Information on EC 5.3.99.11 - 2-keto-myo-inositol isomerase

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The expected taxonomic range for this enzyme is: Bacillus subtilis

EC NUMBER
COMMENTARY hide
5.3.99.11
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RECOMMENDED NAME
GeneOntology No.
2-keto-myo-inositol isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,4,6/3,5-pentahydroxycyclohexanone = 2D-2,3,5/4,6-pentahydroxycyclohexanone
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Inositol phosphate metabolism
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Microbial metabolism in diverse environments
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myo-, chiro- and scyllo-inositol degradation
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SYSTEMATIC NAME
IUBMB Comments
2,4,6/3,5-pentahydroxycyclohexanone 2-isomerase
Requires a divalent metal ion for activity. Mn2+, Fe2+ and Co2+ can be used. The enzyme, found in the bacterium Bacillus subtilis, is part of the myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
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
2,4,6/3,5-pentahydroxycyclohexanone
2D-2,3,5/4,6-pentahydroxycyclohexanone
show the reaction diagram
2-oxo-myo-inositol
1-oxo-D-chiroinositol
show the reaction diagram
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r
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
2,4,6/3,5-pentahydroxycyclohexanone
2D-2,3,5/4,6-pentahydroxycyclohexanone
show the reaction diagram
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of SeMet-derivatized enzyme are grown in hanging drops containing 1.50–1.75 M ammonium sulphate, 0.050 M Tris buffer, pH 8.00, 0.10 M sodium chloride, 1.0m EDTA, and 3.0 mM dithiothreitol. Crystal structure at 1.6 A resolution
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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