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Information on EC 5.3.1.12 - glucuronate isomerase and Organism(s) Escherichia coli and UniProt Accession P0A8G3

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IUBMB Comments
Also converts D-galacturonate to D-tagaturonate.
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This record set is specific for:
Escherichia coli
UNIPROT: P0A8G3
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
uronate isomerase, bh0493, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glucuronate isomerase
-
Uronate isomerase
URI
D-Glucuronate isomerase
-
-
-
-
D-glucuronate ketol-isomerase
-
-
-
-
Glucuronate isomerase
-
-
-
-
Isomerase, glucuronate
-
-
-
-
Uronate isomerase
Uronic isomerase
-
-
-
-
additional information
URI is a member of the amidohydrolase superfamily, AHS
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Glucuronate = D-fructuronate
show the reaction diagram
reaction mechanisms in which an active site base abstracts the proton from C2 of D-glucuronate to form a cisenediol intermediate. The conjugate acid then transfers this proton to C1 of the cis-enediol intermediate to form D-fructuronate
D-Glucuronate = D-fructuronate
show the reaction diagram
reaction mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
D-glucuronate aldose-ketose-isomerase
Also converts D-galacturonate to D-tagaturonate.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-87-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Glucuronate
D-Fructuronate
show the reaction diagram
-
-
-
?
D-Fructuronate
?
show the reaction diagram
-
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
-
-
?
D-Galacturonate
?
show the reaction diagram
-
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
-
-
?
D-Galacturonate
D-Tagaturonate
show the reaction diagram
D-Glucuronate
?
show the reaction diagram
-
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
-
-
?
D-Glucuronate
D-Fructuronate
show the reaction diagram
D-Tagaturonate
?
show the reaction diagram
-
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Fructuronate
?
show the reaction diagram
-
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
-
-
?
D-Galacturonate
?
show the reaction diagram
-
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
-
-
?
D-Galacturonate
D-Tagaturonate
show the reaction diagram
-
-
-
r
D-Glucuronate
?
show the reaction diagram
-
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
-
-
?
D-Glucuronate
D-Fructuronate
show the reaction diagram
-
-
-
r
D-Tagaturonate
?
show the reaction diagram
-
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
enzyme contains 1 equiv of zinc per subunit
Co2+
-
stimulation is more potent at lower concentrations than stimulation by Mn2+
Mn2+
-
maximal stimulation is higher than stimulatipn by Zn2+ or Co2+, stimulation at low concentrations is lower than stimulation by Zn2+ and Co2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-arabinaric acid
competitive inhibitor
D-arabinohydroxamate
competitive inhibitor
L-Gulonic acid
competitive inhibitor
1,10-phenanthroline
-
-
2,2'-dipyridyl
-
-
2-mercaptoethanol
-
-
cysteine
-
-
EDTA
-
0.25 mM, 50% inhibition
glutathione
-
weak
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 8.5
D-glucuronate
0.8 - 1.65
D-galacturonate
0.05 - 220
D-glucuronate
0.75
D-tagaturonate
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 250
D-glucuronate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018 - 400
D-glucuronate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000013
D-arabinaric acid
apo and Zn2+ reconstituted enzyme
0.00067 - 0.00093
D-arabinohydroxamate
0.00043
L-Gulonic acid
Zn2+ reconstituted enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
-
-
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH 6.0: about 30% of maximal activity, pH 9.0: about 40% of maximal activity with D-galacturonate
7.5 - 9
-
pH 7.5: about 55% of maximal activity, pH 9.0: about 75% of maximal activity with glucuronate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SWISSPROT
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D238N
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
D412A
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
D412N
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H297A
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H297N
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H33A
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H33N
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H35A
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H35N
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H59A
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H59N
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R186K
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R186M
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R302K
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R302M
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R414K
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R414M
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
W381A
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
W381F
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
Y60A
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
Y60F
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of the wild type and recombinant protein, ammonium sulfate fractionation, gel filtration, and ion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
overexpression in Escherichia coli BL21(DE3)pLysS
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ashwell, G.; Wahba, A.J.; Hickman, J.
Uronic acid metabolism in bacteria: I. Purification and properties of uronic acid isomerase in Echerichia coli
J. Biol. Chem.
235
1559-1565
1960
Escherichia coli
Manually annotated by BRENDA team
Portalier, R.C.; Robert-Baudouy, J.M.; Nemoz, G.M.
Etudes de mutations affectant les genes de structure de l'isomerase uronique et de l'oxydoreductase altronique chez Escherichia coli K12
Mol. Gen. Genet.
128
301-319
1974
Escherichia coli
Manually annotated by BRENDA team
Linster, C.L.; Van Schaftingen, E.
A spectrophotometric assay of D-glucuronate based on Escherichia coli uronate isomerase and mannonate dehydrogenase
Protein Expr. Purif.
37
352-360
2004
Escherichia coli
Manually annotated by BRENDA team
Williams, L.; Nguyen, T.; Li, Y.; Porter, T.N.; Raushel, F.M.
Uronate isomerase: a nonhydrolytic member of the amidohydrolase superfamily with an ambivalent requirement for a divalent metal ion
Biochemistry
45
7453-7462
2006
Escherichia coli (P0A8G3)
Manually annotated by BRENDA team
Nguyen, T.T.; Fedorov, A.A.; Williams, L.; Fedorov, E.V.; Li, Y.; Xu, C.; Almo, S.C.; Raushel, F.M.
The mechanism of the reaction catalyzed by uronate isomerase illustrates how an isomerase may have evolved from a hydrolase within the amidohydrolase superfamily
Biochemistry
48
8879-8890
2009
Escherichia coli (A0A140N3B4), Escherichia coli, Halalkalibacterium halodurans
Manually annotated by BRENDA team