Information on EC 1.14.13.200 - tetracenomycin A2 monooxygenase-dioxygenase

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The expected taxonomic range for this enzyme is: Streptomyces

EC NUMBER
COMMENTARY hide
1.14.13.200
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RECOMMENDED NAME
GeneOntology No.
tetracenomycin A2 monooxygenase-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tetracenomycin A2 + 2 O2 + 2 NAD(P)H + 2 H+ = tetracenomycin C + 2 NAD(P)+ + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
elloramycin biosynthesis
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tetracenomycin C biosynthesis
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Biosynthesis of type II polyketide products
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
tetracenomycin A2,NAD(P)H:O2 oxidoreductase (tetracenomycin C forming)
Isolated from the bacterium Streptomyces glaucescens. The enzyme was also isolated from the bacterium Streptomyces olivaceus, where it acts on 8-demethyltetracenomycin A2 (tetracenomycin B2) as part of elloramycin biosynthesis. The reaction involves a monooxygenase reaction which is followed by a dioxygenase reaction giving a gem-diol and an epoxide. Water opens the epoxide giving two hydroxy groups. The gem-diol eliminates water to give a ketone which is then reduced to a hydroxy group.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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enzyme is responsible for the hydroxylation of tetracenomycin A2 at positions C-4, C-4a, and C-12a to give tetracenomycin C, i.e. the final step in tetracenomycin C biosynthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
tetracenomycin A2 + 2 O2 + 2 NAD(P)H + 2 H+
tetracenomycin C + 2 NAD(P)+ + H2O
show the reaction diagram
tetracenomycin A2 + 2 O2 + 2 NADH + 2 H+
tetracenomycin C + 2 NAD+ + H2O
show the reaction diagram
tetracenomycin A2 i.e. methyl 10,12-dihydroxy-3,8-dimethoxy-1-methyl-6,11-dioxo-6,11-dihydrotetracene-2-carboxylate. The enzyme prefers NADPH over NADH as an electron donor
tetracenomycin C = methyl (6aR,7S,10aR)-6a,7,10a,12-tetrahydroxy-3,8-dimethoxy-1-methyl-6,10,11-trioxo-6,6a,7,10,10a,11-hexahydrotetracene-2-carboxylate
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?
tetracenomycin A2 + 2 O2 + 2 NADPH + 2 H+
tetracenomycin C + 2 NADP+ + H2O
show the reaction diagram
tetracenomycin A2 i.e. methyl 10,12-dihydroxy-3,8-dimethoxy-1-methyl-6,11-dioxo-6,11-dihydrotetracene-2-carboxylate. The enzyme prefers NADPH over NADH as an electron donor
tetracenomycin C = methyl (6aR,7S,10aR)-6a,7,10a,12-tetrahydroxy-3,8-dimethoxy-1-methyl-6,10,11-trioxo-6,6a,7,10,10a,11-hexahydrotetracene-2-carboxylate
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?
tetracenomycin B2 + 2 O2 + 2 NAD(P)H + 2 H+
8-demethyl tetracenomycin C + 2 NAD(P)+ + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
tetracenomycin A2 + 2 O2 + 2 NAD(P)H + 2 H+
tetracenomycin C + 2 NAD(P)+ + H2O
show the reaction diagram
Q7M0K6
biosynthesis tetracenomycin C, a polyketide antitumor antibiotic
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?
tetracenomycin B2 + 2 O2 + 2 NAD(P)H + 2 H+
8-demethyl tetracenomycin C + 2 NAD(P)+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
contains 1 mol of non-covalently bound FAD. The apoenzyme can be partially reconstituted in vitro by addition of FAD
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.082
NADH
pH 9.0, 25C
0.26
NADPH
pH 9.0, 25C
0.0018
tetracenomycin A2
pH 9.0, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00429
pH 9.0, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 9.5
in 50 mM Tris-HC1 or 50 nm ethanolamine-HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 10
pH 7.5: about 45% of maximal activity, pH 10: about 25% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 60000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein crystallizes in two different space groups, both with six monomers per asymmetric unit, resulting in large unit-cell parameters. Data from both the hexagonal and tetragonal crystal forms to 4.5 and 4.2 A resolution, respectively
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and Streptomyces lividans
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expression in Streptomyces lividans
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expression in Streptomyces lividans 1326
overexpression in Streptomyces lividans