Information on EC 5.1.3.33 - 2-epi-5-epi-valiolone epimerase

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The expected taxonomic range for this enzyme is: Actinomyces

EC NUMBER
COMMENTARY hide
5.1.3.33
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RECOMMENDED NAME
GeneOntology No.
2-epi-5-epi-valiolone epimerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-epi-5-epi-valiolone = 5-epi-valiolone
show the reaction diagram
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
2-epi-5-epi-valiolone 2-epimerase
The enzyme, characterized from the bacterium Actinomyces sp. Lu 9419, is involved in the biosynthesis of the antitumor agent cetoniacytone A.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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
2-epi-5-epi-valiolone
5-epi-valiolone
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
2-epi-5-epi-valiolone
5-epi-valiolone
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
can effectively rescue the activity of H99G mutant enzyme from which the metal ion has been removed with 1,10-phenanthroline
Ni2+
can effectively rescue the activity of H99G mutant enzyme from which the metal ion has been removed with 1,10-phenanthroline
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
2 * 24000, polyhistidine-tagged protein, SDS-PAGE
48000
polyhistidine-tagged protein, gel filtration, nondenaturing-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli BL21(DE3)pLysS
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E151G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
E76G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
E76G/E151G
inactive mutant enzyme
E76G/H99G
inactive mutant enzyme
H14G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
H14G/E151G
inactive mutant enzyme
H14G/E76G
inactive mutant enzyme
H14G/H99G
inactive mutant enzyme
H99G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
H99G/E151G
inactive mutant enzyme
E151G
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in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
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E76G
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in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
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H14G
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in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
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H14G/E76G
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inactive mutant enzyme
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H99G
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in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
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