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Information on EC 2.1.3.3 - ornithine carbamoyltransferase and Organism(s) Enterococcus faecalis and UniProt Accession Q837U7

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EC Tree
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:
Enterococcus faecalis
UNIPROT: Q837U7
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The taxonomic range for the selected organisms is: Enterococcus faecalis
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 transcarbamylase
-
carbamoyltransferase, ornithine
-
-
-
-
carbamylphosphate-ornithine transcarbamylase
-
-
-
-
citrulline phosphorylase
-
-
-
-
L-ornithine carbamoyltransferase
-
-
-
-
L-ornithine carbamyltransferase
-
-
-
-
L-ornithine transcarbamylase
-
-
-
-
ornithine carbamyltransferase
-
-
-
-
ornithine transcarbamoylase
-
-
-
-
OTC
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
show the reaction diagram
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
L-citrulline + phosphate
show the reaction diagram
-
-
-
r
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
carbamoyl phosphate + lysine
phosphate + homocitrulline
show the reaction diagram
-
at alkaline pH
-
?
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
-
-
?
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
L-citrulline + phosphate
show the reaction diagram
-
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
delta-N-(phosphonoacetyl)-L-ornithine
bisubstrate analogue inhibitor
2,4,6-Trinitrobenzenesulfonate
-
10 mM, almost complete inactivation
5,5'-dithiobis(2-nitrobenzoate)
5-hydroxy-2-aminovaleric acid
-
competitive vs. ornithine, uncompetitive vs. carbamoylphosphate
Acetylimidazole
-
50 mM, 95% inhibition at 25°C in 100 mM imidazole-HCl, pH 7.5
Carbamoyl phosphate
-
-
cystamine
-
complete inactivation, activity is completely recovered by incubation with 20 mM dithiothreitol
DL-2-Amino-5-hydroxypentanoic acid
-
-
iodoacetate
-
-
L-2,4-diaminobutyric acid
-
-
L-2-aminobutyrate
-
L-isomer
L-norleucine
-
-
L-norvaline
ornithine
-
at high concentrations
p-hydroxymercuribenzoate
-
inhibition is completely reversed by 2-mercaptoethanol
phosphate
additional information
-
effects of chemical modifications of specific residues on ligand binding and enzymatic activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
32 - 36.4
L-ornithine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
90
L-citrulline
-
-
3400
ornithine
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
Carbamoyl phosphate
-
at 25°C and pH 8.4
8
phosphate
-
at 25°C and pH 7.1
additional information
additional information
-
Ki for norvaline varies with pH, carbamoyl phosphate or phosphate concentration
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
recombinant wild-type enzyme, substrate L-ornithine, pH 8.5, 37°C
82
recombinant enzyme mutant Y230V/G231S/L232M/Y233G, substrate L-ornithine, pH 8.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
-
ornithine synthesis
8.5
-
citrulline synthesis
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the OTC activity of the enzyme is involved in arginine biosynthesis
additional information
sequence 230YGLY233 is the putrescine signature sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120300
trimeric enzyme, gel filtration
230000
hexameric enzyme, gel filtration
223000
-
sedimentation equilibrium measurement
39600
-
6 * 39600, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
two trimer structure
hexamer
-
6 * 39600, SDS-PAGE
additional information
presence or absence of supratrimeric oligomerization, structure comparison and analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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, 21°C, X-ray diffraction structure determination and analysis at 2.5 A, 2.0 A, and 1.59 A resolution, respectively, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
confirmation of decreased stability of the trimer of the enzyme lacking the C-terminal helix by deleting this helix
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
stable at low ionic strength, gradual loss of activity in 1 M KCl
485890
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme suspension in 3.0 M ammonium sulfate, pH 5.0, 3 years, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, streptomycin, DEAE-cellulose, heating, DEAE-Sephadex
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme protomer structure, overview
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
effect of pH and temperature on the rate of renaturation of guanidine-HCl dissociated enzyme, approx. 90% recovery at 25°C and pH 7.0
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Marshall, M.; Cohen, P.P.
Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure
J. Biol. Chem.
247
1641-1653
1972
Bos taurus, Enterococcus faecalis
Manually annotated by BRENDA team
Marshall, M.; Cohen, P.P.
Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for carbamyl-P and L-norvaline, correlation with steady state kinetics
J. Biol. Chem.
247
1654-1668
1972
Bos taurus, Enterococcus faecalis
Manually annotated by BRENDA team
Marshall, M.; Cohen, P.P.
Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. 3. Effects of chemical modifications of specific residues on ligand binding and enzymatic activity
J. Biol. Chem.
247
1669-1682
1972
Bos taurus, Enterococcus faecalis
Manually annotated by BRENDA team
Kurtin, W.E.; Bishop, S.H.; Himoe, A.
Ornithine transcarbamylase: steady-state kinetic properties
Biochem. Biophys. Res. Commun.
45
551-556
1971
Enterococcus faecalis
Manually annotated by BRENDA team
Marshall, M.; Cohen, P.P.
The essential sulfhydryl group of ornithine transcarbamylases. Reaction with anionic, aromatic disulfides and properties of its cyano derivative
J. Biol. Chem.
255
7291-7295
1980
Bos taurus, Enterococcus faecalis
Manually annotated by BRENDA team
Polo, L.M.; Gil-Ortiz, F.; Cantin, A.; Rubio, V.
New insight into the transcarbamylase family: the structure of putrescine transcarbamylase, a key catalyst for fermentative utilization of agmatine
PLoS ONE
7
e31528
2012
Enterococcus faecalis (Q837U7)
Manually annotated by BRENDA team