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Literature summary 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

EC Number Inhibitors Comment Organism Structure
1.3.3.13 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.3.13 0.053
-
 cyclo(L-Leu-L-Phe) in 100 mM Tris/HCl buffer, pH 8.0, at 30°C Streptomyces noursei
1.3.3.13 0.067
-
 cyclo(L-Phe-L-His) in 100 mM Tris/HCl buffer, pH 8.0, at 30°C Streptomyces noursei

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.3.13 21066
-
 x * 21066, calculated from amino acid sequence Streptomyces noursei
1.3.3.13 23000
-
 x * 23000, SDS-PAGE Streptomyces noursei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.13 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
-
 ?
1.3.3.13 cyclo(L-Leu-L-Phe) + O2 Streptomyces noursei
-
 cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
-
 ?
1.3.3.13 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
-
 ?
1.3.3.13 cyclo(L-Leu-L-Phe) + O2 Streptomyces noursei ATCC 11455
-
 cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.13 Streptomyces noursei Q8GED9
-
-
1.3.3.13 Streptomyces noursei ATCC 11455 Q8GED9
-
-

Purification (Commentary)

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

Storage Stability

EC Number Storage Stability Organism
1.3.3.13 -80°C, purified enzyme in the absence of any additive, several months, no loss of activity Streptomyces noursei
1.3.3.13 22°C, purified enzyme in the absence of any additive, 24 h, no loss of activity Streptomyces noursei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.13 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
-
 ?
1.3.3.13 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
-
 ?
1.3.3.13 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
-
 ?
1.3.3.13 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
-
 ?
1.3.3.13 cyclo(L-Leu-L-Ala) + O2 13% mono-dehydro-products and 4% bis-dehydro products Streptomyces noursei ?
-
 ?
1.3.3.13 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
-
 ?
1.3.3.13 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
-
 ?
1.3.3.13 cyclo(L-Leu-L-Phe) + O2
-
 Streptomyces noursei cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
-
 ?
1.3.3.13 cyclo(L-Leu-L-Phe) + O2
-
 Streptomyces noursei ATCC 11455 cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
-
 ?
1.3.3.13 cyclo(L-Phe-Gly) + O2 36% mono-dehydro-products and no bis-dehydro products Streptomyces noursei (3Z)-3-benzylidenepiperazine-2,5-dione + H2O2
-
 ?
1.3.3.13 cyclo(L-Phe-L-His) + O2 21% mono-dehydro-products and less than 1% bis-dehydro products Streptomyces noursei ?
-
 ?
1.3.3.13 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
-
 ?
1.3.3.13 cyclo(L-Trp-L-Trp) + O2 74% mono-dehydro-products and 14% bis-dehydro products Streptomyces noursei ?
-
 ?
1.3.3.13 cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + O2
-
 Streptomyces noursei albonoursin + H2O2
-
 ?
1.3.3.13 additional information no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe Streptomyces noursei ?
-
 ?
1.3.3.13 additional information no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe Streptomyces noursei ATCC 11455 ?
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.3.3.13 cyclic dipeptide oxidase
-
 Streptomyces noursei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.3.13 60
-
 activity increases up to the maximum at 60°C followed by a substantial drop above this temperature Streptomyces noursei

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.3.13 0.453
-
 cyclo(L-Phe-L-His) in 100 mM Tris/HCl buffer, pH 8.0, at 30°C Streptomyces noursei
1.3.3.13 0.69
-
 cyclo(L-Leu-L-Phe) in 100 mM Tris/HCl buffer, pH 8.0, at 30°C Streptomyces noursei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.3.13 8
-
-
 Streptomyces noursei

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.3.3.13 5.5 10.5
-
 Streptomyces noursei

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.3.3.13 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

EC Number Organism Comment pI Value Maximum pI Value
1.3.3.13 Streptomyces noursei isoelectric focusing
-
 3.8