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arsenate + N-carbamoylputrescine
?
carbamoyl phosphate + 1,3-diaminopropane
phosphate + N1-carbamoyl-1,3-diaminopropane
carbamoyl phosphate + 1,6-diaminohexane
phosphate + N1-carbamoyl-1,6-diaminohexane
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
carbamoyl phosphate + ornithine
phosphate + citrulline
-
-
-
?
carbamoyl phosphate + ornithine
phosphate + N-carbamoylornithine
-
only weak activity with ornithine as a substrate
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
carbamoyl phosphate + spermidine
phosphate + N-carbamoylspermidine
carbamoyl phosphate + spermine
phosphate + N-carbamoylspermine
additional information
?
-
arsenate + N-carbamoylputrescine
?
-
-
-
-
?
arsenate + N-carbamoylputrescine
?
-
carbamoyl arsenate as intermediate is not formed
-
-
ir
arsenate + N-carbamoylputrescine
?
-
carbamoyl arsenate as intermediate is not formed
-
-
ir
arsenate + N-carbamoylputrescine
?
-
-
-
-
?
carbamoyl phosphate + 1,3-diaminopropane
phosphate + N1-carbamoyl-1,3-diaminopropane
-
-
-
?
carbamoyl phosphate + 1,3-diaminopropane
phosphate + N1-carbamoyl-1,3-diaminopropane
-
-
-
-
?
carbamoyl phosphate + 1,6-diaminohexane
phosphate + N1-carbamoyl-1,6-diaminohexane
-
-
-
?
carbamoyl phosphate + 1,6-diaminohexane
phosphate + N1-carbamoyl-1,6-diaminohexane
-
-
-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
-
-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
-
-
-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
-
only weak activity with cadaverine a substrate
-
-
?
carbamoyl phosphate + cadaverine
phosphate + N-carbamoylcadaverine
-
only weak activity with cadaverine a substrate
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
-
low activity, reaction of EC 2.1.3.3
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
-
low activity, reaction of EC 2.1.3.3
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
substrate binding structures, overview
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
substrate binding structures, overview
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
-
r
carbamoyl phosphate + spermidine
phosphate + N-carbamoylspermidine
-
-
-
?
carbamoyl phosphate + spermidine
phosphate + N-carbamoylspermidine
-
-
-
-
?
carbamoyl phosphate + spermine
phosphate + N-carbamoylspermine
-
-
-
?
carbamoyl phosphate + spermine
phosphate + N-carbamoylspermine
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
-
-
?
additional information
?
-
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
?
-
-
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
?
-
-
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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carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
additional information
?
-
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
-
low activity, reaction of EC 2.1.3.3
-
-
?
carbamoyl phosphate + L-ornithine
phosphate + N-carbamoyl-L-ornithine
-
low activity, reaction of EC 2.1.3.3
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoyl-putrescine
-
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
phosphorolysis of N-carbamoylputrescine is possibly the physological role of the enzyme
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
?
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
-
r
carbamoyl phosphate + putrescine
phosphate + N-carbamoylputrescine
-
-
-
-
r
additional information
?
-
-
the enzyme catalyzes the second of three steps of ATP synthesis from agmatine
-
-
?
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
?
-
-
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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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
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
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
-
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
-
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
-
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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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
-
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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Srivenugopal, K.S.; Adiga, P.R.
Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase)
J. Biol. Chem.
256
9532-9541
1981
Lathyrus sativus
brenda
Prasad, G.L.; Adiga, P.R.
Purification and characterization of putrescine synthase from cucumber seedlings. A multifunctional enzyme involved in putrescine biosynthesis
J. Biosci.
10
373-391
1986
Cucumis sativus
-
brenda
Roon, R.J.; Barker, H.A.
Fermentation of agmatine in Streptococcus faecalis: occurence of putrescine transcarbamoylase
J. Bacteriol.
109
44-50
1972
Enterococcus faecalis, Enterococcus faecalis 10C1
brenda
Stalon, V.
Putrescine carbamoyltransferase (Streptococcus faecalis)
Methods Enzymol.
94
339343
1983
Enterococcus faecalis, Pediococcus acidilactici
-
brenda
Venugopal, K.S.S.; Adiga, P.R.
A simple procedure for purification of N-carbamoylputrescine: application to assays of putrescine transcarbamoylase and agmatine iminohydrolase activities
Anal. Biochem.
104
440-444
1980
Lathyrus sativus
brenda
Wargnies, B.; Lauwers, N.; Stalon, V.
Structure and properties of the putrescine carbamoyltransferase of Streptococcus faecalis
Eur. J. Biochem.
101
143-12
1979
Enterococcus faecalis
brenda
Llacer, J.L.; Polo, L.M.; Tavarez, S.; Alarcon, B.; Hilario, R.; Rubio, V.
The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction
J. Bacteriol.
189
1254-1265
2007
Enterococcus faecalis, Enterococcus faecalis ATCC 700802
brenda
Chen, J.; Cheng, C.; Xia, Y.; Zhao, H.; Fang, C.; Shan, Y.; Wu, B.; Fang, W.
Lmo0036, an ornithine and putrescine carbamoyltransferase in Listeria monocytogenes, participates in arginine deiminase and agmatine deiminase pathways and mediates acid tolerance
Microbiology
157
3150-3161
2011
Listeria monocytogenes, Listeria monocytogenes 10403S
brenda
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)
brenda
Shi, D.; Yu, X.; Zhao, G.; Ho, J.; Lu, S.; Allewell, N.M.; Tuchman, M.
Crystal structure and biochemical properties of putrescine carbamoyltransferase from Enterococcus faecalis: assembly, active site, and allosteric regulation
Proteins
80
1436-1447
2012
Enterococcus faecalis (Q837U7), Enterococcus faecalis, Enterococcus faecalis ATCC 700802 (Q837U7)
brenda
Shi, D.; Allewell, N.M.; Tuchman, M.
From genome to structure and back again a family portrait of the transcarbamylases
Int. J. Mol. Sci.
16
18836-18864
2015
Enterococcus faecalis
brenda