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Information on EC 1.14.13.215 - protoasukamycin 4-monooxygenase
for references in articles please use BRENDA:EC1.14.13.215
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.215 protoasukamycin 4-monooxygenase
IUBMB Comments
The enzyme, characterized from the bacterium Streptomyces nodosus subsp. asukaensis, is involved in the biosynthesis of the antibiotic asukamycin. Requires a flavin cofactor, with no preference among FMN, FAD or riboflavin. When flavin concentration is low, activity is enhanced by the presence of the NADH-dependent flavin-reductase AsuE2.
The expected taxonomic range for this enzyme is: Streptomyces nodosus
- 1.14.13.215
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epoxidized
- zeaxanthin
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drought
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xanthophyll
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epoxidase
showSynonyms
asue1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
asuE1
flavin-dependent protoasukamycin hydroxylase
asuE1
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protoasukamycin + NADH + H+ + O2 = 4-hydroxyprotoasukamycin + NAD+ + H2O
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SYSTEMATIC NAME
IUBMB Comments
protoasukamycin,NADH:oxygen oxidoreductase (4-hydroxylating)
The enzyme, characterized from the bacterium Streptomyces nodosus subsp. asukaensis, is involved in the biosynthesis of the antibiotic asukamycin. Requires a flavin cofactor, with no preference among FMN, FAD or riboflavin. When flavin concentration is low, activity is enhanced by the presence of the NADH-dependent flavin-reductase AsuE2.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protoasukamycin + NADH + H+ + O2
4-hydroxyprotoasukamycin + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
protoasukamycin + NADH + H+ + O2
4-hydroxyprotoasukamycin + NAD+ + H2O
Substrates: enzyme AsuE1 is a flavin-dependent protoasukamycin hydroxylase, that belongs to the family of single-component monooxygenases: a single enzyme catalyzes both the reduction of flavin by NADPH, and the hydroxylation using molecular oxygen and reduced flavin cofactor
Products: -
Products: -
?
protoasukamycin + NADH + H+ + O2
4-hydroxyprotoasukamycin + NAD+ + H2O
Substrates: NADH is the preferred cofactor, it reduces the flavin that gets oxidized in the hydroxylation of protoasukamycin, reaction chain overview
Products: -
Products: -
?
protoasukamycin + NADH + H+ + O2
4-hydroxyprotoasukamycin + NAD+ + H2O
Substrates: enzyme AsuE1 is a flavin-dependent protoasukamycin hydroxylase, that belongs to the family of single-component monooxygenases: a single enzyme catalyzes both the reduction of flavin by NADPH, and the hydroxylation using molecular oxygen and reduced flavin cofactor
Products: -
Products: -
?
protoasukamycin + NADH + H+ + O2
4-hydroxyprotoasukamycin + NAD+ + H2O
Substrates: NADH is the preferred cofactor, it reduces the flavin that gets oxidized in the hydroxylation of protoasukamycin, reaction chain overview
Products: -
Products: -
?
protoasukamycin + NADPH + H+ + O2
4-hydroxyprotoasukamycin + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
protoasukamycin + NADPH + H+ + O2
4-hydroxyprotoasukamycin + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protoasukamycin + NADH + H+ + O2
4-hydroxyprotoasukamycin + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
protoasukamycin + NADH + H+ + O2
4-hydroxyprotoasukamycin + NAD+ + H2O
Substrates: enzyme AsuE1 is a flavin-dependent protoasukamycin hydroxylase, that belongs to the family of single-component monooxygenases: a single enzyme catalyzes both the reduction of flavin by NADPH, and the hydroxylation using molecular oxygen and reduced flavin cofactor
Products: -
Products: -
?
protoasukamycin + NADH + H+ + O2
4-hydroxyprotoasukamycin + NAD+ + H2O
Substrates: enzyme AsuE1 is a flavin-dependent protoasukamycin hydroxylase, that belongs to the family of single-component monooxygenases: a single enzyme catalyzes both the reduction of flavin by NADPH, and the hydroxylation using molecular oxygen and reduced flavin cofactor
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
enzyme AsuE2 contains a trace amount of FMN at a molar ratio of 1:2000 (FMN:AsuE2) upon purification from Escherichia coli
additional information
enzyme AsuE1 is a flavin-dependent protoasukamycin hydroxylase, that displays no significant preference toward flavin cofactors, because FAD, FMN, and riboflavin are utilized efficiently in the catalysis
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protein AsuE2
endogenous protein AsuE2, UniProt-ID D7P5W0, is necessary for the full catalytic function of AsuE1 as a two-component flavoprotein hydroxylase. AsuE2 is a homologue of the flavin reductase PheA2, which recycles oxidized FADox and provides FADred to its hydroxylase partner PheA1 in the phenol hydroxylation in Bacillus thermoglucosidasius A7
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protein AsuE2
despite being a single-component monooxygenase, AsuE1 activity is enhanced by AsuE2, a pathway-specific flavin reductase, UniProt-ID D7P5W0, AsuE2 is encoded in the asu gene cluster. Enzyme AsuE2 might assist the catalysis of AsuE1 by providing a reduced form of flavin in Streptomyces nodosus
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0123
NADH
in presence of 0.01 mM FAD, recombinant enzyme, pH 7.0, 30°C
1.84
NADPH
in presence of 0.01 mM FAD, recombinant enzyme, pH 7.0, 30°C
0.0213
protoasukamycin
in presence of 0.01 mM FAD, recombinant enzyme, pH 7.0, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.113
NADH
in presence of 0.01 mM FAD, recombinant enzyme, pH 7.0, 30°C
0.324
NADPH
in presence of 0.01 mM FAD, recombinant enzyme, pH 7.0, 30°C
16.67
protoasukamycin
in presence of 0.01 mM FAD, recombinant enzyme, pH 7.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
evolution
enzyme AsuE1 belongs to the family of single-component monooxygenases: a single enzyme catalyzes both the reduction of flavin by NADPH, and the hydroxylation using molecular oxygen and reduced flavin cofactor
evolution
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enzyme AsuE1 belongs to the family of single-component monooxygenases: a single enzyme catalyzes both the reduction of flavin by NADPH, and the hydroxylation using molecular oxygen and reduced flavin cofactor
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malfunction
disruption of asuE2 significantly decreases the yield of asukamycin and results in the accumulation of protoasukamycin
malfunction
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disruption of asuE2 significantly decreases the yield of asukamycin and results in the accumulation of protoasukamycin
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metabolism
in the asukamycin metabolism, enzymes AsuE1 and AsuE2 catalyze the conversion of protoasukamycin to 4-hydroxyprotoasukamycin, which is epoxidized at C5-C6 by enzyme AsuE3 to the final product, asukamycin. Synthesis and structures of asukamycin and related metabolites, overview
metabolism
AsuE1 and AsuE3, both single-component flavin-dependent monooxygenases, catalyze the exquisite regio- and enantiospecific postpolyketide synthase (PKS) assembly oxygenations. AsuE1 installs a hydroxyl group on the 3,4-AHB ring to form a 4-hydroxyquinone moiety, which is epoxidized by AsuE3 to yield the epoxyquinone functionality. Despite being a single-component monooxygenase, AsuE1 activity is elicited by AsuE2, a pathway-specific flavin reductase
metabolism
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AsuE1 and AsuE3, both single-component flavin-dependent monooxygenases, catalyze the exquisite regio- and enantiospecific postpolyketide synthase (PKS) assembly oxygenations. AsuE1 installs a hydroxyl group on the 3,4-AHB ring to form a 4-hydroxyquinone moiety, which is epoxidized by AsuE3 to yield the epoxyquinone functionality. Despite being a single-component monooxygenase, AsuE1 activity is elicited by AsuE2, a pathway-specific flavin reductase
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ASUE1_STRNS
407
0
42773
Swiss-Prot
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chomatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of asukamycin biosynthetic gene cluster, including gene asuE1 encoding the enzyme, recombinant expression in Escherichia coli strain BW25113/pIJ790, heterologous expression of the complete gene cluster in the asukamycin-nonproducing Streptomyces lividans strain K4-114
gene asuE1, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rui, Z.; Sandy, M.; Jung, B.; Zhang, W.
Tandem enzymatic oxygenations in biosynthesis of epoxyquinone pharmacophore of manumycin-type metabolites
Chem. Biol.
20
879-887
2013
Streptomyces nodosus (D7P5V0), Streptomyces nodosus ATCC 29757 (D7P5V0)
brenda
Rui, Z.; Petrickova, K.; Skanta, F.; Pospisil, S.; Yang, Y.; Chen, C.Y.; Tsai, S.F.; Floss, H.G.; Petricek, M.; Yu, T.W.
Biochemical and genetic insights into asukamycin biosynthesis
J. Biol. Chem.
285
24915-24924
2010
Streptomyces nodosus (D7P5V0), Streptomyces nodosus
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.13.215)
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