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Information on EC 2.1.3.3 - ornithine carbamoyltransferase and Organism(s) Pseudomonas aeruginosa

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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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Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
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
-
-
-
-
carbamylphosphate-ornithine transcarbamylase
-
-
-
-
citrulline phosphorylase
-
-
-
-
L-ornithine carbamoyltransferase
-
-
-
-
L-ornithine carbamyltransferase
-
-
-
-
L-ornithine transcarbamylase
-
-
-
-
ornithine carbamyltransferase
-
-
-
-
ornithine transcarbamoylase
-
-
-
-
OTC
-
-
-
-
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
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 + L-ornithine
phosphate + citrulline
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + L-citrulline
show the reaction diagram
-
catabolic ornithine carbamoyltransferase, catalyzes the reverse reaction, i.e. the cleavage of citrulline
-
?
phosphate + L-citrulline
carbamoylphosphate + L-ornithine
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-diaminobutane
-
10 mM; 10 mM, 45% inhibition
spermidine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
10 mM, 350% arsenolytic cleavage activity
arsenate
-
potent activator in the concentration range of 0-10 mM
CTP
-
10 mM, 340% arsenolytic cleavage activity
phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 1.85
ornithine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00058
-
crude cell extract
0.0657
-
purified enzyme
12.67
-
pH 7.5, crude cell exstract
2.33
-
extracts prepared from Escherichia coli CM236 carrying pME178
450
-
pH 7.5, purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
at 10 mM carbamoyl phosphate, sharp decrease of activity above
7.25
-
wild type
7.3
-
catabolic ornithine carbamoyltransferase
8.5
-
mutant arcB6254
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.2
-
at 10 mM carbamoyl phosphate, sharp decrease in activity above
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G2VNE0_PSEAI
305
0
33897
TrEMBL
-
A0A072ZJ66_PSEAI
336
0
38109
TrEMBL
-
A0A8G4ANY4_PSEAI
305
0
33955
TrEMBL
-
A0A8G2VUU5_PSEAI
336
0
38136
TrEMBL
-
A0A8G7LM40_PSEAI
305
0
33924
TrEMBL
-
A0A8G4KDY4_PSEAI
336
0
38110
TrEMBL
-
A0A8G7GGA2_PSEAI
305
0
33935
TrEMBL
-
A0A5K1SG09_PSEAI
305
0
33911
TrEMBL
-
A0A8G4E1A1_PSEAI
305
0
33909
TrEMBL
-
A0A8F9JG67_PSEAI
305
0
33953
TrEMBL
-
A0A6A9K723_PSEAI
305
0
33939
TrEMBL
-
A0A8G3W465_PSEAI
336
0
38075
TrEMBL
-
A0A4P0TGQ2_PSEAI
35
0
3999
TrEMBL
-
A0A8G2NK82_PSEAI
305
0
33911
TrEMBL
-
A0A8G7DAR5_PSEAI
336
0
38125
TrEMBL
-
A0A8G4A3Y8_PSEAI
336
0
38137
TrEMBL
-
A0A8F9JQQ5_PSEAI
305
0
33897
TrEMBL
-
A0A8G4E295_PSEAI
336
0
38137
TrEMBL
-
A0A3S0LCE8_PSEAI
305
0
33997
TrEMBL
-
A0A4P0TGU5_PSEAI
301
0
34177
TrEMBL
-
A0A8H0XCF2_PSEAI
305
0
33906
TrEMBL
-
A0A485HEG3_PSEAI
366
0
41494
TrEMBL
-
A0A072ZQU5_PSEAI
305
0
33925
TrEMBL
-
A0A071L264_PSEAI
336
0
38108
TrEMBL
-
A0A643ECM7_PSEAI
336
0
38081
TrEMBL
-
A0A8G4J5U4_PSEAI
305
0
33895
TrEMBL
-
A0A2R3IPM5_PSEAI
336
0
38124
TrEMBL
-
A0A8B5BM92_PSEAI
305
0
33911
TrEMBL
-
A0A8G3QDR1_PSEAI
336
0
38094
TrEMBL
-
A0A8G3UEE1_PSEAI
305
0
33867
TrEMBL
-
A0A8G3X3X3_PSEAI
305
0
33939
TrEMBL
-
A0A8G7N0J8_PSEAI
305
0
33983
TrEMBL
-
A0A2R3INL0_PSEAI
305
0
33979
TrEMBL
-
A0A8G6VNZ1_PSEAI
305
0
33951
TrEMBL
-
A0A8G4TL07_PSEAI
336
0
38108
TrEMBL
-
A0A8G6FAI9_PSEAI
336
0
38108
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
125000
-
gel filtration
36000
-
3 * 36000, SDs-PAGE
38000
-
12 * 38000, SDS-PAGE
40000
-
3 * 40000, aggregating to form nonamers or dodecamers, SDS-PAGE
420000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
trimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E105G
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Pseudomonas aeruginosa
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tricot, C.; Schmid, S.; Baur, H.; Villeret, V.; Dideberg, O.; Haas, D.; Stalon, V.
Catabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa. Changes of allosteric properties resulting from modifications at the C-terminus
Eur. J. Biochem.
221
555-561
1994
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Tricot, C.; Villeret, V.; Sainz, G.; Dideberg, O.; Stalon, V.
Allosteric regulation in Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase revisited: association of concerted homotropic cooperative interactions and local heterotropic effects
J. Mol. Biol.
283
695-704
1998
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Sainz, G.; Tricot, C.; Foray, M.F.; Marion, D.; Dideberg, O.; Stalon, V.
Kinetic studies of allosteric catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa
Eur. J. Biochem.
251
528-533
1998
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Sainz, G.; Vicat, J.; Kahn, R.; Tricot, C.; Stalon, V.; Dideberg, O.
Purification, crystallization and preliminary X-ray analysis of catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa
Acta Crystallogr. Sect. D
55
1591-1593
1999
Pseudomonas aeruginosa
-
Manually annotated by BRENDA team
Baur, H.; Stalon, V.; Falmagne, P.; Luethi, E.; Haas, D.
Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoyltransferases of Escherichia coli
Eur. J. Biochem.
166
111-117
1987
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Itoh, Y.; Soldati, L.; Stalon, V.; Falmagne, P.; Terawaki, Y.; Leisinger, T.; Haas, D.
Anabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa: nucleotide sequence and transcriptional control of the argF structural gene
J. Bacteriol.
170
2725-2734
1988
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO
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
Marcq, S.; Diaz-Ruano, A.; Charlier, P.; Dideberg, O.; Tricot, C.; Pierard, A.; Stalon, V.
Molecular size and symmetry of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase. An X-ray crystallography analysis
J. Mol. Biol.
220
9-12
1991
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Haas, D.; Evans, R.
Genetic and physiological characterization of Pseudomonas aeruginosa mutants affected in the catabolic ornithine carbamoyltransferase
J. Bacteriol.
139
713 - 720
1979
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Villeret, V.; Tricot, C.; Stalon, V.; Dideberg, O.
Crystal structure of Pseudomonas aeruginosa catabolic ornithine transcarbamoylase at 3.0-A resolution: a different oligomeric organization in the transcarbamoylase family
Proc. Natl. Acad. Sci. USA
92
10762-10766
1995
Pseudomonas aeruginosa
Manually annotated by BRENDA team