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Literature summary for 1.3.3.13 extracted from

  • Gondry, M.; Lautru, S.; Fusai, G.; Meunier, G.; Menez, A.; Genet, R.
    Cyclic dipeptide oxidase from Streptomyces noursei. Isolation, purification and partial characterization of a novel, amino acyl alpha,beta-dehydrogenase (2001), Eur. J. Biochem., 268, 1712-1721.
    View publication on PubMed

Inhibitors

Inhibitors Comment 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 Comment Organism Structure
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment Textmining
Streptomyces noursei Q8GED9
-
-
Streptomyces noursei ATCC 11455 Q8GED9
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, Q-Sepharose column chromatography, EMD propyl column chromatography, and Superose 6 gel filtration Streptomyces noursei

Storage Stability

Storage Stability Organism
-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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclo(L-Glu-Gly) + O2 3% mono-dehydro-products and no bis-dehydro products 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 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 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 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 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 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 Streptomyces noursei ATCC 11455 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 cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
-
?
cyclo(L-Phe-Gly) + O2 36% mono-dehydro-products and no bis-dehydro products 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 Streptomyces noursei ?
-
?
cyclo(L-Ser-Gly) + O2 11% mono-dehydro-products and no bis-dehydro products 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 Streptomyces noursei ?
-
?
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + O2
-
Streptomyces noursei albonoursin + H2O2
-
?
additional information no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe Streptomyces noursei ?
-
?
additional information no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe Streptomyces noursei ATCC 11455 ?
-
?

Subunits

Subunits Comment Organism
? x * 23000, SDS-PAGE Streptomyces noursei
? x * 21066, calculated from amino acid sequence Streptomyces noursei

Synonyms

Synonyms Comment Organism
cyclic dipeptide oxidase
-
Streptomyces noursei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
activity increases up to the maximum at 60°C 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 Comment Organism Structure
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 Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Streptomyces noursei

pH Range

pH Minimum pH Maximum Comment Organism
5.5 10.5
-
Streptomyces noursei

pH Stability

pH Stability pH Stability Maximum Comment 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 Comment pI Value Maximum pI Value
Streptomyces noursei isoelectric focusing
-
3.8