Information on EC 1.13.12.22 - deoxynogalonate monooxygenase

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The expected taxonomic range for this enzyme is: Streptomyces nogalater

EC NUMBER
COMMENTARY hide
1.13.12.22
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RECOMMENDED NAME
GeneOntology No.
deoxynogalonate monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
deoxynogalonate + O2 = nogalonate + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of type II polyketide products
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SYSTEMATIC NAME
IUBMB Comments
deoxynogalonate:oxygen oxidoreductase
The enzyme, characterized from the bacterium Streptomyces nogalater, is involved in the biosynthesis of the aromatic polyketide nogalamycin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate + O2
[4,5-dihydroxy-9,10-dioxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate + 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
[4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate + O2
[4,5-dihydroxy-9,10-dioxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate + H2O
show the reaction diagram
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the enzyme is involved in the biosynthesis of the aromatic polyketide nogalamycin
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CaCl2
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0.1 mM, 9% inhibition
CoSO4
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0.1 mM, 10% inhibition
CuSO4
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0.1 mM, 99% inhibition
EDTA
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1 mM, 8% inhibition
FeSO4
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0.1 mM, 31% inhibition
MgSO4
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0.1 mM, 7% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.068 - 0.22
[4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 1.5
[4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.068 - 15
[4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate
191584
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop or hanging-drop vapour-diffusion method, the enzyme is crystallized in space group P2(1)2(1)2, with unit-cell parameters a = 58.8, b = 114.1, c = 49.5 A, the crystals diffract to 2.4 A resolution. The selenomethionine-substituted mutant F40M/L89M crystallizes in the same space group as the native enzyme
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H49A
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kcat/Km for [4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate is 13% compared to the activity of recombinant wild-type enzyme with N-terminal polyhistidine tag
N18A
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kcat/Km for [4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate is 1.5% compared to the activity of recombinant wild-type enzyme with N-terminal polyhistidine tag
N63A
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kcat/Km for [4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate is 1.5% compared to the activity of recombinant wild-type enzyme with N-terminal polyhistidine tag
R90E
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kcat/Km for [4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate is 17% compared to the activity of recombinant wild-type enzyme with N-terminal polyhistidine tag
W67F
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kcat/Km for [4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate is 0.5% compared to the activity of recombinant wild-type enzyme with N-terminal polyhistidine tag