Data extracted from this reference:
Inhibitors
NaCl
about 50% residual activity in the presence of 1 M NaCl, about 30% residual activity in the presence of 2 M NaCl, about 10% residual activity in the presence of 4 M NaCl, about 3.5% residual activity in the presence of 6 M NaCl
Streptomyces noursei
KM Value [mM]
0.053
cyclo(L-Leu-L-Phe)
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
Streptomyces noursei
0.067
cyclo(L-Phe-L-His)
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
Streptomyces noursei
Molecular Weight [Da]
21066
x * 21066, calculated from amino acid sequence
Streptomyces noursei
23000
x * 23000, SDS-PAGE
Streptomyces noursei
Natural Substrates/ Products (Substrates)
cyclo(L-Leu-L-Phe) + O2
Streptomyces noursei
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
albonoursin + H2O2
?
cyclo(L-Leu-L-Phe) + O2
Streptomyces noursei
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
?
cyclo(L-Leu-L-Phe) + O2
Streptomyces noursei ATCC 11455
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
albonoursin + H2O2
?
cyclo(L-Leu-L-Phe) + O2
Streptomyces noursei ATCC 11455
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
?
Organism
Streptomyces noursei
Q8GED9
Streptomyces noursei ATCC 11455
Q8GED9
Purification (Commentary)
ammonium sulfate precipitation, Q-Sepharose column chromatography, EMD propyl column chromatography, and Superose 6 gel filtration
Streptomyces noursei
Storage Stability
-80°C, purified enzyme in the absence of any additive, several months, no loss of activity
Streptomyces noursei
22°C, purified enzyme in the absence of any additive, 24 h, no loss of activity
Streptomyces noursei
Substrates and Products (Substrate)
cyclo(L-Glu-Gly) + O2
3% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei
(4Z)-4-(3,6-dioxopiperazin-2-yl)butanoate + H2O2
?
cyclo(L-Glu-Gly) + O2
3% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei ATCC 11455
(4Z)-4-(3,6-dioxopiperazin-2-yl)butanoate + H2O2
?
cyclo(L-Leu-Gly) + O2
9% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei
(3Z)-3-(2-methylpropylidene)piperazine-2,5-dione + H2O2
?
cyclo(L-Leu-Gly) + O2
9% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei ATCC 11455
(3Z)-3-(2-methylpropylidene)piperazine-2,5-dione + H2O2
?
cyclo(L-Leu-L-Ala) + O2
13% mono-dehydro-products and 4% bis-dehydro products
722172
Streptomyces noursei
?
?
cyclo(L-Leu-L-Phe) + O2
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
722172
Streptomyces noursei
albonoursin + H2O2
?
cyclo(L-Leu-L-Phe) + O2
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
722172
Streptomyces noursei ATCC 11455
albonoursin + H2O2
?
cyclo(L-Leu-L-Phe) + O2
722172
Streptomyces noursei
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
?
cyclo(L-Leu-L-Phe) + O2
722172
Streptomyces noursei ATCC 11455
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
?
cyclo(L-Phe-Gly) + O2
36% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei
(3Z)-3-benzylidenepiperazine-2,5-dione + H2O2
?
cyclo(L-Phe-L-His) + O2
21% mono-dehydro-products and less than 1% bis-dehydro products
722172
Streptomyces noursei
?
?
cyclo(L-Ser-Gly) + O2
11% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei
(3Z)-3-(2-hydroxyethylidene)piperazine-2,5-dione + H2O2
?
cyclo(L-Trp-L-Trp) + O2
74% mono-dehydro-products and 14% bis-dehydro products
722172
Streptomyces noursei
?
?
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + O2
722172
Streptomyces noursei
albonoursin + H2O2
?
additional information
no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe
722172
Streptomyces noursei
?
?
additional information
no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe
722172
Streptomyces noursei ATCC 11455
?
?
Subunits
?
x * 23000, SDS-PAGE
Streptomyces noursei
?
x * 21066, calculated from amino acid sequence
Streptomyces noursei
Synonyms
cyclic dipeptide oxidase
Streptomyces noursei
Temperature Optimum [°C]
60
activity increases up to the maximum at 60°C followed by a substantial drop above this temperature
Streptomyces noursei
Turnover Number [1/s]
0.453
cyclo(L-Phe-L-His)
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
Streptomyces noursei
0.69
cyclo(L-Leu-L-Phe)
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
Streptomyces noursei
pH Optimum
pH Range
5.5
10.5
Streptomyces noursei
pH Stability
6
8.7
the enzyme activity is quite stable at neutral and basic pH values, whereas it decreases at acidic pH values. Residual activity is 75% after 6.5 h at pH 6.0
Streptomyces noursei
pI Value
Streptomyces noursei
isoelectric focusing
3.8
Inhibitors (protein specific)
NaCl
about 50% residual activity in the presence of 1 M NaCl, about 30% residual activity in the presence of 2 M NaCl, about 10% residual activity in the presence of 4 M NaCl, about 3.5% residual activity in the presence of 6 M NaCl
Streptomyces noursei
KM Value [mM] (protein specific)
0.053
cyclo(L-Leu-L-Phe)
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
Streptomyces noursei
0.067
cyclo(L-Phe-L-His)
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
Streptomyces noursei
Molecular Weight [Da] (protein specific)
21066
x * 21066, calculated from amino acid sequence
Streptomyces noursei
23000
x * 23000, SDS-PAGE
Streptomyces noursei
Natural Substrates/ Products (Substrates) (protein specific)
cyclo(L-Leu-L-Phe) + O2
Streptomyces noursei
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
albonoursin + H2O2
?
cyclo(L-Leu-L-Phe) + O2
Streptomyces noursei
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
?
cyclo(L-Leu-L-Phe) + O2
Streptomyces noursei ATCC 11455
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
albonoursin + H2O2
?
cyclo(L-Leu-L-Phe) + O2
Streptomyces noursei ATCC 11455
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
?
Purification (Commentary) (protein specific)
ammonium sulfate precipitation, Q-Sepharose column chromatography, EMD propyl column chromatography, and Superose 6 gel filtration
Streptomyces noursei
Storage Stability (protein specific)
-80°C, purified enzyme in the absence of any additive, several months, no loss of activity
Streptomyces noursei
22°C, purified enzyme in the absence of any additive, 24 h, no loss of activity
Streptomyces noursei
Substrates and Products (Substrate) (protein specific)
cyclo(L-Glu-Gly) + O2
3% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei
(4Z)-4-(3,6-dioxopiperazin-2-yl)butanoate + H2O2
?
cyclo(L-Glu-Gly) + O2
3% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei ATCC 11455
(4Z)-4-(3,6-dioxopiperazin-2-yl)butanoate + H2O2
?
cyclo(L-Leu-Gly) + O2
9% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei
(3Z)-3-(2-methylpropylidene)piperazine-2,5-dione + H2O2
?
cyclo(L-Leu-Gly) + O2
9% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei ATCC 11455
(3Z)-3-(2-methylpropylidene)piperazine-2,5-dione + H2O2
?
cyclo(L-Leu-L-Ala) + O2
13% mono-dehydro-products and 4% bis-dehydro products
722172
Streptomyces noursei
?
?
cyclo(L-Leu-L-Phe) + O2
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
722172
Streptomyces noursei
albonoursin + H2O2
?
cyclo(L-Leu-L-Phe) + O2
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
722172
Streptomyces noursei ATCC 11455
albonoursin + H2O2
?
cyclo(L-Leu-L-Phe) + O2
722172
Streptomyces noursei
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
?
cyclo(L-Leu-L-Phe) + O2
722172
Streptomyces noursei ATCC 11455
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
?
cyclo(L-Phe-Gly) + O2
36% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei
(3Z)-3-benzylidenepiperazine-2,5-dione + H2O2
?
cyclo(L-Phe-L-His) + O2
21% mono-dehydro-products and less than 1% bis-dehydro products
722172
Streptomyces noursei
?
?
cyclo(L-Ser-Gly) + O2
11% mono-dehydro-products and no bis-dehydro products
722172
Streptomyces noursei
(3Z)-3-(2-hydroxyethylidene)piperazine-2,5-dione + H2O2
?
cyclo(L-Trp-L-Trp) + O2
74% mono-dehydro-products and 14% bis-dehydro products
722172
Streptomyces noursei
?
?
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + O2
722172
Streptomyces noursei
albonoursin + H2O2
?
additional information
no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe
722172
Streptomyces noursei
?
?
additional information
no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe
722172
Streptomyces noursei ATCC 11455
?
?
Subunits (protein specific)
?
x * 23000, SDS-PAGE
Streptomyces noursei
?
x * 21066, calculated from amino acid sequence
Streptomyces noursei
Temperature Optimum [°C] (protein specific)
60
activity increases up to the maximum at 60°C followed by a substantial drop above this temperature
Streptomyces noursei
Turnover Number [1/s] (protein specific)
0.453
cyclo(L-Phe-L-His)
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
Streptomyces noursei
0.69
cyclo(L-Leu-L-Phe)
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
Streptomyces noursei
pH Optimum (protein specific)
pH Range (protein specific)
5.5
10.5
Streptomyces noursei
pH Stability (protein specific)
6
8.7
the enzyme activity is quite stable at neutral and basic pH values, whereas it decreases at acidic pH values. Residual activity is 75% after 6.5 h at pH 6.0
Streptomyces noursei
pI Value (protein specific)
Streptomyces noursei
isoelectric focusing
3.8
Other publictions for EC 1.3.3.13
744181
Li
Analysis of the biosynthesis ...
Nocardiopsis alba, Nocardiopsis alba ATCC BAA-2165
Arch. Microbiol.
196
765-774
2014
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1
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1
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4
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6
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1
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6
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3
3
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722021
Lautru
The albonoursin gene cluster o ...
Streptomyces noursei
Chem. Biol.
9
1355-1364
2002
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1
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1
1
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3
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1
1
1
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1
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1
1
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1
1
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722172
Gondry
Cyclic dipeptide oxidase from ...
Streptomyces noursei, Streptomyces noursei ATCC 11455
Eur. J. Biochem.
268
1712-1721
2001
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1
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16
2
1
1
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1
1
1
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1
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1
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2
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2
4
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1
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2
16
2
1
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2
1
1
1
1
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