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
2.1.3.6
-
RECOMMENDED NAME
GeneOntology No.
putrescine carbamoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
show the reaction diagram
multifunctional enzyme that catalyzes 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 and ornithine into putrescine and citrulline, respectively
-
carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
show the reaction diagram
multifunctional enzyme that catalyzes 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 and ornithine into putrescine and citrulline, respectively
-
carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
transfer of carbamoyl phosphate
-
-
-
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
anabolic putrescine carbamoyltransferase
-
-
catabolic putrescine carbamoyltransferase
-
-
PTC
Enterococcus faecalis SD10
-
-
-
PTCase
-
-
-
-
PTCase
Q837U7
-
PTCase
Enterococcus faecalis ATCC 33913D
Q837U7
-
-
putrescine carbamoyltransferase
-
-
putrescine synthase
-
-
-
-
putrescine transcarbamylase
-
-
-
-
putrescine transcarbamylase
-
-
putrescine transcarbamylase
Q837U7
-
putrescine transcarbamylase
Enterococcus faecalis SD10
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9076-55-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; strain SD10, gene ef0732
-
-
Manually annotated by BRENDA team
gene agcB
UniProt
Manually annotated by BRENDA team
strain 10C1
-
-
Manually annotated by BRENDA team
Enterococcus faecalis 10C1
strain 10C1
-
-
Manually annotated by BRENDA team
Enterococcus faecalis ATCC 33913D
gene agcB
UniProt
Manually annotated by BRENDA team
Enterococcus faecalis SD10
strain SD10, gene ef0732
-
-
Manually annotated by BRENDA team
gene lmo0036
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
absence of this enzyme impairs the growth of Listeria under mild acidic conditions at pH 4.8 and reduced its survival in synthetic human gastric fluid at pH 2.5, corresponding to a loss in ammonia production
malfunction
-
absence of this enzyme impairs the growth of Listeria under mild acidic conditions at pH 4.8 and reduced its survival in synthetic human gastric fluid at pH 2.5, corresponding to a loss in ammonia production
-
physiological function
-
Lmo0036 is responsible for acid tolerance at both sublethal and lethal pH levels and plays a possible role in Listeria virulence
physiological function
Q837U7
the enzyme generates carbamoyl phosphate for ATP production in the fermentative catabolism of agmatine
physiological function
-
Lmo0036 is responsible for acid tolerance at both sublethal and lethal pH levels and plays a possible role in Listeria virulence
-
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
additional information
Q837U7
sequence 230YGLY233 is the putrescine signature sequence
additional information
Q837U7
the C-terminal helix is essential for both formation of the functional trimer and catalytic activity, since truncated PTCase without the C-terminal helix aggregates and has only 3% of native catalytic activity. Active site structure, overview
additional information
Enterococcus faecalis ATCC 33913D
-
the C-terminal helix is essential for both formation of the functional trimer and catalytic activity, since truncated PTCase without the C-terminal helix aggregates and has only 3% of native catalytic activity. Active site structure, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arsenate + N-carbamoylputrescine
?
show the reaction diagram
-
-
-
-
?
arsenate + N-carbamoylputrescine
?
show the reaction diagram
-
-
-
-
-
arsenate + N-carbamoylputrescine
?
show the reaction diagram
Enterococcus faecalis, Enterococcus faecalis 10C1
-
carbamoyl arsenate as intermediate is not formed
-
-
ir
carbamoyl phosphate + 1,3-diaminopropane
phosphate + N1-carbamoyl-1,3-diaminopropane
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 + 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 + cadaverine
phosphate + N-carbamoylcadaverine
show the reaction diagram
-
-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
show the reaction diagram
Enterococcus faecalis, Enterococcus faecalis SD10
-
only weak activity with cadaverine a substrate
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
show the reaction diagram
Enterococcus faecalis, Enterococcus faecalis SD10
-
low activity, reaction of EC 2.1.3.3
-
-
?
carbamoyl phosphate + ornithine
phosphate + citrulline
show the reaction diagram
-
-
-
?
carbamoyl phosphate + ornithine
phosphate + N-carbamoylornithine
show the reaction diagram
-
only weak activity with ornithine as a substrate
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
-
-
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
Q837U7
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
Q837U7
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
Q837U7
substrate binding structures, overview
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
Enterococcus faecalis 10C1
-
-
-, phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
Enterococcus faecalis ATCC 33913D
Q837U7
-, substrate binding structures, overview
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
Enterococcus faecalis SD10
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
show the reaction diagram
Enterococcus faecalis, Enterococcus faecalis SD10
-
-
-
-
?
carbamoyl phosphate + spermidine
phosphate + N-carbamoylspermidine
show the reaction diagram
-
-
-
-
-
carbamoyl phosphate + spermidine
phosphate + N-carbamoylspermidine
show the reaction diagram
-
-
-
?
carbamoyl phosphate + spermine
phosphate + N-carbamoylspermine
show the reaction diagram
-
-
-
-
-
carbamoyl phosphate + spermine
phosphate + N-carbamoylspermine
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
-
-
-
additional information
?
-
-
Lmo0036 is an ornithine carbamoyltransferase, EC 2.1.3.3, and also a putrescine carbamoyltransferase, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
-
-
-
additional information
?
-
Q837U7
in addition to using putrescine, the enzyme can utilize L-ornithine as a poor substrate, see EC 2.1.3.3. Differences between the respective 230 and SMG loops of 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
-
-
-
additional information
?
-
-
Lmo0036 is an ornithine carbamoyltransferase, EC 2.1.3.3, and also a putrescine carbamoyltransferase, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
-
-
-
additional information
?
-
Enterococcus faecalis SD10
-
the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
show the reaction diagram
Enterococcus faecalis, Enterococcus faecalis SD10
-
low activity, reaction of EC 2.1.3.3
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
Q837U7
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
Q837U7
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
show the reaction diagram
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
Enterococcus faecalis 10C1
-
-
phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
Enterococcus faecalis ATCC 33913D
Q837U7
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
show the reaction diagram
-
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
show the reaction diagram
Enterococcus faecalis SD10
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
-
-
-
additional information
?
-
-
Lmo0036 is an ornithine carbamoyltransferase, EC 2.1.3.3, and also a putrescine carbamoyltransferase, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
-
-
-
additional information
?
-
Enterococcus faecalis SD10
-
the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4-aminobutyrate
-
-
arsenate
-
competitive vs. carbamoylphosphate
diphosphate
-
competitive vs. carbamoylphosphate
guanidobutyrate
-
-
N-(phosphonoacetyl)-putrescine
-
; i.e. PAPU, highly potent and selective inhibitor
N-(phosphonoacetyl)-putrescine
Q837U7
bisubstrate analogue inhibitor
phosphate
-
competitive vs. carbamoylphosphate
phosphonoacetyl-L-aspartate
-
-
phosphonoacetyl-L-ornithine
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.9
-
1,3-Diaminopropane
-
-
6.6
-
1,6-diaminohexane
-
-
4
-
arsenate
-
arsenolytic cleavage
7.7
-
cadaverine
-
-
0.058
-
Carbamoyl phosphate
-
-
0.101
-
Carbamoyl phosphate
Q837U7
pH and temperature not specified in the publication
10
-
N-Carbamoylputrescine
-
arsenolytic cleavage
0.0023
-
putrescine
-
-
-
0.02
-
putrescine
-
at pH 7.0
-
0.029
-
putrescine
-
-
-
0.136
-
putrescine
Q837U7
pH and temperature not specified in the publication
-
1.14
-
putrescine
Q837U7
recombinant wild-type PTC, pH 8.5, 37C
-
32.9
-
putrescine
Q837U7
recombinant PTC mutant Y230V/G231S/L232M/Y233G, pH 8.5, 37C
-
19.7
-
spermidine
-
-
0.35
-
spermine
-
-
0.17
-
Carbamoyl phosphate
-
at pH 7.0
additional information
-
additional information
Q837U7
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
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.06
-
diphosphate
-
-
0.00001
-
N-(phosphonoacetyl)-putrescine
-
recombinant enzyme
10
-
N-(phosphonoacetyl)-putrescine
-
-
6
-
phosphate
-
vs. carbamoylphosphate
8.5
-
phosphate
-
vs. putrescine
13.5
-
phosphate
-
vs. ornithine
2.5
-
spermidine
-
vs. putrescine
4.5
-
spermidine
-
vs. carbamoylphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.57
-
-
anabolic reaction, pH 8.0, 37C
1.13
-
Q837U7
recombinant PTC mutant Y230V/G231S/L232M/Y233G, substrate putrescine, pH 8.5, 37C
35.6
-
-
catabolic reaction, pH 5.0, 37C
460
-
-
non-recombinant enzyme from Enterococcus faecalis
597
-
-
recombinant enzyme from Enterococcus faecalis
813
-
Q837U7
recombinant wild-type PTC, substrate putrescine, pH 8.5, 37C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
catabolic reaction
6.7
-
-
in potassium 3,3-dimethylglutarate
7
9
-
at 10 mM putrescine and carbamoyl phosphate
7
-
-
in Tris-HCl
7
-
-
assay at
7.8
-
-
at at 0.5 mM putrescine and carbamyol phosphate
8
-
-
anabolic reaction
8.5
-
Q837U7
assay at
9
-
-
at 0.5 mM putrescine
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
6.5
-
activity range, catabolic reaction
4
11
-
activity range, anabolic reaction
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
37
-
Q837U7
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
-
gel filtration
56000
-
-
gel filtration
120300
-
Q837U7
trimeric PTC, gel filtration
140000
-
-
gel filtration
230000
-
Q837U7
hexameric PTC, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 150000, SDS-PAGE, nonreducing; x * 15000 + x * 18000 + x * 44000, SDS-PAGE, in the presence of 2-mercaptoethanol
hexamer
Q837U7
two trimer structure
trimer
-
3 * 40000, treatment with glutaraldehyde, SDS-PAGE
trimer
-
; crystal strucutre
trimer
Q837U7
PTCase also has a unique structural feature: a long C-terminal helix that interacts with the adjacent subunit to enhance intersubunit interactions in the molecular trimer. The C-terminal helix os essential for both formation of the functional trimer and catalytic activity, since truncated PTCase without the C-terminal helix aggregates and has only 3% of native catalytic activity
trimer
Enterococcus faecalis ATCC 33913D
-
PTCase also has a unique structural feature: a long C-terminal helix that interacts with the adjacent subunit to enhance intersubunit interactions in the molecular trimer. The C-terminal helix os essential for both formation of the functional trimer and catalytic activity, since truncated PTCase without the C-terminal helix aggregates and has only 3% of native catalytic activity
-
trimer
Enterococcus faecalis SD10
-
; crystal strucutre
-
monomer
-
1 * 55000, SDS-PAGE
additional information
Q837U7
presence or absence of supratrimeric oligomerization, structure comparison and analysis, overview
additional information
Q837U7
structure comparison, overview
additional information
Enterococcus faecalis ATCC 33913D
-
structure comparison, overview
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q837U7
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
Q837U7
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55
-
-
carbamoylphosphate, diphosphate, ornithine, 2,4-diaminobutyrate and norvaline protect against denaturation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 2.5 mg/ml, 50 mM potassium phosphate, pH 7.5, 3 years, no loss of activity
-
4C, 48 h, complete loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
65C, ammonium sulfate, DEAE-Sephadex, Sephadex G-200
-
ammonium sulfate, heat treatment, Sephadex G-100
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged protein from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and gel filtration
Q837U7
MnCl2, ammonium sulfate, putrescine-CH-Sepharose affinity column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
gene agcB, expression as His-tagged protein in Escherichia coli strain BL21(DE3)
Q837U7
PTC protomer structure, overview
Q837U7
gene lmo0036, phylogenetic tree, quantitative real-time PCR expresion analysis at different acidic conditions, overview
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
R54G
Q837U7
site-directed mutagenesis, inactive mutant, not exhibiting any PTC or OTC activity
additional information
Q837U7
confirmation of decreased stability of the trimer of PTC lacking the C-terminal helix by deleting this helix
Y230V/G231S/L232M/Y233G
Q837U7
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
-
construction of a lmo0036 knockout mutant by homologous recombination using for in-frame deletion of the whole length of lmo0036
additional information
-
construction of a lmo0036 knockout mutant by homologous recombination using for in-frame deletion of the whole length of lmo0036
-