Information on EC 2.1.3.6 - putrescine carbamoyltransferase

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

EC NUMBER
COMMENTARY hide
2.1.3.6
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RECOMMENDED NAME
GeneOntology No.
putrescine carbamoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transfer of carbamoyl phosphate
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-
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SYSTEMATIC NAME
IUBMB Comments
carbamoyl-phosphate:putrescine carbamoyltransferase
The plant enzyme also catalyses the reactions of EC 2.1.3.3 ornithine 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
9076-55-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
strain 10C1
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-
Manually annotated by BRENDA team
gene agcB
UniProt
Manually annotated by BRENDA team
strain SD10, gene ef0732
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-
Manually annotated by BRENDA team
gene lmo0036
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-
Manually annotated by BRENDA team
gene lmo0036
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arsenate + N-carbamoylputrescine
?
show the reaction diagram
carbamoyl phosphate + 1,3-diaminopropane
phosphate + N1-carbamoyl-1,3-diaminopropane
show the reaction diagram
carbamoyl phosphate + 1,6-diaminohexane
phosphate + N1-carbamoyl-1,6-diaminohexane
show the reaction diagram
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
show the reaction diagram
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
show the reaction diagram
carbamoyl phosphate + ornithine
phosphate + citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + ornithine
phosphate + N-carbamoylornithine
show the reaction diagram
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only weak activity with ornithine as a substrate
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-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
show the reaction diagram
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
carbamoyl phosphate + spermidine
phosphate + N-carbamoylspermidine
show the reaction diagram
carbamoyl phosphate + spermine
phosphate + N-carbamoylspermine
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + N-carbamoyl-L-ornithine
show the reaction diagram
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
show the reaction diagram
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-aminobutyrate
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arsenate
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competitive vs. carbamoylphosphate
diphosphate
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competitive vs. carbamoylphosphate
guanidobutyrate
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N-(phosphonoacetyl)-putrescine
phosphate
phosphonoacetyl-L-aspartate
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phosphonoacetyl-L-ornithine
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spermidine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9
1,3-Diaminopropane
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6.6
1,6-diaminohexane
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4
arsenate
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arsenolytic cleavage
7.7
cadaverine
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0.058 - 0.17
Carbamoyl phosphate
10
N-Carbamoylputrescine
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arsenolytic cleavage
13
ornithine
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0.0023 - 32.9
putrescine
19.7
spermidine
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0.35
spermine
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-
additional information
additional information
in contrast to other trimeric carbamoyltransferases, PTCase binds both carbamoyl phosphate and putrescine with Hill coefficients at saturating concentrations of the other substrate of 1.53 and 1.80, respectively
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12
arsenate
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0.06
diphosphate
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0.00001 - 10
N-(phosphonoacetyl)-putrescine
4 - 13.5
phosphate
2.5 - 4.5
spermidine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.57
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anabolic reaction, pH 8.0, 37C
1.13
recombinant PTC mutant Y230V/G231S/L232M/Y233G, substrate putrescine, pH 8.5, 37C
35.6
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catabolic reaction, pH 5.0, 37C
597
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recombinant enzyme from Enterococcus faecalis
813
recombinant wild-type PTC, substrate putrescine, pH 8.5, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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catabolic reaction
6.7
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in potassium 3,3-dimethylglutarate
7.8
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at at 0.5 mM putrescine and carbamyol phosphate
8
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anabolic reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 6.5
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activity range, catabolic reaction
4 - 11
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activity range, anabolic reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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gel filtration
56000
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gel filtration
120300
trimeric PTC, gel filtration
140000
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gel filtration
230000
hexameric PTC, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 150000, SDS-PAGE, nonreducing; x * 15000 + x * 18000 + x * 44000, SDS-PAGE, in the presence of 2-mercaptoethanol
hexamer
two trimer structure
monomer
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1 * 55000, SDS-PAGE
trimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified full-length PTC or in complex with inhibitors N-(phosphonoacetyl)-putrescine or N-(phosphonoacetyl)-L-ornithine, and trunacted PTC 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
purified His-tagged wild-type PTCase, from a solution containing 200 mM magnesium sulfate, 15-17% w/v PEG 3350, 100 mM Bis-tris, pH 5.5, soaking in mother liquor containing 25% v/v ethylene glycol for 1 min for cryoprotection, X-ray diffraction structure determination and analysis at 3.2 A resolution
purified recombinant enzyme in presence of inhibitor N-(phosphonoacetyl)-putrescine, X-ray diffraction structure determination and analysis at 3.0 A resolution; using the sparse-matrix sampling vapor-diffusion method. The addition of N-(phosphonoacetyl)-putrescine to the crystallization drop strongly improves the results of the crystallization
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
carbamoylphosphate, diphosphate, ornithine, 2,4-diaminobutyrate and norvaline protect against denaturation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly unstable even in the presence of glycerol, dithiothreitol and Mg2+, activity is stabilized in dilute solutions, less than 0.05 mg protein/ml for about 3-4 h at 37C by 0.25 mg/ml bovine serum albumine
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 2.5 mg/ml, 50 mM potassium phosphate, pH 7.5, 3 years, no loss of activity
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4C, 48 h, complete loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
65C, ammonium sulfate, DEAE-Sephadex, Sephadex G-200
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ammonium sulfate, heat treatment, Sephadex G-100
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MnCl2, ammonium sulfate, putrescine-CH-Sepharose affinity column
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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recombinant His-tagged protein from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli; gene ef0732, gene cluster organization, DNA and amino acid sequence determination and analysis, overexpression of His-tagged enzyme in Escherichia coli
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gene agcB, expression as His-tagged protein in Escherichia coli strain BL21(DE3)
gene lmo0036, phylogenetic tree, quantitative real-time PCR expresion analysis at different acidic conditions, overview
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PTC protomer structure, overview
ENGINEERING
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 PTC, 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
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