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
5.3.1.12
-
RECOMMENDED NAME
GeneOntology No.
Glucuronate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-Glucuronate = D-fructuronate
show the reaction diagram
-
-
-
-
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
P0A8G3
D-Glucuronate = D-fructuronate
show the reaction diagram
reaction mechanism, overview
-
D-Glucuronate = D-fructuronate
show the reaction diagram
reaction mechanism, overview
C6EHQ2, -
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
isomerization
-
-
-
-
isomerization
P0A8G3
-
isomerization
-
-
PATHWAY
KEGG Link
MetaCyc Link
beta-D-glucuronide and D-glucuronate degradation
-
D-galacturonate degradation I
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D-Glucuronate isomerase
-
-
-
-
D-glucuronate ketol-isomerase
-
-
-
-
Glucuronate isomerase
-
-
-
-
Glucuronate isomerase
P0A8G3
-
URI
C6EHQ2
-
Uronate isomerase
-
-
-
-
Uronate isomerase
-
-
Uronate isomerase
-
-
Uronate isomerase
C6EHQ2
-
Uronate isomerase
P0A8G3
URI
Uronic isomerase
-
-
-
-
UxaC
C6EHQ2
-
Isomerase, glucuronate
-
-
-
-
additional information
-
URI is a member of the amidohydrolase superfamily, AHS
additional information
C6EHQ2
URI is a member of the amidohydrolase superfamily, AHS
CAS REGISTRY NUMBER
COMMENTARY
9023-87-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene uxaC
UniProt
Manually annotated by BRENDA team
strain K-12, wild type and mutant strains
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
D-Tagaturonate
show the reaction diagram
-
-
-
-
-
D-Galacturonate
D-Tagaturonate
show the reaction diagram
-
-
-
-
D-Galacturonate
D-Tagaturonate
show the reaction diagram
-
-
-
-
?
D-Galacturonate
D-Tagaturonate
show the reaction diagram
-
-
-
-
r
D-Galacturonate
D-Tagaturonate
show the reaction diagram
C6EHQ2, -
-
-
-
r
D-Galacturonate
D-Tagaturonate
show the reaction diagram
-
r
-
-
-
D-Galacturonate
D-Tagaturonate
show the reaction diagram
-
r
-
-
-
D-Galacturonate
?
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-Glucuronate
D-Fructuronate
show the reaction diagram
-
-
-
-
?
D-Glucuronate
D-Fructuronate
show the reaction diagram
-
-
-
-
D-Glucuronate
D-Fructuronate
show the reaction diagram
-
-
-
-
-
D-Glucuronate
D-Fructuronate
show the reaction diagram
-
-
-
-
?
D-Glucuronate
D-Fructuronate
show the reaction diagram
-
-
-
-
r
D-Glucuronate
D-Fructuronate
show the reaction diagram
P0A8G3
-
-
-
?
D-Glucuronate
D-Fructuronate
show the reaction diagram
C6EHQ2, -
-
-
-
r
D-Glucuronate
D-Fructuronate
show the reaction diagram
-
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
-
-
r
D-Glucuronate
?
show the reaction diagram
-
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
-
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
C6EHQ2, -
chemical mechanism and active site structure, mutational analysis, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
D-Tagaturonate
show the reaction diagram
-
-
-
-
r
D-Galacturonate
D-Tagaturonate
show the reaction diagram
C6EHQ2, -
-
-
-
r
D-Galacturonate
?
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-Glucuronate
D-Fructuronate
show the reaction diagram
C6EHQ2, -
-
-
-
r
D-Glucuronate
?
show the reaction diagram
-
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism
-
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NADH
C6EHQ2, -
required
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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+
Zn2+
-
stimulation is more potent at lower concentrations than stimulation by Mn2+. Vmax is about 3times higher in presence of 0.1 mM Mn2+ than in presence of 0.01 mM Zn2+ or Co2+
Zn2+
P0A8G3
enzyme contains 1 equiv of zinc per subunit
Zn2+
-
contains 0.5 equivalents of Zn2+ per subunit
Zn2+
C6EHQ2, -
URI contains up to 1 equivalent
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2S,3R,4S)-4-(hydroxycarbamoyl)-2,3,4-trihydroxybutanoate
-
-
1,10-phenanthroline
-
-
2,2'-dipyridyl
-
-
2-mercaptoethanol
-
-
arabinohydroxamate
-
-
D-arabinarate
-
-
D-arabinaric acid
P0A8G3
competitive inhibitor
D-arabinaric acid
-
-
D-arabinohydroxamate
P0A8G3
competitive inhibitor
EDTA
-
0.25 mM, 50% inhibition
glutathione
-
weak
L-Gulonic acid
P0A8G3
competitive inhibitor
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.05
-
D-galacturonate
-
at 30C, pH 8.0
0.8
-
D-galacturonate
-
strain Hfr P4X
1.65
-
D-galacturonate
-
-
0.05
-
D-glucuronate
-
at 30C, pH 8.0
0.05
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H33N
0.16
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant Y60F
0.2
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H33A
0.29
-
D-glucuronate
-
in absence of added metal or chelator
0.3
-
D-glucuronate
P0A8G3
reconstituted with Co2+, 30C, pH 8
0.31
-
D-glucuronate
-
in presence of 0.01 mM Zn2+
0.4
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant D412A
0.41
-
D-glucuronate
-
in presence of 0.01 mM Co2+
0.48
-
D-glucuronate
P0A8G3
reconstituted with Mn2+, 30C, pH 8
0.49
-
D-glucuronate
P0A8G3
apoenzyme
0.5
-
D-glucuronate
P0A8G3
reconstituted with Zn2+, 30C, pH 8
0.5
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, wild-type enzyme
0.55
-
D-glucuronate
P0A8G3
reconstituted with Cd2+, 30C, pH 8
0.7
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H59A; pH 8.0, 25C, mutant H59N
0.82
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R414K
0.9
-
D-glucuronate
-
strain Hfr P4X
1
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant D412N
1.2
-
D-glucuronate
-
in presence of 0.1 mM Mn2+
1.3
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant D238N
1.4
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R414M
1.7
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant W381F
2.5
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R302K
2.6
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R186K
3.7
-
D-glucuronate
-
-
8.5
-
D-glucuronate
P0A8G3
reconstituted with Ni2+, 30C, pH 8
9.4
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H35N
10.21
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant Y60A
21
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant W381A
38
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R186M
39
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H35A
56
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H297N
200
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R302M
220
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H297A
0.75
-
D-Tagaturonate
-
-
additional information
-
additional information
C6EHQ2, -
primary isotope effects on the kinetic constants with D-glucuronate and the effects of changes in solvent viscosity are consistent with product release being the rate-limiting step
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.4
-
D-galacturonate
-
at 30C, pH 8.0
0.6
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant D412N; pH 8.0, 25C, mutant H33A; pH 8.0, 25C, mutant H59A
0.7
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H35A; pH 8.0, 25C, mutant R414M
2.1
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H33N
4
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H35N
4.7
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R186M
5.2
-
D-glucuronate
-
at 30C, pH 8.0
5.8
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R414K
9
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant D412A
10
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H297A
13.9
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant Y60A
15
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H59N
16
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant W381F
21.7
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant Y60F
30
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H297N
54
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R186K
60
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant D238N
160
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R302K
180
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R302M
196
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, wild-type enzyme
250
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant W381A
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.018
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H35A
9213
0.021
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant D412A
9213
0.043
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H297A
9213
0.054
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R414M
9213
0.06
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant D412N
9213
0.088
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R302M
9213
0.13
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R186M
9213
0.43
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H35N
9213
0.5
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H297N
9213
0.83
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H59A
9213
3
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H33A
9213
7.1
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R414K
9213
9.5
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant W381F
9213
12
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant W381A
9213
21
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H59N; pH 8.0, 25C, mutant R186K
9213
46
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant D238N
9213
47
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant H33N
9213
63
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant R302K
9213
66
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant Y60A
9213
140
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, mutant Y60F
9213
400
-
D-glucuronate
C6EHQ2, -
pH 8.0, 25C, wild-type enzyme
9213
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0021
-
(2S,3R,4S)-4-(hydroxycarbamoyl)-2,3,4-trihydroxybutanoate
-
at 30C, pH 8.0
0.000013
-
D-arabinaric acid
P0A8G3
apo and Zn2+ reconstituted enzyme
0.0055
-
D-arabinaric acid
-
at 30C, pH 8.0
0.00067
-
D-arabinohydroxamate
P0A8G3
Zn2+ reconstituted enzyme
0.00093
-
D-arabinohydroxamate
P0A8G3
apo enzyme
0.00043
-
L-Gulonic acid
P0A8G3
Zn2+ reconstituted enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
C6EHQ2, -
assay at
additional information
-
C6EHQ2, -
the pH-rate profiles for kcat and kcat/Km for URI from Escherichia coli are bellshaped and indicate that one group must be unprotonated and another residue must be protonated for catalytic activity
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8.2
-
pH 6.0: about 50% of maximal activity at pH 6.0 and 8.2
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
C6EHQ2, -
assay at
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
49000
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
trimer
-
x-ray crystallography
additional information
-
structure modelling, overview
additional information
C6EHQ2, -
structure modelling using the crystal structure of URI from Bacillus halodurans, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
0-3C, stable for several months without loss of activity
-
-20C, stable for at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Resource Q column chromatography and Superdex 200 gel filtration
-
of the wild type and recombinant protein, ammonium sulfate fractionation, gel filtration, and ion exchange chromatography
P0A8G3
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
overexpression in Escherichia coli
P0A8G3
overexpression in Escherichia coli BL21(DE3)pLysS
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D238N
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
D412A
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
D412N
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H297A
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H297N
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H33A
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H33N
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H35A
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H35N
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H59A
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R186K
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R186M
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R302K
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R302M
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R414K
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
R414M
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
W381A
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
W381F
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
Y60A
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
Y60F
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
H59N
C6EHQ2, -
site-directed mutagenesis, the mutant shows altered kinetics and zinc content compared to the wild-type enzyme
additional information
C6EHQ2, -
construction of mutants in association with the active site structure of URI from Bacillus halodurans