BRENDA - Enzyme Database
show all sequences of 3.5.3.24

Dual biosynthesis pathway for longer-chain polyamines in the hyperthermophilic archaeon Thermococcus kodakarensis

Morimoto, N.; Fukuda, W.; Nakajima, N.; Masuda, T.; Terui, Y.; Kanai, T.; Oshima, T.; Imanaka, T.; Fujiwara, S.; J. Bacteriol. 192, 4991-5001 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Thermococcus kodakarensis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00642
-
N1-aminopropylagmatine
pH 7.5, 70C
Thermococcus kodakarensis
0.486
-
agmatine
pH 7.5, 70C
Thermococcus kodakarensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N1-aminopropylagmatine + H2O
Thermococcus kodakarensis
in Pyrococcus kodakaraensis spermidine is synthesized mainly from agmatine. The enzyme is involved in the biosynthesis of spermidine from agmatine
spermidine + urea
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermococcus kodakarensis
Q5JI38
-
-
Purification (Commentary)
Commentary
Organism
-
Thermococcus kodakarensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
agmatine + H2O
43fold higher kcat/Km value for N1-aminopropylagmatine than for agmatine
719718
Thermococcus kodakarensis
putrescine + urea
-
-
-
?
N1-aminopropylagmatine + H2O
in Pyrococcus kodakaraensis spermidine is synthesized mainly from agmatine. The enzyme is involved in the biosynthesis of spermidine from agmatine
719718
Thermococcus kodakarensis
spermidine + urea
-
-
-
?
N1-aminopropylagmatine + H2O
43fold higher kcat/Km value for N1-aminopropylagmatine than for agmatine
719718
Thermococcus kodakarensis
spermidine + urea
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
70
-
assay at
Thermococcus kodakarensis
90
-
-
Thermococcus kodakarensis
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
90
-
enzyme is not fully unfolded
Thermococcus kodakarensis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.001
-
N1-aminopropylagmatine
pH 7.5, 70C
Thermococcus kodakarensis
0.00186
-
agmatine
pH 7.5, 70C
Thermococcus kodakarensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Thermococcus kodakarensis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Thermococcus kodakarensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00642
-
N1-aminopropylagmatine
pH 7.5, 70C
Thermococcus kodakarensis
0.486
-
agmatine
pH 7.5, 70C
Thermococcus kodakarensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N1-aminopropylagmatine + H2O
Thermococcus kodakarensis
in Pyrococcus kodakaraensis spermidine is synthesized mainly from agmatine. The enzyme is involved in the biosynthesis of spermidine from agmatine
spermidine + urea
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermococcus kodakarensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
agmatine + H2O
43fold higher kcat/Km value for N1-aminopropylagmatine than for agmatine
719718
Thermococcus kodakarensis
putrescine + urea
-
-
-
?
N1-aminopropylagmatine + H2O
in Pyrococcus kodakaraensis spermidine is synthesized mainly from agmatine. The enzyme is involved in the biosynthesis of spermidine from agmatine
719718
Thermococcus kodakarensis
spermidine + urea
-
-
-
?
N1-aminopropylagmatine + H2O
43fold higher kcat/Km value for N1-aminopropylagmatine than for agmatine
719718
Thermococcus kodakarensis
spermidine + urea
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
70
-
assay at
Thermococcus kodakarensis
90
-
-
Thermococcus kodakarensis
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
90
-
enzyme is not fully unfolded
Thermococcus kodakarensis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.001
-
N1-aminopropylagmatine
pH 7.5, 70C
Thermococcus kodakarensis
0.00186
-
agmatine
pH 7.5, 70C
Thermococcus kodakarensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Thermococcus kodakarensis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00387
-
agmatine
pH 7.5, 70C
Thermococcus kodakarensis
0.165
-
N1-aminopropylagmatine
pH 7.5, 70C
Thermococcus kodakarensis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00387
-
agmatine
pH 7.5, 70C
Thermococcus kodakarensis
0.165
-
N1-aminopropylagmatine
pH 7.5, 70C
Thermococcus kodakarensis
Other publictions for EC 3.5.3.24
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)
719718
Morimoto
Dual biosynthesis pathway for ...
Thermococcus kodakarensis
J. Bacteriol.
192
4991-5001
2010
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3
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3
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2
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1
2
1
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1
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1
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1
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3
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2
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1
2
1
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2
2
719832
Ohnuma
N1-aminopropylagmatine, a new ...
Thermus thermophilus
J. Biol. Chem.
280
30073-30082
2005
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1
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1
1
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1
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1
1
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1
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