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Information on EC 1.3.3.13 - albonoursin synthase for references in articles please use BRENDA:EC1.3.3.13Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Actinobacteria
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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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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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cyclo(dipeptide):oxygen oxidoreductase
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AlbA
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cyclic dipeptide oxidase
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cyclic dipeptide oxidase
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cyclic dipeptide oxidase
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isolated from the guts of healthy honeybees in a year-round survey
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brenda
isolated from the guts of healthy honeybees in a year-round survey
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brenda
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UniProt
brenda
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UniProt
brenda
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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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cyclo(L-Glu-Gly) + O2
(4Z)-4-(3,6-dioxopiperazin-2-yl)butanoate + H2O2
cyclo(L-Leu-Gly) + O2
(3Z)-3-(2-methylpropylidene)piperazine-2,5-dione + H2O2
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-Leu-L-Phe) + O2
albonoursin + H2O2
cyclo(L-Leu-L-Phe) + O2
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
cyclo(L-leucyl-L-phenylalanyl) + 2 O2
albonoursin + 2 H2O2
cyclo(L-leucyl-L-phenylalanyl) + O2
albonoursin + H2O2
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ir
cyclo(L-methoxytyrosine-L-leucine) + 2 O2
? + 2 H2O2
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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?
additional information
?
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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-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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?
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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cyclo(L-Leu-L-Phe) + O2
albonoursin + H2O2
cyclo(L-Leu-L-Phe) + O2
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
cyclo(L-leucyl-L-phenylalanyl) + 2 O2
albonoursin + 2 H2O2
cyclo(L-leucyl-L-phenylalanyl) + O2
albonoursin + H2O2
Q8GED9
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ir
cyclo(L-methoxytyrosine-L-leucine) + 2 O2
? + 2 H2O2
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
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-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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?
cyclo(L-methoxytyrosine-L-leucine) + 2 O2
? + 2 H2O2
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?
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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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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
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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
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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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3.8
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isoelectric focusing
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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
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?
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x * 21000, SDS-PAGE
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x * 21066, calculated from amino acid sequence; x * 23000, SDS-PAGE
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x * 21066, calculated from amino acid sequence; x * 23000, SDS-PAGE
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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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-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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ammonium sulfate precipitation, Q-Sepharose column chromatography, EMD propyl column chromatography, and Superose 6 gel filtration
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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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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
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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
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ALBA_STRNR
219
23763
Swiss-Prot
A0A1V4IBE8_9FIRM
[Clostridium] thermoalcaliphilum
170
19251
TrEMBL
A0A1D3UGI7_TANFO
168
19682
TrEMBL
A0A1V5HEJ8_9BACT
173
19966
TrEMBL
A0A1V5ZXB6_9BACT
178
19792
TrEMBL
A0A136WGY7_9FIRM
168
19077
TrEMBL
A0A0P0GAM0_9BACE
415
45914
TrEMBL
A0A1V4IJ28_9CLOT
174
19723
TrEMBL
A0A0P8W1M1_9CLOT
187
21218
TrEMBL
A0A1V5QXT0_9PROT
170
18346
TrEMBL
A0A161XCD5_9CLOT
166
19108
TrEMBL
A0A1E7RTL9_BUTME
169
19340
TrEMBL
A0A1V5G3Q8_9BACT
172
19917
TrEMBL
A0A0J6VP72_9MYCO
123
13464
TrEMBL
A0A1V5SXN5_9BACT
173
19087
TrEMBL
A0A1V5IL89_9ACTN
179
20134
TrEMBL
A0A1V5YKY6_9CHLR
172
18375
TrEMBL
A0A1V4WTI5_9DELT
202
21885
TrEMBL
A0A1V4Y2J9_9DELT
185
20561
TrEMBL
A0A2T0BEC8_9CLOT
181
20394
TrEMBL
A0A1V5I3N9_9SPIR
186
20265
TrEMBL
A0A1V5U7W3_9BACT
203
21824
TrEMBL
A0A1F2PIL0_9FIRM
163
18170
TrEMBL
A0A168PNB3_9CLOT
180
20154
TrEMBL
A0A0M2H6R5_9MICO
193
20539
TrEMBL
A0A1V6JQC4_9BACT
193
21621
TrEMBL
A0A108TBK5_9BACE
415
45904
TrEMBL
A0A1V6GLI9_9BACT
169
18470
TrEMBL
A0A1V5PUI9_9ACTN
167
19165
TrEMBL
A0A0J6YMW2_9MYCO
236
26586
TrEMBL
A0A1V6GE41_9BACT
176
19061
TrEMBL
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Lautru, S.; Gondry, M.; Genet, R.; Pernodet, J.L.
The albonoursin gene cluster of S. noursei biosynthesis of diketopiperazine metabolites independent of nonribosomal peptide synthetases
Chem. Biol.
9
1355-1364
2002
Streptomyces noursei (Q8GED9), Streptomyces noursei
brenda
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
Eur. J. Biochem.
268
1712-1721
2001
Streptomyces noursei (Q8GED9), Streptomyces noursei, Streptomyces noursei ATCC 11455 (Q8GED9)
brenda
Li, Y.; Lai, Y.M.; Lu, Y.; Yang, Y.L.; Chen, S.
Analysis of the biosynthesis of antibacterial cyclic dipeptides in Nocardiopsis alba
Arch. Microbiol.
196
765-774
2014
Nocardiopsis alba, Nocardiopsis alba ATCC BAA-2165
brenda
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