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Information on EC 2.1.3.6 - putrescine carbamoyltransferase
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2.1.3.6 putrescine carbamoyltransferaseIUBMB Comments
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.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
putrescine carbamoyltransferase, ptcase, putrescine transcarbamylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PTC
PTCase
putrescine synthase
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-
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putrescine transcarbamylase
PTCase
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-
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putrescine transcarbamylase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
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
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carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
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
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carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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.
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CAS REGISTRY NUMBER
COMMENTARY
9076-55-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + ornithine
phosphate + N-carbamoylornithine
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only weak activity with ornithine as a substrate
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?
arsenate + N-carbamoylputrescine
?
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carbamoyl arsenate as intermediate is not formed
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ir
arsenate + N-carbamoylputrescine
?
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carbamoyl arsenate as intermediate is not formed
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ir
carbamoyl phosphate + 1,3-diaminopropane
phosphate + N1-carbamoyl-1,3-diaminopropane
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-
-
?
carbamoyl phosphate + 1,3-diaminopropane
phosphate + N1-carbamoyl-1,3-diaminopropane
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-
-
-
?
carbamoyl phosphate + 1,6-diaminohexane
phosphate + N1-carbamoyl-1,6-diaminohexane
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-
-
?
carbamoyl phosphate + 1,6-diaminohexane
phosphate + N1-carbamoyl-1,6-diaminohexane
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-
-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
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-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
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-
-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
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only weak activity with cadaverine a substrate
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-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
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only weak activity with cadaverine a substrate
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-
?
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
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low activity, reaction of EC 2.1.3.3
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-
?
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
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low activity, reaction of EC 2.1.3.3
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-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
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-
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
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-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
substrate binding structures, overview
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
substrate binding structures, overview
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
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r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
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r
carbamoyl phosphate + spermidine
phosphate + N-carbamoylspermidine
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?
carbamoyl phosphate + spermidine
phosphate + N-carbamoylspermidine
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?
carbamoyl phosphate + spermine
phosphate + N-carbamoylspermine
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?
carbamoyl phosphate + spermine
phosphate + N-carbamoylspermine
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?
additional information
?
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the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
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?
additional information
?
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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
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?
additional information
?
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the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
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?
additional information
?
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Lmo0036 is an ornithine carbamoyltransferase, EC 2.1.3.3, and also a putrescine carbamoyltransferase, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
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?
additional information
?
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Lmo0036 is an ornithine carbamoyltransferase, EC 2.1.3.3, and also a putrescine carbamoyltransferase, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
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low activity, reaction of EC 2.1.3.3
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?
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
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low activity, reaction of EC 2.1.3.3
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
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-
-
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
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-
-
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
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r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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-
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r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
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r
additional information
?
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the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
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?
additional information
?
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-
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
-
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?
additional information
?
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Lmo0036 is an ornithine carbamoyltransferase, EC 2.1.3.3, and also a putrescine carbamoyltransferase, catalysing reversible ornithine and putrescine carbamoyltransfer reactions
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?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-(phosphonoacetyl)-putrescine
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i.e. PAPU, highly potent and selective inhibitor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.101
Carbamoyl phosphate
pH and temperature not specified in the publication
0.136
putrescine
pH and temperature not specified in the publication
32.9
putrescine
recombinant PTC mutant Y230V/G231S/L232M/Y233G, pH 8.5, 37°C
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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additional information
additional information
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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
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.13
recombinant PTC mutant Y230V/G231S/L232M/Y233G, substrate putrescine, pH 8.5, 37°C
460
813
recombinant wild-type PTC, substrate putrescine, pH 8.5, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
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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
malfunction
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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
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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
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physiological function
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Lmo0036 is responsible for acid tolerance at both sublethal and lethal pH levels and plays a possible role in Listeria virulence
physiological function
the enzyme generates carbamoyl phosphate for ATP production in the fermentative catabolism of agmatine
physiological function
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Lmo0036 is responsible for acid tolerance at both sublethal and lethal pH levels and plays a possible role in Listeria virulence
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additional information
sequence 230YGLY233 is the putrescine signature sequence
additional information
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
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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
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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
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Show AA Sequence and Transmembrane Helices (410 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15000
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x * 15000 + x * 18000 + x * 44000, SDS-PAGE, in the presence of 2-mercaptoethanol
18000
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x * 15000 + x * 18000 + x * 44000, SDS-PAGE, in the presence of 2-mercaptoethanol
40000
44000
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x * 15000 + x * 18000 + x * 44000, SDS-PAGE, in the presence of 2-mercaptoethanol
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
additional information
?
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x * 15000 + x * 18000 + x * 44000, SDS-PAGE, in the presence of 2-mercaptoethanol
trimer
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
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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
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additional information
presence or absence of supratrimeric oligomerization, structure comparison and analysis, overview
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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, 21°C, 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
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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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