Information on EC 1.3.3.13 - albonoursin synthase

for references in articles please use BRENDA:EC1.3.3.13
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The expected taxonomic range for this enzyme is: Actinobacteria

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
isolated from the guts of healthy honeybees in a year-round survey
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Manually annotated by BRENDA team
isolated from the guts of healthy honeybees in a year-round survey
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
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) + 2 O2
albonoursin + 2 H2O2
show the reaction diagram
cyclo(L-leucyl-L-phenylalanyl) + O2
albonoursin + H2O2
show the reaction diagram
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ir
cyclo(L-methoxytyrosine-L-leucine) + 2 O2
? + 2 H2O2
show the reaction diagram
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) + 2 O2
albonoursin + 2 H2O2
show the reaction diagram
cyclo(L-leucyl-L-phenylalanyl) + O2
albonoursin + H2O2
show the reaction diagram
Q8GED9
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ir
cyclo(L-methoxytyrosine-L-leucine) + 2 O2
? + 2 H2O2
show the reaction diagram
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 30°C
0.067
cyclo(L-Phe-L-His)
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in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.69
cyclo(L-Leu-L-Phe)
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in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
0.453
cyclo(L-Phe-L-His)
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in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
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 60°C followed by a substantial drop above this temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
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x * 21000, SDS-PAGE
21066
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x * 21066, calculated from amino acid sequence
23000
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x * 23000, SDS-PAGE
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
-80°C, purified enzyme in the absence of any additive, several months, no loss of activity
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22°C, 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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the enzyme is encoded in the albonoursin biosynthetic gene cluster, albABC, genes albAB encode units for a cyclic dipeptide oxidase complex, responsible for generating two dehydrogenated double bonds
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information