Information on EC 5.5.1.27 - D-galactarolactone cycloisomerase

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The expected taxonomic range for this enzyme is: Agrobacterium tumefaciens

EC NUMBER
COMMENTARY hide
5.5.1.27
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RECOMMENDED NAME
GeneOntology No.
D-galactarolactone cycloisomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-galactaro-1,4-lactone = 5-dehydro-4-deoxy-D-glucarate
show the reaction diagram
D-glucaro-1,4-lactone = 5-dehydro-4-deoxy-D-glucarate
show the reaction diagram
(2)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ascorbate and aldarate metabolism
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D-galacturonate degradation II
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D-glucuronate degradation II
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degradation of sugar acids
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SYSTEMATIC NAME
IUBMB Comments
D-galactaro-1,4-lactone lyase (ring-opening)
The enzyme, characterized from the bacterium Agrobacterium fabrum strain C58, is involved in degradation of D-galacturonate and D-glucuronate. Activity with D-galactaro-1,4-lactone is 4-fold higher than with D-glucaro-1,4-lactone.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-galactarolactone
3-deoxy-2-dehydro-L-threo-hexarate
show the reaction diagram
D-glucarolactone
3-deoxy-2-dehydro-L-threo-hexarate
show the reaction diagram
additional information
?
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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
D-galactarolactone
3-deoxy-2-dehydro-L-threo-hexarate
show the reaction diagram
D-glucarolactone
3-deoxy-2-dehydro-L-threo-hexarate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
compete inhibition at 1 mM, addition of M2+ to the apoenzyme results in a complete restoration of the original activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
8 * 41000, SDS-PAGE, 8 * 42600, about, sequence calculation
42600
8 * 41000, SDS-PAGE, 8 * 42600, about, sequence calculation
340900
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homooctamer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant Strep-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography and gel filtration, recombinant enzyme from Escherichia coli by ammonium sulfate fractionation, hydrophobic interaction chromatography, gel filtration, and two steps of anion exchange chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene gci, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli, recombinant expression of Strep-tagged enzyme in Escherichia coli strain BL21(DE3)