Information on EC 1.3.3.13 - albonoursin synthase

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The expected taxonomic range for this enzyme is: Streptomyces noursei

EC NUMBER
COMMENTARY hide
1.3.3.13
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RECOMMENDED NAME
GeneOntology No.
albonoursin synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cyclo(L-leucyl-L-phenylalanyl) + 2 O2 = albonoursin + 2 H2O2
show the reaction diagram
overall reaction
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cyclo(L-leucyl-L-phenylalanyl) + O2 = cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
show the reaction diagram
(1a)
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cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + O2 = albonoursin + H2O2
show the reaction diagram
(1b)
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SYSTEMATIC NAME
IUBMB Comments
cyclo(L-leucyl-L-phenylalanyl):oxygen oxidoreductase
A flavoprotein from the bacterium Streptomyces noursei. The enzyme can also oxidize several other cyclo dipeptides, the best being cyclo(L-tryptophyl-L-tryptophyl) and cyclo(L-phenylalanyl-L-phenylalanyl) [1,2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cyclo(L-Glu-Gly) + O2
(4Z)-4-(3,6-dioxopiperazin-2-yl)butanoate + H2O2
show the reaction diagram
cyclo(L-Leu-Gly) + O2
(3Z)-3-(2-methylpropylidene)piperazine-2,5-dione + H2O2
show the reaction diagram
cyclo(L-Leu-L-Ala) + O2
?
show the reaction diagram
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13% mono-dehydro-products and 4% bis-dehydro products
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?
cyclo(L-Leu-L-Phe) + O2
albonoursin + H2O2
show the reaction diagram
cyclo(L-Leu-L-Phe) + O2
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
show the reaction diagram
cyclo(L-leucyl-L-phenylalanyl) + O2
albonoursin + H2O2
show the reaction diagram
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ir
cyclo(L-Phe-Gly) + O2
(3Z)-3-benzylidenepiperazine-2,5-dione + H2O2
show the reaction diagram
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36% mono-dehydro-products and no bis-dehydro products
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?
cyclo(L-Phe-L-His) + O2
?
show the reaction diagram
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21% mono-dehydro-products and less than 1% bis-dehydro products
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?
cyclo(L-Ser-Gly) + O2
(3Z)-3-(2-hydroxyethylidene)piperazine-2,5-dione + H2O2
show the reaction diagram
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11% mono-dehydro-products and no bis-dehydro products
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?
cyclo(L-Trp-L-Trp) + O2
?
show the reaction diagram
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74% mono-dehydro-products and 14% bis-dehydro products
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?
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + O2
albonoursin + H2O2
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cyclo(L-Leu-L-Phe) + O2
albonoursin + H2O2
show the reaction diagram
cyclo(L-Leu-L-Phe) + O2
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
show the reaction diagram
cyclo(L-leucyl-L-phenylalanyl) + O2
albonoursin + H2O2
show the reaction diagram
Q8GED9
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ir
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.053
cyclo(L-Leu-L-Phe)
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in 100 mM Tris/HCl buffer, pH 8.0, at 30C
0.067
cyclo(L-Phe-L-His)
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in 100 mM Tris/HCl buffer, pH 8.0, at 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.69
cyclo(L-Leu-L-Phe)
Streptomyces noursei
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in 100 mM Tris/HCl buffer, pH 8.0, at 30C
0.453
cyclo(L-Phe-L-His)
Streptomyces noursei
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in 100 mM Tris/HCl buffer, pH 8.0, at 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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activity increases up to the maximum at 60C followed by a substantial drop above this temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
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isoelectric focusing
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.7
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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
722172
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, purified enzyme in the absence of any additive, several months, no loss of activity
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22C, purified enzyme in the absence of any additive, 24 h, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Q-Sepharose column chromatography, EMD propyl column chromatography, and Superose 6 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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