5.3.1.12: glucuronate isomerase
This is an abbreviated version!
For detailed information about glucuronate isomerase, go to the full flat file.
Word Map on EC 5.3.1.12
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5.3.1.12
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amidohydrolase
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isomerization
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cis-enediol
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d-galacturonate
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halodurans
- 5.3.1.12
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amidohydrolase
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isomerization
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cis-enediol
- d-galacturonate
- halodurans
Reaction
Synonyms
Bh0493, D-Glucuronate isomerase, D-glucuronate ketol-isomerase, Glucuronate isomerase, Isomerase, glucuronate, More, URI, Uronate isomerase, Uronic isomerase, UxaC
ECTree
5.3.1.12 glucuronate isomeraseAdvanced search results
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results (Substrates Products
Substrates Products on EC 5.3.1.12 - glucuronate isomerase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-Fructuronate
?
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first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
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?
D-Galacturonate
?
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first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
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?
D-Glucuronate
?
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first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
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?
D-Tagaturonate
?
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first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
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?
D-Glucuronate
D-Fructuronate
Halalkalibacterium halodurans
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the mononuclear metal center in the active site is ligated to the C6 carboxylate and the C5 hydroxyl group of the substrate, this hydroxyl group is also hydrogen-bonded to Asp355. The C2 and C3 hydroxyl groups of the substrate are hydrogen bonded to Arg357 and the carbonyl group at C1 is hydrogen bonded to Tyr50
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r
additional information
?
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chemical mechanism and active site structure, mutational analysis, overview
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?
additional information
?
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chemical mechanism and active site structure, mutational analysis, overview
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?
additional information
?
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Halalkalibacterium halodurans
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active site structure and molecular reaction mechanism, proton transfer from C2 of D-glucuronate to C1 that is initiated by the combined actions of Asp-355 from the end of ?-strand 8 and the C-5 hydroxyl of the substrate that is bound to the metal ion. Formation of the proposed cis-enediol intermediate is further facilitated by the shuttling of the proton between the C2 and C1 oxygens by the conserved Tyr50 and/or Arg355
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?
additional information
?
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the enzyme does not participate in the metabolism of heparin or chondroitin sulfate
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?
