BRENDA - Enzyme Database

Agmatine deiminase from cucumber seedlings is a mono-specific enzyme: purification and characteristics

Sakakibara, Y.; Yanagisawa, H.; Protein Expr. Purif. 30, 88-93 (2003)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
3.5.3.12
arcaine
agmatine analogue, strong competitive inhibition
Cucumis sativus
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.5.3.12
0.016
-
agmatine
pH 7.0, 30C
Cucumis sativus
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.5.3.12
36000
-
x * 36000, deglycosylated enzyme, SDS-PAGE, x * 47000, glycosylated enzyme, SDS-PAGE, monomer or dimer
Cucumis sativus
3.5.3.12
47000
-
x * 36000, deglycosylated enzyme, SDS-PAGE, x * 47000, glycosylated enzyme, SDS-PAGE, monomer or dimer
Cucumis sativus
3.5.3.12
67000
-
gel filtration
Cucumis sativus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.5.3.12
Cucumis sativus
-
cv. Tokiwajibae
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
3.5.3.12
glycoprotein
N-glycosylation
Cucumis sativus
Purification (Commentary)
EC Number
Commentary
Organism
3.5.3.12
2470fold
Cucumis sativus
Reaction
EC Number
Reaction
Commentary
Organism
3.5.3.12
agmatine + H2O = N-carbamoylputrescine + NH3
the enzyme does not show activity of EC 2.1.3.3, ornithine carbamoyltransferase, EC 2.1.3.6, putrescine carbamoyltransferase, and EC 2.7.2.2, carbamate kinase, while putrescine synthase is a multifunctional enzyme, overview
Cucumis sativus
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
3.5.3.12
seedling
-
Cucumis sativus
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
3.5.3.12
14.5
-
purified enzyme
Cucumis sativus
Storage Stability
EC Number
Storage Stability
Organism
3.5.3.12
4C, purified enzyme, 2 months, stable
Cucumis sativus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.5.3.12
agmatine + H2O
-
657259
Cucumis sativus
N-carbamoylputrescine + NH3
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
3.5.3.12
More
x * 36000, deglycosylated enzyme, SDS-PAGE, x * 47000, glycosylated enzyme, SDS-PAGE, monomer or dimer
Cucumis sativus
Temperature Optimum [C]
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
3.5.3.12
30
-
assay at
Cucumis sativus
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.5.3.12
7
-
-
Cucumis sativus
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
3.5.3.12
6.5
8
89% of maximal activity at pH 6.5, 91% of maximal activity at pH 8.0
Cucumis sativus
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3.5.3.12
0.0071
-
arcaine
pH 7.0, 30C
Cucumis sativus
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
3.5.3.12
arcaine
agmatine analogue, strong competitive inhibition
Cucumis sativus
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3.5.3.12
0.0071
-
arcaine
pH 7.0, 30C
Cucumis sativus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.5.3.12
0.016
-
agmatine
pH 7.0, 30C
Cucumis sativus
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.5.3.12
36000
-
x * 36000, deglycosylated enzyme, SDS-PAGE, x * 47000, glycosylated enzyme, SDS-PAGE, monomer or dimer
Cucumis sativus
3.5.3.12
47000
-
x * 36000, deglycosylated enzyme, SDS-PAGE, x * 47000, glycosylated enzyme, SDS-PAGE, monomer or dimer
Cucumis sativus
3.5.3.12
67000
-
gel filtration
Cucumis sativus
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
3.5.3.12
glycoprotein
N-glycosylation
Cucumis sativus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.5.3.12
2470fold
Cucumis sativus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
3.5.3.12
seedling
-
Cucumis sativus
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
3.5.3.12
14.5
-
purified enzyme
Cucumis sativus
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
3.5.3.12
4C, purified enzyme, 2 months, stable
Cucumis sativus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.5.3.12
agmatine + H2O
-
657259
Cucumis sativus
N-carbamoylputrescine + NH3
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
3.5.3.12
More
x * 36000, deglycosylated enzyme, SDS-PAGE, x * 47000, glycosylated enzyme, SDS-PAGE, monomer or dimer
Cucumis sativus
Temperature Optimum [C] (protein specific)
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
3.5.3.12
30
-
assay at
Cucumis sativus
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.5.3.12
7
-
-
Cucumis sativus
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
3.5.3.12
6.5
8
89% of maximal activity at pH 6.5, 91% of maximal activity at pH 8.0
Cucumis sativus