Information on EC 3.5.1.53 - N-carbamoylputrescine amidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.53
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RECOMMENDED NAME
GeneOntology No.
N-carbamoylputrescine amidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-carbamoylputrescine + H2O = putrescine + CO2 + NH3
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of linear amides
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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L-arginine degradation IV (arginine decarboxylase/agmatine deiminase pathway)
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Metabolic pathways
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putrescine biosynthesis II
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polyamine pathway
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SYSTEMATIC NAME
IUBMB Comments
N-carbamoylputrescine amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
85030-69-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain C-x
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-
Manually annotated by BRENDA team
strain C-x
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-
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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NCPAH is ivolved in the arginine pathway for putrescine biosynthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carbamoylagmatine + H2O
?
show the reaction diagram
N-acetylputrescin + H2O
putrescine + acetate
show the reaction diagram
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-
-
-
?
N-amylurea + H2O
CO2 + NH3 + 1-n-pentanamine
show the reaction diagram
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-
-
?
N-butylurea + H2O
CO2 + NH3 + 1-n-butylamine
show the reaction diagram
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-
-
?
N-carbamoyl-beta-alanine + H2O
?
show the reaction diagram
N-carbamoylcadaverine + H2O
cadaverine + CO2 + NH3
show the reaction diagram
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poor substrate
-
?
N-carbamoyldiaminoheptane + H2O
CO2 + NH3 + diaminoheptane
show the reaction diagram
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-
-
?
N-carbamoyldiaminohexane + H2O
CO2 + NH3 + diaminohexane
show the reaction diagram
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-
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?
N-carbamoyldiaminooctane + H2O
CO2 + NH3 + diaminooctane
show the reaction diagram
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-
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?
N-carbamoyldiaminopentane + H2O
CO2 + NH3 + diaminopentane
show the reaction diagram
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?
N-carbamoyldiaminopropane + H2O
CO2 + NH3 + diaminopropane
show the reaction diagram
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?
N-carbamoyldiaminopropane + H2O
diaminopropane + CO2 + NH3
show the reaction diagram
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poor substrate
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?
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
show the reaction diagram
N-hexylurea + H2O
CO2 + NH3 + 1-n-hexylamine
show the reaction diagram
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?
additional information
?
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the alanine-pyruvate cycle is indispensable for polyamine utilization, detailed transcriptome profile analysis of Pseudomonas aeruginosa in response to agmatine and putrescine, overview
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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
N-carbamoylputrescine + H2O
putrescine + CO2 + NH3
show the reaction diagram
additional information
?
-
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the alanine-pyruvate cycle is indispensable for polyamine utilization, detailed transcriptome profile analysis of Pseudomonas aeruginosa in response to agmatine and putrescine, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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activates
Mg2+
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activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
; strong inhibitor
Cu2+
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Fe2+
; strong inhibitor
iodoacetamide
Mn2+
; strong inhibitor
p-chloromercuribenzoate
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94% inhibition at 0.1 mM
p-hydroxymercuribenzoate
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additional information
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not inhibitory at 1 mM: arginine, ornithine, EDTA, putrescine, spermidine, spermine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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induction of aphA and aphB by exogenous agmatine and acetylputrescine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 0.5
N-Carbamoylputrescine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
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induction by L-asparagine
0.035
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induction by agmatine
0.062
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induction by 1,4-diguanidinobutane
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
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7
; assay at pH 6.5, 10 min, 40°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
; assay at pH 6.5, 10 min, 40°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
additional information
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found in all organs investigated
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32532
2 * 32532, calculated from sequence
33000
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6 * 33000, SDS-PAGE
37000
2 * 37000, SDS-PAGE; SDS-PAGE
80000
gel filtration; gel filtration
125000
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gel filtration
230000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 32532, calculated from sequence; 2 * 37000, SDS-PAGE
homohexamer
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6 * 33000, SDS-PAGE
homooctamer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
; stable
685687
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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10 min, 47% loss of activity
70
AguB activity is stable at up to 70°C for 30 min in 50 mM PIPES buffer, pH 6.5; up to 70°C, stable for 30 min at pH 6.5, 50 mM PIPES buffer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in 50 mM PIPES buffer at pH 6.5 stable for 30 min up to 70°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tris-HCl buffer, 5 mM mercaptoethanol, 0.1 mM EDTA, pH 7, 3 days, 40% loss of activity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli to form C-terminal (His)6-tagged protein
expressed in Escherichia coli; expression in Escherichia coli strain DE3
expression in Escherichia coli, His6-tag
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overexpression of gene aphA in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C153A
inactive mutant enzyme; mutant without enzyme activity
E160A
inactive mutant enzyme; mutant without enzyme activity
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