range for the selected organisms is: Escherichia coli
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
ornithine transcarbamoylase
-
carbamoyltransferase, ornithine
-
-
-
-
carbamylphosphate-ornithine transcarbamylase
-
-
-
-
citrulline phosphorylase
-
-
-
-
L-ornithine carbamoyltransferase
-
-
-
-
L-ornithine carbamyltransferase
-
-
-
-
L-ornithine transcarbamylase
-
-
-
-
ornithine carbamyltransferase
-
-
-
-
ornithine transcarbamoylase
-
-
-
-
ornithine transcarbamylase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbamoyl group transfer
-
-
-
-
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
-
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 + citrulline
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
NATURAL SUBSTRATE
NATURAL 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
2,4-diaminobutyrate
-
-
arsenate
-
competitive vs. carbamoylphosphate, noncompetitive vs. ornithine
glycine
-
-
L-2,4-diaminobutyric acid
-
-
L-alanine
-
-
L-asparagine
-
weak
L-isoleucine
-
-
L-leucine
-
-
L-lysine
-
weak
L-norvaline
-
-
L-serine
-
weak
L-valine
-
-
methionine
-
L-isomer
N-delta-(phosphosulfamyl)ornithylalanylhomoarginine
-
trivial name phaseolotoxin, 0.1 mM, 93% inhibition
ornithine
phosphate
-
competitive vs. carbamoylphosphate, noncompetitive vs. ornithine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 1.4
Carbamoyl phosphate
0.33 - 17
L-ornithine
0.06 - 0.36
Carbamoyl phosphate
0.85
ornithine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48 - 410
Carbamoyl phosphate
0.7 - 460
L-ornithine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.4 - 1500
Carbamoyl phosphate
1.4 - 830
L-ornithine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7
2,4-diaminobutyrate
-
-
15
glycine
-
-
13
L-alanine
-
-
110
L-asparagine
-
-
14
L-isoleucine
-
-
5.5
L-leucine
-
-
40
L-methionine
-
-
0.4
L-norvaline
-
-
63.5
L-serine
-
-
13.5
L-valine
-
-
0.0002 - 0.0009
N-delta-(phosphosulfamyl)ornithylalanylhomoarginine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
gel filtration
35000
-
3 * 35000, SDS-PAGE
37500
-
3 * 37500, SDS-PAGE
95000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C273A
the mutant shows 2.8 and 3.2fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
D140N
the mutant shows 5.4 and 28fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
D231A
the mutant shows 450 and 580fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
E299D
the mutant shows 2.5 and 4.2fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
E299Q
the mutant shows 110 and 51fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
H272L
the mutant shows 310 and 120fold and decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
H272N
the mutant shows 4.2 and 3.4fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Q104L
the mutant shows 5.9 and 10fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
R57A
the mutant shows 57 and 44fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
S61A
the mutant shows 6.1 and 1.8fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y160F
the mutant shows 6.7 and 8.2fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y160S
the mutant shows 1.5 and 14fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y229F
the mutant shows 3.5 and 2.7fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Y229S
the mutant shows 1.7 and 1.4fold decrease of activity with respect to carbamoyl phosphate and L-ornithine, respectively, compared to the wild type enzyme
Q106E
-
mutant to study the carbamoyl phosphate cooperativity on the anabolic OTCase
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68
melting temperature of the apoenzyme
57
-
melting temperature, in absence and presence of carbamoyl phosphate
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, prolonged storage, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
recombinant enzyme
heat, ammonium sulfate, DEAE-Sephadex, Sephadex G-200, aminohexyl-Sepharose
-
N-delta-(phosphonoacetyl)ornithine affinity chromatography, Sephadex G-100
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) Tuner cells
expression in Escherichia coli
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Legrain, C.; Stalon, V.
Ornithine carbamoyltransferase from Escherichia coli W. Purification, structure and steady-state kinetic analysis
Eur. J. Biochem.
63
289-301
1976
Escherichia coli
Manually annotated by BRENDA team
Templeton, M.D.; Sullivan, P.A.; Sheperd, M.G.
The inhibition of ornithine transcarbamoylase from Escherichia coli W by phaseolotoxin
Biochem. J.
224
379-388
1984
Escherichia coli
Manually annotated by BRENDA team
Langley, D.B.; Templeton, M.D.; Fields, B.A.; Mitchell, R.E.; Collyer, C.A.
Mechanism of inactivation of ornithine transcarbamoylase by Nd-(N'-sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism
J. Biol. Chem.
275
20012-20019
2000
Escherichia coli (P04391), Escherichia coli
Manually annotated by BRENDA team
Baur, H.; Tricot, C.; Stalon, V.; Haas, D.
Converting catabolic ornithine carbamoyltransferase to an anabolic enzyme
J. Biol. Chem.
265
14728-14731
1990
Escherichia coli, Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO532
Manually annotated by BRENDA team
Wang, Q.; Xia, J.; Guallar, V.; Krilov, G.; Kantrowitz, E.R.
Mechanism of thermal decomposition of carbamoyl phosphate and its stabilization by aspartate and ornithine transcarbamoylases
Proc. Natl. Acad. Sci. USA
105
16918-16923
2008
Escherichia coli
Manually annotated by BRENDA team
Sriramoju, M.K.; Yang, T.J.; Hsu, S.D.
Comparative folding analyses of unknotted versus trefoil-knotted ornithine transcarbamylases suggest stabilizing effects of protein knots
Biochem. Biophys. Res. Commun.
503
822-829
2018
Escherichia coli
Manually annotated by BRENDA team
Ngu, L.; Winters, J.N.; Nguyen, K.; Ramos, K.E.; DeLateur, N.A.; Makowski, L.; Whitford, P.C.; Ondrechen, M.J.; Beuning, P.J.
Probing remote residues important for catalysis in Escherichia coli ornithine transcarbamoylase
PLoS ONE
15
e0228487
2020
Escherichia coli (P04391), Escherichia coli
Manually annotated by BRENDA team