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Information on EC 1.3.3.13 - albonoursin synthase
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1.3.3.13 albonoursin synthaseIUBMB Comments
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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The expected taxonomic range for this enzyme is: Actinobacteria
Reaction Schemes
Synonyms
AlbA, cyclic dipeptide oxidase, cyclo(dipeptide):oxygen oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AlbA
cyclic dipeptide oxidase
cyclo(dipeptide):oxygen oxidoreductase
-
-
-
-
AlbA
-
-
-
-
cyclic dipeptide oxidase
-
-
-
-
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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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-
-
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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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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
?
-
13% mono-dehydro-products and 4% bis-dehydro products
-
-
?
cyclo(L-Phe-Gly) + O2
(3Z)-3-benzylidenepiperazine-2,5-dione + H2O2
-
36% mono-dehydro-products and no bis-dehydro products
-
-
?
cyclo(L-Phe-L-His) + O2
?
-
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
-
11% mono-dehydro-products and no bis-dehydro products
-
-
?
cyclo(L-Trp-L-Trp) + O2
?
-
74% mono-dehydro-products and 14% bis-dehydro products
-
-
?
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + O2
albonoursin + H2O2
-
-
-
-
?
cyclo(L-4-O-methyltyrosine-L-leucine) + 2 O2
? + 2 H2O2
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
-
?
cyclo(L-leucyl-L-phenylalanyl) + 2 O2
albonoursin + 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
?
-
no activity towards N-acetyl-L-Phe-L-Leu and N-actely-L-Leu-L-Phe
-
-
-
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NATURAL SUBSTRATE
NATURAL 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-4-O-methyltyrosine-L-leucine) + 2 O2
? + 2 H2O2
-
-
-
-
?
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
-
-
?
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
-
-
?
cyclo(L-Leu-L-Phe) + O2
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
-
-
-
-
?
cyclo(L-Leu-L-Phe) + O2
cyclo[(Z)-alpha,beta-didehydrophenylalanyl-L-leucyl] + H2O2
Q8GED9
-
-
-
?
cyclo(L-leucyl-L-phenylalanyl) + 2 O2
albonoursin + 2 H2O2
-
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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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
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
the albABC gene operon deletion mutant of Nocariopsis alba cannot produce cyclic dipeptides, cyclo(DELTAPhe-DELTALeu) i.e. albonoursin, and cyclo(DELTAmTyr-DELTALeu)
malfunction
-
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
-
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
-
the enzyme is required for biosynthesis of antibacterial cyclic dipeptides, cyclo(DELTAPhe-DELTALeu) i.e. albonoursin, and cyclo(DELTAmTyr-DELTALeu)
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A1V5QXT0_9PROT
170
0
18346
TrEMBL
A0A1V5V038_9BACT
186
2
21026
TrEMBL
A0A4Z0Y1H8_9FIRM
166
0
18586
TrEMBL
A0A1V5IQ28_9BACT
174
0
19544
TrEMBL
A0A1V6GE41_9BACT
176
0
19061
TrEMBL
A0A1V5YEF6_9CHLR
168
0
18569
TrEMBL
A0A1V6K7J3_9BACT
175
0
19910
TrEMBL
A0A1V6F027_9BACT
182
0
20904
TrEMBL
A0A1V5HEJ8_9BACT
173
0
19966
TrEMBL
A0A1V5ZXB6_9BACT
178
0
19792
TrEMBL
A0A1V5H6A5_9DELT
184
0
19976
TrEMBL
A0A0M2H6R5_9MICO
193
0
20539
TrEMBL
A0A1V6GLI9_9BACT
169
0
18470
TrEMBL
A0A1V6JQC4_9BACT
193
0
21621
TrEMBL
A0A1V5IL89_9ACTN
179
0
20134
TrEMBL
A0A1V5I3N9_9SPIR
186
0
20265
TrEMBL
A0A1V5YKY6_9CHLR
172
0
18375
TrEMBL
A0A1V4IBE8_9FIRM
[Clostridium] thermoalcaliphilum
170
0
19251
TrEMBL
A0A1V6JIC6_9BACT
175
0
19302
TrEMBL
A0A1V5PUI9_9ACTN
167
0
19165
TrEMBL
A0A1V6BFK6_9BACT
173
0
19521
TrEMBL
A0A1V4WTI5_9DELT
202
0
21885
TrEMBL
A0A1V5G3Q8_9BACT
172
0
19917
TrEMBL
A0A0J6VP72_9MYCO
123
0
13464
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 21066, calculated from amino acid sequence; x * 23000, SDS-PAGE
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
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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
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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