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Information on EC 3.5.1.53 - N-carbamoylputrescine amidase
for references in articles please use BRENDA:EC3.5.1.53
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EC Tree 3 Hydrolases
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.5.1 In linear amides
3.5.1.53 N-carbamoylputrescine amidase
The enzyme appears in viruses and cellular organisms
- 3.5.1.53
- agmatine
- polyamine
- ornithine
- deiminase
- aeruginosa
-
iminohydrolase
- spermidine
-
agua
- hydrolases
-
medicago
- truncatula
- beta-alanine
-
nitrilase-like
- aminopropyltransferase
-
his6-tagged
- cadaverine
showSynonyms
n-carbamoylputrescine amidohydrolase, n-carbamoylputrescine amidinohydrolase, n-carbamoylputrescine amidase, n-carbamoyl-putrescine amidohydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AguB
N-carbamoylputrescine amidinohydrolase
-
-
-
-
N-carbamoylputrescine amidohydrolase
NCP amidohydrolase
NCPAH
NCP amidohydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-carbamoylputrescine + H2O = putrescine + CO2 + NH3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of linear amides
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-arginine degradation IV (arginine decarboxylase/agmatine deiminase pathway), putrescine biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
N-carbamoylputrescine amidohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
85030-69-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(8-aminooctyl)urea + H2O
CO2 + NH3 + 1,8-diaminooctane
-
Substrates: -
Products: -
Products: -
?
N-acetylputrescin + H2O
putrescine + acetate
-
Substrates: -
Products: -
Products: -
?
N-carbamoylcadaverine + H2O
cadaverine + CO2 + NH3
-
Substrates: poor substrate
Products: -
Products: -
?
N-carbamoyldiaminoheptane + H2O
CO2 + NH3 + diaminoheptane
-
Substrates: -
Products: -
Products: -
?
N-carbamoyldiaminohexane + H2O
CO2 + NH3 + diaminohexane
-
Substrates: -
Products: -
Products: -
?
N-carbamoyldiaminopentane + H2O
CO2 + NH3 + diaminopentane
-
Substrates: -
Products: -
Products: -
?
N-carbamoyldiaminopropane + H2O
CO2 + NH3 + diaminopropane
-
Substrates: -
Products: -
Products: -
?
N-carbamoyldiaminopropane + H2O
diaminopropane + CO2 + NH3
-
Substrates: poor substrate
Products: -
Products: -
?
carbamoylagmatine + H2O
?
-
Substrates: 63% relative activity compared to carbamoylputrescine
Products: -
Products: -
?
carbamoylagmatine + H2O
?
-
Substrates: 63% relative activity compared to carbamoylputrescine
Products: -
Products: -
?
N-carbamoyl-beta-alanine + H2O
?
-
Substrates: 12% relative activity compared to carbamoylputrescine
Products: -
Products: -
?
N-carbamoyl-beta-alanine + H2O
?
-
Substrates: 12% relative activity compared to carbamoylputrescine
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: NCPAH is a nitrilase belonging to a superfamily of C-N hydrolases acting on non-peptide C-N bonds
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: quantification of ammonia released from N-carbamoylputrescine using indophenol blue method (calorimetric method)
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
Bacteroides thetaiotaomicron JCM 5827
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
Bacteroides thetaiotaomicron JCM 5827
-
Substrates: quantification of ammonia released from N-carbamoylputrescine using indophenol blue method (calorimetric method)
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
ir
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: catalyses final step in putrescine biosynthesis from arginine
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: the two acetylpolyamine amidohydrolases, AphA and AphB, are involved in the conversion of agmatine into putrescine, catabolic pathways of agmatine and putrescine, overview
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: 1,4-diguanidinobutane degradation pathway
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: 1,4-diguanidinobutane degradation pathway
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
Substrates: 10 mM, assay at pH 6.5, 10 min, 40°C
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: catalyses final step in putrescine biosynthesis from arginine
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: catalyses final step in putrescine biosynthesis from arginine
Products: -
Products: -
?
additional information
?
-
-
Substrates: polyamine (agmatine, cadaverine, N-carbamoylputrescine, putrescine, spermidine, and spermine) analysis in cells and cell culture supernatant, by cation exchange HPLC, overview
Products: -
Products: -
-
additional information
?
-
Bacteroides thetaiotaomicron JCM 5827
-
Substrates: polyamine (agmatine, cadaverine, N-carbamoylputrescine, putrescine, spermidine, and spermine) analysis in cells and cell culture supernatant, by cation exchange HPLC, overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: the alanine-pyruvate cycle is indispensable for polyamine utilization, detailed transcriptome profile analysis of Pseudomonas aeruginosa in response to agmatine and putrescine, overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
Bacteroides thetaiotaomicron JCM 5827
-
Substrates: -
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: catalyses final step in putrescine biosynthesis from arginine
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: the two acetylpolyamine amidohydrolases, AphA and AphB, are involved in the conversion of agmatine into putrescine, catabolic pathways of agmatine and putrescine, overview
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: 1,4-diguanidinobutane degradation pathway
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: 1,4-diguanidinobutane degradation pathway
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: catalyses final step in putrescine biosynthesis from arginine
Products: -
Products: -
?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
-
Substrates: catalyses final step in putrescine biosynthesis from arginine
Products: -
Products: -
?
additional information
?
-
-
Substrates: polyamine (agmatine, cadaverine, N-carbamoylputrescine, putrescine, spermidine, and spermine) analysis in cells and cell culture supernatant, by cation exchange HPLC, overview
Products: -
Products: -
-
additional information
?
-
Bacteroides thetaiotaomicron JCM 5827
-
Substrates: polyamine (agmatine, cadaverine, N-carbamoylputrescine, putrescine, spermidine, and spermine) analysis in cells and cell culture supernatant, by cation exchange HPLC, overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: the alanine-pyruvate cycle is indispensable for polyamine utilization, detailed transcriptome profile analysis of Pseudomonas aeruginosa in response to agmatine and putrescine, overview
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-arginine
-
low inhibitory effect on the NCPAH activity at 1 mM
additional information
-
not inhibitory at 1 mM: arginine, ornithine, EDTA, putrescine, spermidine, spermine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
induction of aphA and aphB by exogenous agmatine and acetylputrescine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics, enzyme NCPAH has a substrate-saturation curve with N-carbamoylputrescine as a substrate (fitting to the Michaelis-Menten equation)
-
0.135
N-Carbamoylputrescine
-
recombinant enzyme, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.062
-
induction by 1,4-diguanidinobutane
11.6
-
pH 7.0, 50°C, recombinant enzyme, substrate N-carbamoylputrescine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
-
maximal activity at pH 7.0, the activity is decreased to less than 40% either under pH 6.0 or over pH 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
45
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cells are grown in polyamine-free minimal medium
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
NCPAH is ivolved in the arginine pathway for putrescine biosynthesis
physiological function
malfunction
-
ncpah gene deletion depletes the mutant strain for spermidine, the mutant can be functionally complemented
malfunction
Bacteroides thetaiotaomicron JCM 5827
-
ncpah gene deletion depletes the mutant strain for spermidine, the mutant can be functionally complemented
-
physiological function
-
the polyamine biosynthetic enzyme N-carbamoylputrescine amidohydrolase (NCPAH) converts N-carbamoylputrescine to putrescine, a precursor of spermidine in Bacteroides thetaiotaomicron, which is one of the most dominant species in the human gut microbiota. Feedback inhibition regulates the reaction catalyzed by NCPAH and may play a role in intracellular polyamine homeostasis in Bacteroides thetaiotaomicron. Polyamine metabolic pathways and transporters and mmechanism of polyamine biosynthesis in the gut microbiota, overview
physiological function
Bacteroides thetaiotaomicron JCM 5827
-
the polyamine biosynthetic enzyme N-carbamoylputrescine amidohydrolase (NCPAH) converts N-carbamoylputrescine to putrescine, a precursor of spermidine in Bacteroides thetaiotaomicron, which is one of the most dominant species in the human gut microbiota. Feedback inhibition regulates the reaction catalyzed by NCPAH and may play a role in intracellular polyamine homeostasis in Bacteroides thetaiotaomicron. Polyamine metabolic pathways and transporters and mmechanism of polyamine biosynthesis in the gut microbiota, overview
-
Show AA Sequence and Transmembrane Helices (348 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
37000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C153A
E160A
additional information
additional information
-
generation of strains MS123 (MS39 except DELTAncpah, GmR) and MS140 (MS123 except att1::ncpah+, GmR, EmR). Gene ncpah deletion and complemented strains are generated, and the intracellular polyamines of these strains cultured in a polyamine-free minimal medium are analyzed using high-performance liquid chromatography. The results show that spermidine detected in the parental and complemented strains is depleted in the gene deletion strain. The generation time is longer in the Dncpah mutant strain (144.4 min) compared to parental strain and ncpah-complemented strains (112.7 and 116.8 min), but is indistinguishable between the parental and ncpah-complemented strains. The ability of DELTAncpah to produce spermidine is severely decreased
additional information
Bacteroides thetaiotaomicron JCM 5827
-
generation of strains MS123 (MS39 except DELTAncpah, GmR) and MS140 (MS123 except att1::ncpah+, GmR, EmR). Gene ncpah deletion and complemented strains are generated, and the intracellular polyamines of these strains cultured in a polyamine-free minimal medium are analyzed using high-performance liquid chromatography. The results show that spermidine detected in the parental and complemented strains is depleted in the gene deletion strain. The generation time is longer in the Dncpah mutant strain (144.4 min) compared to parental strain and ncpah-complemented strains (112.7 and 116.8 min), but is indistinguishable between the parental and ncpah-complemented strains. The ability of DELTAncpah to produce spermidine is severely decreased
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
70
AguB activity is stable at up to 70°C for 30 min in 50 mM PIPES buffer, pH 6.5
70
up to 70°C, stable for 30 min at pH 6.5, 50 mM PIPES buffer
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged NCPAH from Escherichia coli strain MS821 by nickel affinity chromatography and ultrafiltration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli to form C-terminal (His)6-tagged protein
gene ncpah, recombinant overexpression of His6-tagged NCPAH in Escherichia coli strain MS821
-
expressed in Escherichia coli to form C-terminal (His)6-tagged protein
-
expressed in Escherichia coli to form C-terminal (His)6-tagged protein
-
expressed in Escherichia coli to form C-terminal (His)6-tagged protein
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yanagisawa, H.; Suzuki, Y.
Purification and properties of N-carbamylputrescine amidohydrolase from maize shoots
Phytochemistry
21
2201-2203
1982
Zea mays
-
brenda
Mercenier, A.; Simon, J.P.; Haas, D.; Stalon, V.
Catabolism of L-arginine by Pseudomonas aeruginosa
J. Gen. Microbiol.
116
381-389
1980
Pseudomonas aeruginosa
brenda
Shoeb, S.M.; Hirota, M.; Shimizu, E.; Yorifuji, T.
Diguanidinobutane (arcaine) degradation in Rhodococcus sp. C-x
Biosci. Biotechnol. Biochem.
58
859-863
1994
Rhodococcus sp. (in: high G+C Gram-positive bacteria), Rhodococcus sp. (in: high G+C Gram-positive bacteria) C-x
-
brenda
Mendum, M.L.; Adams D.O.
Substrate utilization by grape N-carbamoylputrescine amidohydrolase: the final enzyme in putrescine biosynthesis
Am. J. Enol. Vitic.
48
137-144
1997
Vitis vinifera
-
brenda
Piotrowski, M.; Janowitz, T.; Kneifel, H.
Plant C-N hydrolases and the identification of a plant N-carbamoylputrescine amidohydrolase involved in polyamine biosynthesis
J. Biol. Chem.
278
1708-1712
2003
Arabidopsis thaliana
brenda
Nakada, Y.; Itoh, Y.
Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway
Microbiology
149
707-714
2003
Pseudomonas aeruginosa
brenda
Liao, S.; Poonpairoj, P.; Ko, K.; Takatuska, Y.; Yamaguchi, Y.; Abe, N.; Kaneko, J.; Kamio, Y.
Occurrence of agmatine pathway for putrescine synthesis in Selenomonas ruminatium
Biosci. Biotechnol. Biochem.
72
445-455
2008
Selenomonas ruminantium, Selenomonas ruminantium (Q5KR04)
brenda
Baumann, S.; Sander, A.; Gurnon, J.R.; Yanai-Balser, G.M.; Van Etten, J.L.; Piotrowski, M.
Chlorella viruses contain genes encoding a complete polyamine biosynthetic pathway
Virology
360
209-217
2007
Paramecium bursaria Chlorella virus 1, Paramecium bursaria Chlorella virus NY2A, Paramecium bursaria chlorella virus MT325
brenda
Chou, H.T.; Kwon, D.H.; Hegazy, M.; Lu, C.D.
Transcriptome analysis of agmatine and putrescine catabolism in Pseudomonas aeruginosa PAO1
J. Bacteriol.
190
1966-1975
2008
Pseudomonas aeruginosa
brenda
Fuell, C.; Elliott, K.A.; Hanfrey, C.C.; Franceschetti, M.; Michael, A.J.
Polyamine biosynthetic diversity in plants and algae
Plant Physiol. Biochem.
48
513-520
2010
Arabidopsis thaliana
brenda
Landete, J.M.; Arena, M.E.; Pardo, I.; Manca de Nadra, M.C.; Ferrer, S.
The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
Int. Microbiol.
13
169-177
2010
Pseudomonas aeruginosa
brenda
Shimokawa, H.; Sakanaka, M.; Fujisawa, Y.; Ohta, H.; Sugiyama, Y.; Kurihara, S.
N-Carbamoylputrescine amidohydrolase of Bacteroides thetaiotaomicron, a dominant species of the human gut microbiota
Biomedicines
11
1123
2023
Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron JCM 5827
brenda
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