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Information on EC 1.14.13.181 - 13-deoxydaunorubicin hydroxylase
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1.14.13.181 13-deoxydaunorubicin hydroxylaseIUBMB Comments
The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius show broad substrate specificity for structures based on an anthracycline aglycone, but have a strong preference for 4-methoxy anthracycline intermediates (13-deoxydaunorubicin and 13-dihydrodaunorubicin) over their 4-hydroxy analogues (13-deoxycarminomycin and 13-dihydrocarminomycin), as well as a preference for substrates hydroxylated at the C-13 rather than the C-14 position.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
+
+
=
+
+
2
Synonyms
cyp109a2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DoxA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
13-deoxydaunorubicin + NADPH + H+ + O2 = 13-dihydrodaunorubicin + NADP+ + H2O
-
-
-
-
13-dihydrodaunorubicin + NADPH + H+ + O2 = daunorubicin + NADP+ + 2 H2O
(2)
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
13-deoxydaunorubicin,NADPH:oxygen oxidoreductase (13-hydroxylating)
The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius show broad substrate specificity for structures based on an anthracycline aglycone, but have a strong preference for 4-methoxy anthracycline intermediates (13-deoxydaunorubicin and 13-dihydrodaunorubicin) over their 4-hydroxy analogues (13-deoxycarminomycin and 13-dihydrocarminomycin), as well as a preference for substrates hydroxylated at the C-13 rather than the C-14 position.
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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
13-deoxydaunorubicin + NADPH + H+ + O2
daunorubicinol + NADP+ + H2O
-
-
-
?
13-dihydrodaunorubicin + NADPH + H+ + O2
daunorubicin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
-
-
?
resveratrol + NADPH + H+ + O2
piceatannol + NADP+ + H2O
DoxA along with accessory enzymes ferrdoxin reductase and ferredoxin from spinach hydroxylates resveratrol at the 3'-position in vitro to produce piceatannol
-
-
?
13-deoxycarminomycin + NADPH + H+ + O2
13-dihydrocarminomycin + NADP+ + H2O
-
-
-
?
13-deoxycarminomycin + NADPH + H+ + O2
13-dihydrocarminomycin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin
-
-
?
13-deoxycarminomycin + NADPH + H+ + O2
13-dihydrocarminomycin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
-
-
?
13-deoxydaunorubicin + NADPH + H+ + O2
13-dihydrodaunorubicin + NADP+ + H2O
-
i.e. daunorubicinol
-
?
13-deoxydaunorubicin + NADPH + H+ + O2
13-dihydrodaunorubicin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin
-
-
?
13-deoxydaunorubicin + NADPH + H+ + O2
13-dihydrodaunorubicin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
-
-
?
13-dihydrocarminomycin + NADPH + H+ + O2
carminomycin + NADP+ + H2O
-
-
-
?
13-dihydrocarminomycin + NADPH + H+ + O2
carminomycin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin
-
-
?
13-dihydrocarminomycin + NADPH + H+ + O2
carminomycin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
-
-
?
13-dihydrodaunorubicin + NADPH + H+ + O2
daunorubicin + NADP+ + 2 H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin
-
-
?
13-dihydrodaunorubicin + NADPH + H+ + O2
daunorubicin + NADP+ + 2 H2O
i.e. daunorubicinol
-
-
?
daunomycin + NADPH + H+ + O2
doxorubicin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and 13-dihydrodaunorubicin and the hydroxylation at C-14 of daunorubicin
-
-
?
daunorubicin + NADPH + H+ + O2
doxorubicin + NADP+ + H2O
-
-
-
-
?
daunorubicin + NADPH + H+ + O2
doxorubicin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
-
-
?
additional information
?
-
the enzyme convert daunomycin to doxorubicin
-
-
?
additional information
?
-
daunomycinone (daunomycin aglycone), carminomycin, 13-dihydrocarminomycin, idarubicin, and aklavin are not apparent substrates for DoxA
-
-
?
additional information
?
-
the enzyme shows broad substrate specificity for anthracycline glycone substrates. DoxA has a strong preference for 4-methoxyanthracycline intermediates over their 4-hydroxy analogues as well as a preference for hydroxylation of the C-13 position over the C-14 position
-
-
?
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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
13-dihydrodaunorubicin + NADPH + H+ + O2
daunorubicin + NADP+ + 2 H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin
-
-
?
13-dihydrodaunorubicin + NADPH + H+ + O2
daunorubicin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
-
-
?
daunomycin + NADPH + H+ + O2
doxorubicin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and 13-dihydrodaunorubicin and the hydroxylation at C-14 of daunorubicin
-
-
?
additional information
?
-
the enzyme convert daunomycin to doxorubicin
-
-
?
13-deoxycarminomycin + NADPH + H+ + O2
13-dihydrocarminomycin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin
-
-
?
13-deoxycarminomycin + NADPH + H+ + O2
13-dihydrocarminomycin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
-
-
?
13-deoxydaunorubicin + NADPH + H+ + O2
13-dihydrodaunorubicin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin
-
-
?
13-deoxydaunorubicin + NADPH + H+ + O2
13-dihydrodaunorubicin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
-
-
?
13-dihydrocarminomycin + NADPH + H+ + O2
carminomycin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin
-
-
?
13-dihydrocarminomycin + NADPH + H+ + O2
carminomycin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
-
-
?
daunorubicin + NADPH + H+ + O2
doxorubicin + NADP+ + H2O
-
-
-
-
?
daunorubicin + NADPH + H+ + O2
doxorubicin + NADP+ + H2O
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and daunorubicinol and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
reduced flavin adenine dinucleotide, reduced flavin mononucleotide, and NADH do not substitute for NADPH in these reactions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
strongly inhibitory, inhibition is reversible after desalting
doxorubicin
completely inhibits DoxA activity at both 1 and 5 mM, competitive with respect to daunorubicinol oxidation
quinidine
inhibits DoxA oxidation of daunorubicinol by 11% at 1 mM. At 5 mM, it inhibits at more than 95%
sulfaphenazole
inhibits DoxA oxidation of daunorubicinol by 20% at 1 mM. At 5 mM, it inhibits at more than 95%
troleandomycin
inhibits DoxA oxidation of daunorubicinol by 35% at 1 mM. At 5 mM, it inhibits at more than 95%
additional information
high ionic strength buffers containing 100 mM sodium phosphate, also strongly inhibits DoxA activity. This effect is partially reversible after exchange into low ionic strength buffers, such as 20 mM N-(2-hydroxyethyl)piperazine-N9-(2-ethanesulfonic acid) (HEPES) or 10 mM sodium phosphate (pH 7.5). No inhibition: 4-methylpyrazole (1 or 5 mM), rhodomycin D (1-5 mM)
-
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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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
the block in the SPDHC mutant is probably due to a defective C-13 oxidation activity of DoxA. Since this mutant accumulates 13-dihydrocarminomycin, the C-13 hydroxylation activity of DoxA is probably not affected
physiological function
additional information
physiological function
DoxA catalyzes three steps in the daunorubicin/doxorubicin biosynthesis pathway: hydroxylation at C13 of 13-deoxycarminomycin and 13-deoxydaunorubicin, oxidation at C-13 of 13-dihydrocarminomycin and 13-dihydrodaunorubicin and the hydroxylation at C-14 of daunorubicin. It appears that the primary function of DoxA is to catalyze the enzymatic conversion of 13-deoxydaunorubicin to daunorubicin via daunorubicinol
physiological function
-
the cytochrome P450 monoxygenase DoxA is responsible for the hydroxylation of daunorubicin into doxorubicin
physiological function
-
the cytochrome P450 monoxygenase DoxA is responsible for the hydroxylation of daunorubicin into doxorubicin
-
additional information
-
protein-protein interaction and docking analysis of recombinant enzymes, structure homology modeling, DoxA active site structure, overview. Enzyme DoxA interacts with ist redox partners FDX1, FDR2, and FDX3
additional information
-
protein-protein interaction and docking analysis of recombinant enzymes, structure homology modeling, DoxA active site structure, overview. Enzyme DoxA interacts with ist redox partners FDX1, FDR2, and FDX3
-
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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). DOXA_STRC0
420
0
45646
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46096
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
stable for 1 h in presence of 20% (vol/vol) glycerol. All activity is lost after 30 min at room temperature in the absence of glycerol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme DoxA from Escherichia coli, copurification with His-tagged FDX1, FDR2, FDX3, and putidaredoxin and putidaredoxin reductase from Pseudomonas putida from Escherichia coli by cobalt affinity chromatography and ultrafiltration
-
the recombinant DoxA is purified to homogeneity from Streptomyces lividans transformed with a plasmid containing the Streptomyces sp. strain C5 doxA gene under the control of the strong SnpR-activated snpA promoter
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant overexpression of His-tagged enzyme DoxA along with its His-tagged redox partners from Streptomyces peucetius FDX1, FDR2, and FDX3, and the putidaredoxin and putidaredoxin reductase from Pseudomonas putida, that are essential equivalents of the class I type of bacterial electron-transport system, in Escherichia coli strain BL21(DE3) harboring the GroES/EL-expressing plasmid pGro7
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dickens, M.L.; Strohl, W.R.
Isolation and characterization of a gene from Streptomyces sp. strain C5 that confers the ability to convert daunomycin to doxorubicin on Streptomyces lividans TK24
J. Bacteriol.
178
3389-3395
1996
Streptomyces sp. (Q59971)
brenda
Dickens, M.L.; Priestley, N.D.; Strohl, W.R.
In vivo and in vitro bioconversion of epsilon-rhodomycinone glycoside to doxorubicin: functions of DauP, DauK, and DoxA
J. Bacteriol.
179
2641-2650
1997
Streptomyces sp. (Q59971)
brenda
Walczak, R.J.; Dickens, M.L.; Priestley, N.D.; Strohl, W.R.
Purification, properties, and characterization of recombinant Streptomyces sp. strain C5 DoxA, a cytochrome P-450 catalyzing multiple steps in doxorubicin biosynthesis
J. Bacteriol.
181
298-304
1999
Streptomyces sp. (Q59971)
brenda
Lomovskaya, N.; Otten, S.L.; Doi-Katayama, Y.; Fonstein, L.; Liu, X.C.; Takatsu, T.; Inventi-Solari, A.; Filippini, S.; Torti, F.; Colombo, A.L.; Hutchinson, C.R.
Doxorubicin overproduction in Streptomyces peucetius: cloning and characterization of the dnrU ketoreductase and dnrV genes and the doxA cytochrome P-450 hydroxylase gene
J. Bacteriol.
181
305-318
1999
Streptomyces peucetius (Q9ZAU3), Streptomyces peucetius ATCC 29050 (Q9ZAU3)
brenda
Vetrive,l K.S.; Dharmalingam, K.
Isolation and characterization of stable mutants of Streptomyces peucetius defective in daunorubicin biosynthesis
J. Genet.
80
31-38
2001
Streptomyces peucetius
brenda
Rimal, H.; Lee, S.; Lee, J.; Oh, T.
Understanding of real alternative redox partner of Streptomyces peucetius DoxA Prediction and validation using in silico and in vitro analyses
Arch. Biochem. Biophys.
585
64-74
2015
Streptomyces peucetius, Streptomyces peucetius ATCC 27952
brenda
Rimal, H.; Yu, S.C.; Lee, J.H.; Tokutaro, Y.; Oh, T.J.
Hydroxylation of resveratrol with DoxA in vitro an enzyme with the potential for the bioconversion of a bioactive stilbene
J. Microbiol. Biotechnol.
28
561-565
2018
Streptomyces peucetius (Q9ZAU3)
brenda
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