Information on EC 5.1.3.31 - D-tagatose 3-epimerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.1.3.31
-
RECOMMENDED NAME
GeneOntology No.
D-tagatose 3-epimerase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-psicose = D-fructose
show the reaction diagram
D-tagatose = D-sorbose
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
D-tagatose 3-epimerase
The enzymes isolated from the bacteria Pseudomonas cichorii [2], Pseudomonas sp. ST-24 [1], Rhodobacter sphaeroides [3] and Mesorhizobium loti [4] catalyse the epimerization of various ketoses at the C-3 position, interconverting D-fructose and D-psicose, D-tagatose and D-sorbose, D-ribulose and D-xylulose, and L-ribulose and L-xylulose. The specificity depends on the species. The enzymes from Pseudomonas cichorii and Rhodobacter sphaeroides require Mn2+ [2,3].
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-fructose
D-psicose
show the reaction diagram
D-psicose
D-fructose
show the reaction diagram
D-ribulose
D-xylulose
show the reaction diagram
D-tagatose
D-sorbose
show the reaction diagram
L-ribulose
L-xylulose
show the reaction diagram
L-xylulose
L-ribulose
show the reaction diagram
-
-
-
-
r
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
1 mM, about 90% inhibition
Hg2+
-
1 mM, about 90% inhibition
p-chloromercuribenzoate
-
1 mM, about 90% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
58
D-psicose
-
pH 8.0, 60C
55 - 140
D-tagatose
291
L-ribulose
-
pH 8.0, 60C
230
L-xylulose
-
pH 8.0, 60C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0057
D-psicose
Mesorhizobium loti
-
pH 8.0, 60C
0.057
D-tagatose
Mesorhizobium loti
-
pH 8.0, 60C
0.22
L-ribulose
Mesorhizobium loti
-
pH 8.0, 60C
0.14
L-xylulose
Mesorhizobium loti
-
pH 8.0, 60C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000098 - 0.00017
D-psicose
2077
0.00018 - 0.00041
D-tagatose
2197
0.000093 - 0.00076
L-ribulose
1621
0.00061
L-xylulose
Mesorhizobium loti
-
pH 8.0, 60C
1238
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
pH 7.5, 30C, substrate: D-tagatose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
30C
7.5
-
assay at
8
-
sodium phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10
pH 8.0: about 75% of maximal activity, pH 10.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
30C: about 70% of maximal activity, 50C: about 70% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
2 * 32000, SDS-PAGE
33000
-
2 * 33000, SDS-PAGE
64000
gel filtration
68000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
concentrated by ultrafiltration, sitting-drop vapour-diffusion method at 20C
-
crystal structures of the enzyme alone and in complexes with D-tagatose and D-fructose are determined at resolutions of 1.79, 2.28, and 2.06 A, respectively
-
crystals are obtained by the sitting-drop method at room temperature. The crystal belongs to the monoclinic space group P2(1), with unit-cell parameters a = 76.80, b = 94.92, c = 91.73 A , beta = 102.82
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
4C, 1 h, 65% loss of activity
727219
7 - 11
-
30C, 1 h, stable
727188
7
4C, 1 h, 25% loss of activity
727219
8 - 10
4C, 1 h, stable
727219
11
4C, 1 h, 30% loss of activity
727219
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
4 h, less than 10% loss of activity
45
4 h, about 65% loss of activity
50
1 h, about 50% loss of activity
55
30 min, about 80% loss of activity
60
-
10 min, stable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherchia coli
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y39A
-
the Vmax value of the mutant is about one-half of the Vmax value of the wild-type enzyme. The Km values for L-ribulose of the mutant and wild-type enzymes did not differ greatly
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
rare sugar production