BRENDA - Enzyme Database show
show all sequences of 1.3.3.13

Cyclic dipeptide oxidase from Streptomyces noursei. Isolation, purification and partial characterization of a novel, amino acyl alpha,beta-dehydrogenase

Gondry, M.; Lautru, S.; Fusai, G.; Meunier, G.; Menez, A.; Genet, R.; Eur. J. Biochem. 268, 1712-1721 (2001)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
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]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.053
-
cyclo(L-Leu-L-Phe)
in 100 mM Tris/HCl buffer, pH 8.0, at 30C
Streptomyces noursei
0.067
-
cyclo(L-Phe-L-His)
in 100 mM Tris/HCl buffer, pH 8.0, at 30C
Streptomyces noursei
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
21066
-
x * 21066, calculated from amino acid sequence
Streptomyces noursei
23000
-
x * 23000, SDS-PAGE
Streptomyces noursei
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces noursei
Q8GED9
-
-
Streptomyces noursei ATCC 11455
Q8GED9
-
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate precipitation, Q-Sepharose column chromatography, EMD propyl column chromatography, and Superose 6 gel filtration
Streptomyces noursei
Storage Stability
Storage Stability
Organism
-80C, purified enzyme in the absence of any additive, several months, no loss of activity
Streptomyces noursei
22C, purified enzyme in the absence of any additive, 24 h, no loss of activity
Streptomyces noursei
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
Subunits
Commentary
Organism
?
x * 21066, calculated from amino acid sequence; x * 23000, SDS-PAGE
Streptomyces noursei
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
60
-
activity increases up to the maximum at 60C followed by a substantial drop above this temperature
Streptomyces noursei
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.453
-
cyclo(L-Phe-L-His)
in 100 mM Tris/HCl buffer, pH 8.0, at 30C
Streptomyces noursei
0.69
-
cyclo(L-Leu-L-Phe)
in 100 mM Tris/HCl buffer, pH 8.0, at 30C
Streptomyces noursei
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Streptomyces noursei
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
10.5
-
Streptomyces noursei
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
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
Organism
Commentary
pI Value Maximum
pI Value
Streptomyces noursei
isoelectric focusing
-
3.8
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
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)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.053
-
cyclo(L-Leu-L-Phe)
in 100 mM Tris/HCl buffer, pH 8.0, at 30C
Streptomyces noursei
0.067
-
cyclo(L-Phe-L-His)
in 100 mM Tris/HCl buffer, pH 8.0, at 30C
Streptomyces noursei
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
21066
-
x * 21066, calculated from amino acid sequence
Streptomyces noursei
23000
-
x * 23000, SDS-PAGE
Streptomyces noursei
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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)
Commentary
Organism
ammonium sulfate precipitation, Q-Sepharose column chromatography, EMD propyl column chromatography, and Superose 6 gel filtration
Streptomyces noursei
Storage Stability (protein specific)
Storage Stability
Organism
-80C, purified enzyme in the absence of any additive, several months, no loss of activity
Streptomyces noursei
22C, purified enzyme in the absence of any additive, 24 h, no loss of activity
Streptomyces noursei
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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)
Subunits
Commentary
Organism
?
x * 21066, calculated from amino acid sequence; x * 23000, SDS-PAGE
Streptomyces noursei
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
60
-
activity increases up to the maximum at 60C followed by a substantial drop above this temperature
Streptomyces noursei
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.453
-
cyclo(L-Phe-L-His)
in 100 mM Tris/HCl buffer, pH 8.0, at 30C
Streptomyces noursei
0.69
-
cyclo(L-Leu-L-Phe)
in 100 mM Tris/HCl buffer, pH 8.0, at 30C
Streptomyces noursei
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Streptomyces noursei
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
10.5
-
Streptomyces noursei
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
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)
Organism
Commentary
pI Value Maximum
pI Value
Streptomyces noursei
isoelectric focusing
-
3.8
Other publictions for EC 1.3.3.13
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)
744181
Li
Analysis of the biosynthesis ...
Nocardiopsis alba, Nocardiopsis alba ATCC BAA-2165
Arch. Microbiol.
196
765-774
2014
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-
1
-
1
-
-
-
-
-
-
4
-
2
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
722021
Lautru
The albonoursin gene cluster o ...
Streptomyces noursei
Chem. Biol.
9
1355-1364
2002
-
-
1
-
-
-
-
-
-
-
1
1
-
3
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722172
Gondry
Cyclic dipeptide oxidase from ...
Streptomyces noursei, Streptomyces noursei ATCC 11455
Eur. J. Biochem.
268
1712-1721
2001
-
-
-
-
-
-
1
2
-
-
2
4
-
3
-
-
1
-
-
-
-
2
16
1
1
-
-
2
1
1
1
-
-
1
-
-
-
-
-
-
-
-
-
1
-
2
-
-
2
4
-
-
-
1
-
-
-
2
16
1
1
-
-
2
1
1
1
1
-
-
-
-
-
-