BRENDA - Enzyme Database
show all sequences of 3.5.1.53

Purification and properties of N-carbamylputrescine amidohydrolase from maize shoots

Yanagisawa, H.; Suzuki, Y.; Phytochemistry 21, 2201-2203 (1982)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Zea mays
p-hydroxymercuribenzoate
-
Zea mays
Zn2+
-
Zea mays
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.09
-
N-Carbamoylputrescine
-
Zea mays
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Zea mays
5829
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
125000
-
gel filtration
Zea mays
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N-carbamoylputrescine + H2O
Zea mays
catalyses final step in putrescine biosynthesis from arginine
putrescine + CO2 + NH3
-
Zea mays
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Zea mays
-
-
-
Purification (Commentary)
Commentary
Organism
70fold
Zea mays
Source Tissue
Source Tissue
Commentary
Organism
Textmining
shoot
-
Zea mays
-
Storage Stability
Storage Stability
Organism
4°C, 50 mM Tris-HCl buffer, 5 mM mercaptoethanol, 0.1 mM EDTA, pH 7, 3 days, 40% loss of activity
Zea mays
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N-carbamoylputrescine + H2O
-
209189
Zea mays
putrescine + CO2 + NH3
-
209189
Zea mays
?
N-carbamoylputrescine + H2O
catalyses final step in putrescine biosynthesis from arginine
209189
Zea mays
putrescine + CO2 + NH3
-
209189
Zea mays
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
10 min, 47% loss of activity
Zea mays
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7
-
Zea mays
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Zea mays
p-hydroxymercuribenzoate
-
Zea mays
Zn2+
-
Zea mays
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.09
-
N-Carbamoylputrescine
-
Zea mays
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Zea mays
5829
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
125000
-
gel filtration
Zea mays
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N-carbamoylputrescine + H2O
Zea mays
catalyses final step in putrescine biosynthesis from arginine
putrescine + CO2 + NH3
-
Zea mays
?
Purification (Commentary) (protein specific)
Commentary
Organism
70fold
Zea mays
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
shoot
-
Zea mays
-
Storage Stability (protein specific)
Storage Stability
Organism
4°C, 50 mM Tris-HCl buffer, 5 mM mercaptoethanol, 0.1 mM EDTA, pH 7, 3 days, 40% loss of activity
Zea mays
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N-carbamoylputrescine + H2O
-
209189
Zea mays
putrescine + CO2 + NH3
-
209189
Zea mays
?
N-carbamoylputrescine + H2O
catalyses final step in putrescine biosynthesis from arginine
209189
Zea mays
putrescine + CO2 + NH3
-
209189
Zea mays
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
10 min, 47% loss of activity
Zea mays
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
7
-
Zea mays
Other publictions for EC 3.5.1.53
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
713298
Fuell
Polyamine biosynthetic diversi ...
Arabidopsis thaliana
Plant Physiol. Biochem.
48
513-520
2010
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1
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7
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1
1
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1
1
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1
1
-
-
-
719620
Landete
The role of two families of ba ...
Pseudomonas aeruginosa
Int. Microbiol.
13
169-177
2010
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8
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1
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1
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685687
Liao
Occurrence of agmatine pathway ...
Selenomonas ruminantium
Biosci. Biotechnol. Biochem.
72
445-455
2008
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-
1
-
2
1
6
1
-
-
3
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6
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1
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2
2
1
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1
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1
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1
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2
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4
1
-
12
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2
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5
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2
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2
2
2
-
2
-
2
-
2
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692846
Chou
Transcriptome analysis of agma ...
Pseudomonas aeruginosa
J. Bacteriol.
190
1966-1975
2008
1
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1
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2
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2
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1
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4
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1
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1
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1
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1
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2
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2
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4
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1
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-
1
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690188
Baumann
Chlorella viruses contain gene ...
Paramecium bursaria Chlorella virus 1, Paramecium bursaria chlorella virus MT325, Paramecium bursaria Chlorella virus NY2A
Virology
360
209-217
2007
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3
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9
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3
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3
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3
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3
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3
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652383
Piotrowski
Plant C-N hydrolases and the i ...
Arabidopsis thaliana
J. Biol. Chem.
278
1708-1712
2003
-
-
1
-
-
-
-
1
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1
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6
-
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1
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1
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1
-
1
-
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-
-
1
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-
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1
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-
-
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-
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1
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1
-
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1
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1
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1
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1
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1
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-
653166
Nakada
Identification of the putresci ...
Pseudomonas aeruginosa
Microbiology
149
707-714
2003
-
-
-
-
-
-
4
1
-
-
2
-
-
3
-
-
-
-
-
-
-
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3
1
1
-
-
-
1
-
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-
-
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4
-
1
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-
2
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3
1
1
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1
-
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-
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-
209192
Mendum
-
Substrate utilization by grape ...
Vitis vinifera
Am. J. Enol. Vitic.
48
137-144
1997
-
-
-
-
-
-
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1
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1
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1
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10
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1
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1
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1
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10
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1
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209191
Shoeb
-
Diguanidinobutane (arcaine) de ...
Rhodococcus sp., Rhodococcus sp. C-x
Biosci. Biotechnol. Biochem.
58
859-863
1994
-
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2
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3
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1
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3
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8
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1
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2
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1
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3
-
8
-
-
-
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1
-
-
-
-
-
-
-
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-
209189
Yanagisawa
-
Purification and properties of ...
Zea mays
Phytochemistry
21
2201-2203
1982
-
-
-
-
-
-
3
1
1
-
1
1
-
1
-
-
1
-
-
1
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1
2
-
-
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1
-
1
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-
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3
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1
1
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1
1
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1
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1
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1
2
-
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-
1
-
1
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-
-
-
-
-
-
-
-
209190
Mercenier
Catabolism of L-arginine by Ps ...
Pseudomonas aeruginosa
J. Gen. Microbiol.
116
381-389
1980
-
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1
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1
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2
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2
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1
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1
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1
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2
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1
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