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Information on EC 5.1.3.31 - D-tagatose 3-epimerase and Organism(s) Cereibacter sphaeroides and UniProt Accession C1KKR1
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5.1.3.31 D-tagatose 3-epimeraseIUBMB Comments
The enzymes isolated from the bacteria Pseudomonas cichorii , Pseudomonas sp. ST-24 , Rhodobacter sphaeroides and Mesorhizobium loti 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].
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Word Map
- 5.1.3.31
- d-fructose
- d-psicose
-
epimerization
- d-allulose
- cichorii
-
ketohexose
- tumefaciens
-
izumoring
- l-fuculose
- d-arabinose
- d-sorbose
-
aldohexose
-
bioproduction
- dpease
- l-xylulose
- synthesis
- loti
-
mesorhizobium
-
epimerizes
-
low-calorie
- d-ribulose
The taxonomic range for the selected organisms is: Cereibacter sphaeroides
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
d-tagatose 3-epimerase, l-ribulose 3-epimerase, ketose 3-epimerase, rsdte, pcdte, mj1311p, mj1311, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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].
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
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
-
-
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
-
-
?
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
-
-
r
D-fructose
D-psicose
best substrate for the recombinant wild-type enzyme
-
-
r
D-tagatose
D-sorbose
best substrate for the recombinant enzyme mutant R118W
-
-
r
additional information
?
-
no activity with D-fructose 6-phosphate and D-ribulose 5-phosphate
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
dependent on, activates at 0.1 mM, metalloenzyme, Mn2+ is the most effective activating divalent cation
additional information
additional information
no effect on enzyme activity by Mg2+ at .1 mM
additional information
-
no effect on enzyme activity by Mg2+ at .1 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 10
pH 8.0: about 75% of maximal activity, pH 10.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
30°C: about 70% of maximal activity, 50°C: about 70% of maximal activity
20 - 70
half-maximal activity at 20°C, near inactivation at 70°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the D-tagatose 3-epimerase (D-TE) family
physiological function
the purified D-tagatose 3-epimerase from Rhodobacter sphaeroides catalyzes the epimerization of D-fructose to D-psicose at the C3 position
additional information
additional information
the O1 of substrate D-fructose forms hydrogen bonds with His192 and Glu162 to help the correct metal coordination of the substrate. The O2 forms hydrogen bonds with His192 and Arg221. Glu156 forms hydrogen bonds with O3, and Glu250 directs its OE2 atom to a hydrogen atom attached to C3. Because D-fructose has the same configurations of C1, C2 and C3 as D-tagatose, the interactions between D-fructose at the 1-, 2- and 3-positions and the enzyme are very similar to those in other DTE/DPE family enzymes. Residue R118 forms a hydrogen bond with O4 of D-fructose and may regulate the substrate specificity. The strengthened hydrophobic interaction may attribute to the recognition of D-tagatose, D-psicose, and D-sorbose. Enzyme homology modeling and structure comparisons, overview
additional information
-
the O1 of substrate D-fructose forms hydrogen bonds with His192 and Glu162 to help the correct metal coordination of the substrate. The O2 forms hydrogen bonds with His192 and Arg221. Glu156 forms hydrogen bonds with O3, and Glu250 directs its OE2 atom to a hydrogen atom attached to C3. Because D-fructose has the same configurations of C1, C2 and C3 as D-tagatose, the interactions between D-fructose at the 1-, 2- and 3-positions and the enzyme are very similar to those in other DTE/DPE family enzymes. Residue R118 forms a hydrogen bond with O4 of D-fructose and may regulate the substrate specificity. The strengthened hydrophobic interaction may attribute to the recognition of D-tagatose, D-psicose, and D-sorbose. Enzyme homology modeling and structure comparisons, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R118W
site-directed mutagenesis, the unique hydrogen bond between Arg118 and O4 of D-fructose is broken when Arg118 is mutated to Trp, the mutation improves the substrate recognition and activity of the enzyme. The mutant enzyme RsDTE_R118W shows decreased catalytic activity compared to the wild-type enzyme toward D-fructose, the kcat/Km for D-tagatose is about twofold higher than for D-psicose. Mutant R118W shows 1.5fold higher catalytic efficiency toward D-tagatose than the wild-type
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene RSP_3671, sequence comparisons and phylogenetic tree, recombinant expression in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, L.; Mu, W.; Jiang, B.; Zhang, T.
Characterization of D-tagatose-3-epimerase from Rhodobacter sphaeroides that converts D-fructose into D-psicose
Biotechnol. Lett.
31
857-862
2009
Cereibacter sphaeroides (C1KKR1)
Qi, Z.; Zhu, Z.; Wang, J.W.; Li, S.; Guo, Q.; Xu, P.; Lu, F.; Qin, H.M.
Biochemical analysis and the preliminary crystallographic characterization of D-tagatose 3-epimerase from Rhodobacter sphaeroides
Microb. Cell Fact.
16
193
2017
Cereibacter sphaeroides (Q3IW04), Cereibacter sphaeroides, Cereibacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 (Q3IW04)
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