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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
DoxA, DoxA monooxygenase, 
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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
-
-
?
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
-
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
-
-
-
-
?
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
-
-
?
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
?
-
Q59971
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
-
-
-
-
?
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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
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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
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