Information on EC 5.3.1.12 - Glucuronate isomerase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
5.3.1.12
-
RECOMMENDED NAME
GeneOntology No.
Glucuronate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Glucuronate = D-fructuronate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
beta-D-glucuronide and D-glucuronate degradation
-
-
D-galacturonate degradation I
-
-
degradation of sugar acids
-
-
Metabolic pathways
-
-
pectin degradation III
-
-
Pentose and glucuronate interconversions
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glucuronate aldose-ketose-isomerase
Also converts D-galacturonate to D-tagaturonate.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-87-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
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
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 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-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
?
-
-
the enzyme does not participate in the metabolism of heparin or chondroitin sulfate
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S,3R,4S)-4-(hydroxycarbamoyl)-2,3,4-trihydroxybutanoate
-
-
1,10-phenanthroline
-
-
2,2'-dipyridyl
-
-
2-mercaptoethanol
-
-
arabinohydroxamate
-
-
cysteine
-
-
D-arabinarate
-
-
D-arabinaric acid
D-arabinohydroxamate
competitive inhibitor
EDTA
-
0.25 mM, 50% inhibition
glutathione
-
weak
L-Gulonic acid
competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 1.65
D-galacturonate
0.16 - 220
D-glucuronate
0.75
D-Tagaturonate
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
D-galacturonate
Bacillus halodurans
-
at 30C, pH 8.0
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
0.0021
(2S,3R,4S)-4-(hydroxycarbamoyl)-2,3,4-trihydroxybutanoate
-
at 30C, pH 8.0
0.000013 - 0.0055
D-arabinaric acid
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
6 - 8.2
-
pH 6.0: about 50% of maximal activity at pH 6.0 and 8.2
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
PDB
SCOP
CATH
ORGANISM
UNIPROT
Caulobacter crescentus (strain ATCC 19089 / CB15)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
-
x-ray crystallography
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complexed with Zn2+, vapour diffusion method, with 45% polypropylene glycol and 0.1 M Bis-Tris, pH 6.5
-
enzyme Bh0493 in complex with substrate D-glucuronate, D-fructuronate, or two inhibitory mimics of the cis-enediol intermediate, hanging drop method at room temperature, B16 mg/ml h0493 in 10 mM HEPES, pH 7.5, 150 mM NaCl, 10 mM methionine, 10% glycerol, 1.0 mM DTT, 0.2 mM ZnCl2, and the corresponding substrate or inhibitor at 40 mM, precipitation solutions are 20% PEG 3350 and 0.2 M sodium citrate, pH 6.0, or 25% PEG 3350, 0.1 M Tris, pH 8.5, and 0.2 M NaCl, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 6 months
-
0-3C, stable for several months without loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
of the wild type and recombinant protein, ammonium sulfate fractionation, gel filtration, and ion exchange chromatography
Resource Q column chromatography and Superdex 200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
overexpression in Escherichia coli
overexpression in Escherichia coli BL21(DE3)pLysS
-
ENGINEERING
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
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