Information on EC 1.14.11.52 - validamycin A dioxygenase

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The expected taxonomic range for this enzyme is: Streptomyces hygroscopicus subsp. limoneus

EC NUMBER
COMMENTARY hide
1.14.11.52
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RECOMMENDED NAME
GeneOntology No.
validamycin A dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
validamycin A + 2-oxoglutarate + O2 = validamycin B + succinate + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Acarbose and validamycin biosynthesis
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Biosynthesis of antibiotics
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validamycin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
validamycin-A,2-oxoglutarate:oxygen oxidoreductase (6'-hydroxylating)
The enzyme was characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus. Requires Fe2+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
validamycin A + 2-oxoglutarate + O2
validamycin B + succinate + CO2
show the reaction diagram
validoxylamine A + 2-oxoglutarate + O2
?
show the reaction diagram
the enzyme is also able to convert validoxylamine A to its hydroxylated derivative, albeit much less efficiently than the conversion of validamycin A to validamycin B
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?
additional information
?
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no products are observed when validamine, validamine 7-phosphate, or validoxylamine A 7'-phosphate are used as substrate
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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
validamycin A + 2-oxoglutarate + O2
validamycin B + succinate + CO2
show the reaction diagram
Q15JG7
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ni2+
atalytic activity is affected by Ni2+. A significant reduction of activity is observed when the protein is purified using Ni-NTA column. The activity can be restored by dialysis of the protein in a buffer solution containing 0.1 mM EDTA, followed by the addition of 0.2 mM of Fe2+ to the protein solution
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
2-oxoglutarate
pH 7.2, 30C, obtained from Hanes-Woolf plot
0.303
validamycin A
pH 7.2, 30C, obtained from Hanes-Woolf plot
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.97
2-oxoglutarate
Streptomyces hygroscopicus subsp. limoneus
Q15JG7
pH 7.2, 30C, obtained from Hanes-Woolf plot
0.97
validamycin A
Streptomyces hygroscopicus subsp. limoneus
Q15JG7
pH 7.2, 30C, obtained from Hanes-Woolf plot
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
the enzyme is most active in potassium phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
pH 6.5: 65% of maximal activity, pH 8.0: about 70% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43400
x * 43400, recombinantly His6-tagged protein, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43400, recombinantly His6-tagged protein, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inserted into an expression vector pRSET B to give pTMS005. The plasmid is then used to transform Escherichia coli BL21(DE3)pLysS