BRENDA - Enzyme Database

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)
EC Number
Commentary
Organism
2.5.1.104
expression in Escherichia coli
Thermococcus kodakarensis
3.5.3.24
expression in Escherichia coli
Thermococcus kodakarensis
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.5.1.104
0.012
-
agmatine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
0.0807
-
cadaverine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
1.053
-
putrescine
pH 9.0, 70°C
Thermococcus kodakarensis
3.5.3.24
0.00642
-
N1-aminopropylagmatine
pH 7.5, 70°C
Thermococcus kodakarensis
3.5.3.24
0.486
-
agmatine
pH 7.5, 70°C
Thermococcus kodakarensis
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.5.1.104
S-adenosyl 3-(methylthio)propylamine + agmatine
Thermococcus kodakarensis
the enzyme is involved in polyamine biosynthesis
5'-S-methyl-5'-thioadenosine + N1-aminopropylagamatine
-
-
?
3.5.3.24
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
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.5.1.104
Thermococcus kodakarensis
Q5JFG9
-
-
3.5.3.24
Thermococcus kodakarensis
Q5JI38
-
-
Purification (Commentary)
EC Number
Commentary
Organism
2.5.1.104
-
Thermococcus kodakarensis
3.5.3.24
-
Thermococcus kodakarensis
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.5.1.104
S-adenosyl 3-(methylthio)propylamine + agmatine
the enzyme is involved in polyamine biosynthesis
719718
Thermococcus kodakarensis
5'-S-methyl-5'-thioadenosine + N1-aminopropylagamatine
-
-
-
?
2.5.1.104
S-adenosyl 3-(methylthio)propylamine + agmatine
-
719718
Thermococcus kodakarensis
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
-
?
2.5.1.104
S-adenosyl 3-(methylthio)propylamine + cadaverine
-
719718
Thermococcus kodakarensis
5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine
-
-
-
?
2.5.1.104
S-adenosyl 3-(methylthio)propylamine + putrescine
-
719718
Thermococcus kodakarensis
5'-S-methyl-5'-thioadenosine + spermidine
-
-
-
?
3.5.3.24
agmatine + H2O
43fold higher kcat/Km value for N1-aminopropylagmatine than for agmatine
719718
Thermococcus kodakarensis
putrescine + urea
-
-
-
?
3.5.3.24
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
-
-
-
?
3.5.3.24
N1-aminopropylagmatine + H2O
43fold higher kcat/Km value for N1-aminopropylagmatine than for agmatine
719718
Thermococcus kodakarensis
spermidine + urea
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.5.1.104
70
-
assay at
Thermococcus kodakarensis
3.5.3.24
70
-
assay at
Thermococcus kodakarensis
3.5.3.24
90
-
-
Thermococcus kodakarensis
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
3.5.3.24
90
-
enzyme is not fully unfolded
Thermococcus kodakarensis
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.5.1.104
0.02
-
cadaverine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
0.28
-
agmatine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
0.3
-
putrescine
pH 9.0, 70°C
Thermococcus kodakarensis
3.5.3.24
0.001
-
N1-aminopropylagmatine
pH 7.5, 70°C
Thermococcus kodakarensis
3.5.3.24
0.00186
-
agmatine
pH 7.5, 70°C
Thermococcus kodakarensis
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.5.1.104
9
-
assay at
Thermococcus kodakarensis
3.5.3.24
7.5
-
assay at
Thermococcus kodakarensis
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
2.5.1.104
expression in Escherichia coli
Thermococcus kodakarensis
3.5.3.24
expression in Escherichia coli
Thermococcus kodakarensis
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.5.1.104
0.012
-
agmatine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
0.0807
-
cadaverine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
1.053
-
putrescine
pH 9.0, 70°C
Thermococcus kodakarensis
3.5.3.24
0.00642
-
N1-aminopropylagmatine
pH 7.5, 70°C
Thermococcus kodakarensis
3.5.3.24
0.486
-
agmatine
pH 7.5, 70°C
Thermococcus kodakarensis
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.5.1.104
S-adenosyl 3-(methylthio)propylamine + agmatine
Thermococcus kodakarensis
the enzyme is involved in polyamine biosynthesis
5'-S-methyl-5'-thioadenosine + N1-aminopropylagamatine
-
-
?
3.5.3.24
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)
EC Number
Commentary
Organism
2.5.1.104
-
Thermococcus kodakarensis
3.5.3.24
-
Thermococcus kodakarensis
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.5.1.104
S-adenosyl 3-(methylthio)propylamine + agmatine
the enzyme is involved in polyamine biosynthesis
719718
Thermococcus kodakarensis
5'-S-methyl-5'-thioadenosine + N1-aminopropylagamatine
-
-
-
?
2.5.1.104
S-adenosyl 3-(methylthio)propylamine + agmatine
-
719718
Thermococcus kodakarensis
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
-
?
2.5.1.104
S-adenosyl 3-(methylthio)propylamine + cadaverine
-
719718
Thermococcus kodakarensis
5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine
-
-
-
?
2.5.1.104
S-adenosyl 3-(methylthio)propylamine + putrescine
-
719718
Thermococcus kodakarensis
5'-S-methyl-5'-thioadenosine + spermidine
-
-
-
?
3.5.3.24
agmatine + H2O
43fold higher kcat/Km value for N1-aminopropylagmatine than for agmatine
719718
Thermococcus kodakarensis
putrescine + urea
-
-
-
?
3.5.3.24
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
-
-
-
?
3.5.3.24
N1-aminopropylagmatine + H2O
43fold higher kcat/Km value for N1-aminopropylagmatine than for agmatine
719718
Thermococcus kodakarensis
spermidine + urea
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.5.1.104
70
-
assay at
Thermococcus kodakarensis
3.5.3.24
70
-
assay at
Thermococcus kodakarensis
3.5.3.24
90
-
-
Thermococcus kodakarensis
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
3.5.3.24
90
-
enzyme is not fully unfolded
Thermococcus kodakarensis
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.5.1.104
0.02
-
cadaverine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
0.28
-
agmatine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
0.3
-
putrescine
pH 9.0, 70°C
Thermococcus kodakarensis
3.5.3.24
0.001
-
N1-aminopropylagmatine
pH 7.5, 70°C
Thermococcus kodakarensis
3.5.3.24
0.00186
-
agmatine
pH 7.5, 70°C
Thermococcus kodakarensis
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.5.1.104
9
-
assay at
Thermococcus kodakarensis
3.5.3.24
7.5
-
assay at
Thermococcus kodakarensis
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2.5.1.104
0.29
-
cadaverine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
0.29
-
putrescine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
22.5
-
agmatine
pH 9.0, 70°C
Thermococcus kodakarensis
3.5.3.24
0.00387
-
agmatine
pH 7.5, 70°C
Thermococcus kodakarensis
3.5.3.24
0.165
-
N1-aminopropylagmatine
pH 7.5, 70°C
Thermococcus kodakarensis
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2.5.1.104
0.29
-
cadaverine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
0.29
-
putrescine
pH 9.0, 70°C
Thermococcus kodakarensis
2.5.1.104
22.5
-
agmatine
pH 9.0, 70°C
Thermococcus kodakarensis
3.5.3.24
0.00387
-
agmatine
pH 7.5, 70°C
Thermococcus kodakarensis
3.5.3.24
0.165
-
N1-aminopropylagmatine
pH 7.5, 70°C
Thermococcus kodakarensis