Information on EC 1.3.3.13 - albonoursin synthase

for references in articles please use BRENDA:EC1.3.3.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Streptomyces noursei

top print hide
EC NUMBER
COMMENTARY hide
1.3.3.13
-
top print hide
RECOMMENDED NAME
GeneOntology No.
albonoursin synthase
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cyclo(L-leucyl-L-phenylalanyl) + 2 O2 = albonoursin + 2 H2O2
show the reaction diagram
overall reaction
-
-
-
cyclo(L-leucyl-L-phenylalanyl) + O2 = cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
show the reaction diagram
(1a)
-
-
-
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + O2 = albonoursin + H2O2
show the reaction diagram
(1b)
-
-
-
top print hide
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].
top
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
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
-
13% mono-dehydro-products and 4% bis-dehydro products
-
-
?
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
-
-
-
ir
cyclo(L-Phe-Gly) + O2
(3Z)-3-benzylidenepiperazine-2,5-dione + H2O2
show the reaction diagram
-
36% mono-dehydro-products and no bis-dehydro products
-
-
?
cyclo(L-Phe-L-His) + O2
?
show the reaction diagram
-
21% mono-dehydro-products and less than 1% bis-dehydro products
-
-
?
cyclo(L-Ser-Gly) + O2
(3Z)-3-(2-hydroxyethylidene)piperazine-2,5-dione + H2O2
show the reaction diagram
-
11% mono-dehydro-products and no bis-dehydro products
-
-
?
cyclo(L-Trp-L-Trp) + O2
?
show the reaction diagram
-
74% mono-dehydro-products and 14% bis-dehydro products
-
-
?
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + O2
albonoursin + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
top print hide
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
-
-
-
ir
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.053
cyclo(L-Leu-L-Phe)
-
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
0.067
cyclo(L-Phe-L-His)
-
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
top print hide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.69
cyclo(L-Leu-L-Phe)
-
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
0.453
cyclo(L-Phe-L-His)
-
in 100 mM Tris/HCl buffer, pH 8.0, at 30°C
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10.5
-
-
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
activity increases up to the maximum at 60°C followed by a substantial drop above this temperature
top print hide
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
-
isoelectric focusing
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
-
x * 21000, SDS-PAGE
21066
-
x * 21066, calculated from amino acid sequence
23000
-
x * 23000, SDS-PAGE
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
722172
top print hide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified enzyme in the absence of any additive, several months, no loss of activity
-
22°C, purified enzyme in the absence of any additive, 24 h, no loss of activity
-
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Q-Sepharose column chromatography, EMD propyl column chromatography, and Superose 6 gel filtration
-
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.3.3.13)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)