5.1.3.31: D-tagatose 3-epimerase
This is an abbreviated version!
For detailed information about D-tagatose 3-epimerase, go to the full flat file.
Word Map on EC 5.1.3.31
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5.1.3.31
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d-fructose
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d-psicose
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epimerization
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d-allulose
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cichorii
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ketohexose
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tumefaciens
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izumoring
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l-fuculose
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d-arabinose
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d-sorbose
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aldohexose
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bioproduction
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dpease
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l-xylulose
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synthesis
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loti
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mesorhizobium
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epimerizes
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low-calorie
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d-ribulose
- 5.1.3.31
- d-fructose
- d-psicose
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epimerization
- d-allulose
- cichorii
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ketohexose
- tumefaciens
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izumoring
- l-fuculose
- d-arabinose
- d-sorbose
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aldohexose
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bioproduction
- dpease
- l-xylulose
- synthesis
- loti
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mesorhizobium
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epimerizes
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low-calorie
- d-ribulose
Reaction
Synonyms
D-TE, DTE, ketose 3-epimerase, L-RE, L-ribulose 3-epimerase, L-TE, MJ1311, MJ1311p, PcDTE, RsDTE, RSP_3671, ycjR
ECTree
5.1.3.31 D-tagatose 3-epimeraseAdvanced search results
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results (Substrates Products
Substrates Products on EC 5.1.3.31 - D-tagatose 3-epimerase
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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
1-deoxy 3-keto D-galactitol
1-deoxy 3-keto D-allitol
7% activity compared to the activity with D-tagatose
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r
1-deoxy D-tagatose
1-deoxy D-sorbose
0.12% activity compared to the activity with D-tagatose
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r
1-deoxy L-tagatose
1-deoxy L-sorbose
0.14% activity compared to the activity with D-tagatose
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r
6-deoxy L-psicose
6-deoxy L-fructose
15.7% activity compared to the activity with D-tagatose
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r
D-fructose
D-psicose
specificity is highest with D-fructose and decreases for other substrates in the order: D-tagatose, D-psicose, D-ribulose, D-xylulose and D-sorbose. The equilibrium ratio between D-psicose and D-fructose is 23:77 after 24 h at 40°C
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r
D-fructose
D-psicose
best substrate for the recombinant wild-type enzyme
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r
D-fructose
D-psicose
Cereibacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
best substrate for the recombinant wild-type enzyme
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r
D-fructose
D-psicose
relative activity with D-fructose is 4.1% compared to L-ribulose, relative activity with D-psicose is 2.3% compared to L-ribulose
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r
D-psicose
D-fructose
relative activity with D-fructose is 4.1% compared to L-ribulose, relative activity with D-psicose is 2.3% compared to L-ribulose
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r
D-psicose
D-fructose
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epimerization of D-psicose at 60% compared to the activity with D-tagatose, epimerization of D-fructose at 20% compared to the activity with D-tagatose
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r
D-psicose
D-fructose
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epimerization of D-psicose at 60% compared to the activity with D-tagatose, epimerization of D-fructose at 20% compared to the activity with D-tagatose
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r
D-ribulose
D-xylulose
specificity is highest with D-fructose and decreases for other substrates in the order: D-tagatose, D-psicose, D-ribulose, D-xylulose and D-sorbose
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?
D-ribulose
D-xylulose
relative activity with D-ribulose is 20% compared to L-ribulose, relative activity with D-xylulose is 5.4% compared to L-ribulose
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r
D-ribulose
D-xylulose
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epimerization of D-ribulose at 90% compared to the activity with D-tagatose, epimerization of D-xylulose at 40% compared to the activity with D-tagatose
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r
D-ribulose
D-xylulose
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epimerization of D-ribulose at 90% compared to the activity with D-tagatose, epimerization of D-xylulose at 40% compared to the activity with D-tagatose
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r
D-tagatose
D-sorbose
specificity is highest with D-fructose and decreases for other substrates in the order: D-tagatose, D-psicose, D-ribulose, D-xylulose and D-sorbose
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r
D-tagatose
D-sorbose
best substrate for the recombinant enzyme mutant R118W
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r
D-tagatose
D-sorbose
relative activity with D-tagatose is 24% compared to L-ribulose, relative activity with D-sorbose is 6% compared to L-ribulose
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r
D-tagatose
D-sorbose
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epimerization of D-sorbose at 20% compared to the activity with D-tagatose
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r
D-tagatose
D-sorbose
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epimerization of D-sorbose at 20% compared to the activity with D-tagatose
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r
L-ribulose
L-xylulose
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epimerization of L-ribulose at 70% compared to the activity with D-tagatose, epimerization of L-xylulose at 20% compared to the activity with D-tagatose
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r
L-ribulose
L-xylulose
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epimerization of L-ribulose at 70% compared to the activity with D-tagatose, epimerization of L-xylulose at 20% compared to the activity with D-tagatose
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r
additional information
?
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no activity with D-fructose 6-phosphate and D-ribulose 5-phosphate
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?
additional information
?
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RsDTE wild-type shows lower Michaelis-Menten constant (Km), lower turnover number (kcat), but higher catalytic efficiency (kcat/Km) values for D-fructose than for D-psicose. The kcat/Km for D-fructose is 5.5fold higher than for D-psicose, indicating that enzyme RsDTE highly catalyzes D-fructose, although it is a D-tagatose 3-epimerase
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?
additional information
?
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RsDTE wild-type shows lower Michaelis-Menten constant (Km), lower turnover number (kcat), but higher catalytic efficiency (kcat/Km) values for D-fructose than for D-psicose. The kcat/Km for D-fructose is 5.5fold higher than for D-psicose, indicating that enzyme RsDTE highly catalyzes D-fructose, although it is a D-tagatose 3-epimerase
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?
additional information
?
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Cereibacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
RsDTE wild-type shows lower Michaelis-Menten constant (Km), lower turnover number (kcat), but higher catalytic efficiency (kcat/Km) values for D-fructose than for D-psicose. The kcat/Km for D-fructose is 5.5fold higher than for D-psicose, indicating that enzyme RsDTE highly catalyzes D-fructose, although it is a D-tagatose 3-epimerase
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?
additional information
?
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D-tagatose 3-epimerase (PcDTE) has a broad substrate specificity, it efficiently catalyzes the epimerization of not only D-tagatose to D-sorbose but also D-fructose to D-psicose (D-allulose) and also recognizes the deoxy sugars as substrates. Substrate recognition by the enzyme at the 1-, 2-, and 3-positions is responsible for enzymatic activity and substrate-enzyme interactions at the 4-, 5-, and 6-positions are not essential for the catalytic reaction of the enzyme leading to the broad substrate specificity of PcDTE. 1-Deoxy sugars may bind to the catalytic site in the inhibitor-binding mode. Ligand-binding structure at the catalytic site, overview. Binding structures of 6-deoxy L-psicose, 1-deoxy-3-oxo-D-galactitol, 1-deoxy-D-tagatose, 1-deoxy L-tagatose, L-erythrulose, D-talitol, and glycerol
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?
additional information
?
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D-tagatose 3-epimerase (PcDTE) has a broad substrate specificity, it efficiently catalyzes the epimerization of not only D-tagatose to D-sorbose but also D-fructose to D-psicose (D-allulose) and also recognizes the deoxy sugars as substrates. Substrate recognition by the enzyme at the 1-, 2-, and 3-positions is responsible for enzymatic activity and substrate-enzyme interactions at the 4-, 5-, and 6-positions are not essential for the catalytic reaction of the enzyme leading to the broad substrate specificity of PcDTE. 1-Deoxy sugars may bind to the catalytic site in the inhibitor-binding mode. Ligand-binding structure at the catalytic site, overview. Binding structures of 6-deoxy L-psicose, 1-deoxy-3-oxo-D-galactitol, 1-deoxy-D-tagatose, 1-deoxy L-tagatose, L-erythrulose, D-talitol, and glycerol
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?
additional information
?
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no activity with D-fructose 6-phosphate and D-ribulose 5-phosphate
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?
additional information
?
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no activity with D-fructose 6-phosphate and D-ribulose 5-phosphate
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?
