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Enzyme Nomenclature
Information on EC 1.3.3.13 - albonoursin synthase
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The expected taxonomic range for this enzyme is: Actinobacteria
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EC NUMBER 
COMMENTARY 
1.3.3.13
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RECOMMENDED NAME
GeneOntology No.
albonoursin synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclo(L-leucyl-L-phenylalanyl) + 2 O2 = albonoursin + 2 H2O2
overall reaction
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cyclo(L-leucyl-L-phenylalanyl) + O2 = cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
(1a)
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cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + O2 = albonoursin + H2O2
(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].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from the guts of healthy honeybees in a year-round survey
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
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the albABC gene operon deletion mutant of Nocariopsis alba cannot produce cyclic dipeptides, cyclo(DELTAPhe-DELTALeu) i.e. albonoursin, and cyclo(DELTAmTyr-DELTALeu)
malfunction
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the albABC gene operon deletion mutant of Nocariopsis alba cannot produce cyclic dipeptides, cyclo(DELTAPhe-DELTALeu) i.e. albonoursin, and cyclo(DELTAmTyr-DELTALeu)
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metabolism
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the albonoursin biosynthetic gene cluster is involved in the regulated biosynthesis of antibacterial cyclic dipeptides in Nocardiopsis alba
metabolism
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the albonoursin biosynthetic gene cluster is involved in the regulated biosynthesis of antibacterial cyclic dipeptides in Nocardiopsis alba
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physiological function
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the enzyme is required for biosynthesis of antibacterial cyclic dipeptides, cyclo(DELTAPhe-DELTALeu) i.e. albonoursin, and cyclo(DELTAmTyr-DELTALeu)
physiological function
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the enzyme is required for biosynthesis of antibacterial cyclic dipeptides, cyclo(DELTAPhe-DELTALeu) i.e. albonoursin, and cyclo(DELTAmTyr-DELTALeu)
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cyclo(L-Leu-L-Ala) + O2
?
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13% mono-dehydro-products and 4% bis-dehydro products
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-
?
cyclo(L-Phe-Gly) + O2
(3Z)-3-benzylidenepiperazine-2,5-dione + H2O2
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36% mono-dehydro-products and no bis-dehydro products
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-
?
cyclo(L-Phe-L-His) + O2
?
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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
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11% mono-dehydro-products and no bis-dehydro products
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-
?
cyclo(L-Trp-L-Trp) + O2
?
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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
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-
-
?
cyclo(L-Glu-Gly) + O2
(4Z)-4-(3,6-dioxopiperazin-2-yl)butanoate + H2O2
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3% mono-dehydro-products and no bis-dehydro products
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-
?
cyclo(L-Glu-Gly) + O2
(4Z)-4-(3,6-dioxopiperazin-2-yl)butanoate + H2O2
3% mono-dehydro-products and no bis-dehydro products
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-
?
cyclo(L-Leu-Gly) + O2
(3Z)-3-(2-methylpropylidene)piperazine-2,5-dione + H2O2
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9% mono-dehydro-products and no bis-dehydro products
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-
?
cyclo(L-Leu-Gly) + O2
(3Z)-3-(2-methylpropylidene)piperazine-2,5-dione + H2O2
9% mono-dehydro-products and no bis-dehydro products
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-
?
cyclo(L-Leu-L-Phe) + O2
albonoursin + H2O2
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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
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-
?
cyclo(L-Leu-L-Phe) + O2
albonoursin + H2O2
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
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?
cyclo(L-Leu-L-Phe) + O2
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
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?
cyclo(L-Leu-L-Phe) + O2
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
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-
-
?
cyclo(L-leucyl-L-phenylalanyl) + 2 O2
albonoursin + 2 H2O2
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?
cyclo(L-methoxytyrosine-L-leucine) + 2 O2
? + 2 H2O2
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?
additional information
?
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albonoursin is then methoxylated to cyclo(L-methoxytyrosine-L-leucine) by O-methyltranferases, encoded by genes B005_4460 and B005_4464, termed albM1 and albM2
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additional information
?
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albonoursin is then methoxylated to cyclo(L-methoxytyrosine-L-leucine) by O-methyltranferases, encoded by genes B005_4460 and B005_4464, termed albM1 and albM2
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additional information
?
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no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe
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additional information
?
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no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cyclo(L-Leu-L-Phe) + O2
albonoursin + H2O2
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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
-
-
?
cyclo(L-Leu-L-Phe) + O2
albonoursin + H2O2
Q8GED9
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
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?
cyclo(L-Leu-L-Phe) + O2
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
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?
cyclo(L-Leu-L-Phe) + O2
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
Q8GED9
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?
cyclo(L-leucyl-L-phenylalanyl) + 2 O2
albonoursin + 2 H2O2
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?
cyclo(L-methoxytyrosine-L-leucine) + 2 O2
? + 2 H2O2
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?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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activity increases up to the maximum at 60°C followed by a substantial drop above this temperature
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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x * 21066, calculated from amino acid sequence; x * 23000, SDS-PAGE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
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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
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
LITERATURE
additional information
additional information
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generation of an albABC gene deletion mutant YL001 of Nocardiopsis alba, genetic organization, overview. Strain YL001 show no significant difference from the wild-type in colonial morphology, and it has a slightly vibrant growth on the MS agar, production of the cyclic dipeptides is abolished in the DELTAalbABC mutant
additional information
-
generation of an albABC gene deletion mutant YL001 of Nocardiopsis alba, genetic organization, overview. Strain YL001 show no significant difference from the wild-type in colonial morphology, and it has a slightly vibrant growth on the MS agar, production of the cyclic dipeptides is abolished in the DELTAalbABC mutant
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.3.13)
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