Information on EC 1.14.13.200 - tetracenomycin A2 monooxygenase-dioxygenase

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The expected taxonomic range for this enzyme is: Streptomyces

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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
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
elloramycin biosynthesis
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Biosynthesis of type II polyketide products
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Biosynthesis of antibiotics
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tetracenomycin C biosynthesis
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elloramycin biosynthesis
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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.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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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
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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
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.082
NADH
pH 9.0, 25°C
0.26
NADPH
pH 9.0, 25°C
0.0018
tetracenomycin A2
pH 9.0, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00429
pH 9.0, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 9.5
in 50 mM Tris-HC1 or 50 nm ethanolamine-HCl buffer
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
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x * 58085, clalculated, x * 58000, SDS-PAGE
58085
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x * 58085, clalculated, x * 58000, SDS-PAGE
60000
1 * 60000, SDS-PAGE
61000
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 60000, SDS-PAGE
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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
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.200)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)