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Information on EC 2.2.1.2 - transaldolase and Organism(s) Escherichia coli and UniProt Accession P0A870
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2.2.1.2 transaldolaseSpecify your search results
Word Map
- 2.2.1.2
- pentose
- transketolase
- glucose-6-phosphate
- 5-phosphate
-
non-oxidative
-
methylotrophic
- hexose
- 6-phosphogluconate
- fructose-6-phosphate
- hansenula
- xylulose
-
egypt
- boidinii
- triose
- polymorpha
- xylitol
- xylulokinase
-
hepatosplenomegaly
- phosphoketolase
- erythrose
-
isotopomer
-
methanol-induced
- ribitol
- erythritol
- stipitis
- molecular biology
- medicine
- industry
- synthesis
-
3-epimerase
- ribulose-5-phosphate
-
co-circulation
-
hpaiv
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
transaldolase, taldo1, dihydroxyacetone synthase, taldo, transaldolase 1, transaldolase b, fotal, transaldolase a, talase, peroxisomal transaldolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dihydroxyacetone synthase
-
-
-
-
dihydroxyacetonetransferase
-
-
-
-
formaldehyde transketolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aldehyde group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase
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CAS REGISTRY NUMBER
COMMENTARY
9014-46-4
-
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-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
dihydroxyacetone + D-glyceraldehyde 3-phosphate
D-fructose 6-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
2,5-D-threo-diketohexose phosphate + D-glyceraldehyde 3-phosphate
?
-
-
-
-
?
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 6-phosphate + erythrose 4-phosphate
sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate
-
-
-
-
?
dihydroxypropanone + glyceraldehyde 3-phosphate
D-fructose 6-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
-
not: glycoaldehyde, glycoaldehyde phosphate
-
-
r
additional information
?
-
-
enzyme participates in the interconversion of metabolically significant triose, tetrose, pentose, hexose and heptose phosphates, enzyme is involved in the metabolism of carbohydrates via the nonoxidative part of the pentose phosphate pathway
-
-
?
additional information
?
-
-
key enzyme in the nonoxidative pentose phosphate pathway, overview
-
-
?
additional information
?
-
-
enzyme catalyzes a stereospecifc carboligation resulting in D-threo configuration of the product. Donor substrates require a 1-hydroxy-2-alkanone moiety. No substrates: propanone, butanone
-
-
?
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
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
-
-
-
r
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
-
-
-
-
r
additional information
?
-
-
enzyme participates in the interconversion of metabolically significant triose, tetrose, pentose, hexose and heptose phosphates, enzyme is involved in the metabolism of carbohydrates via the nonoxidative part of the pentose phosphate pathway
-
-
?
additional information
?
-
-
key enzyme in the nonoxidative pentose phosphate pathway, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-fructose 1,6-bisphosphate
-
competitive inhibition against D-fructose 6-phosphate and uncompetitively against D-erythrose 4-phosphate
additional information
the wild type enzyme is not inhibited by D-tagatose 6-phosphate
-
additional information
-
the wild type enzyme is not inhibited by D-tagatose 6-phosphate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
30
dihydroxyacetone
mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate
1.5
D-fructose 6-phosphate
mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate
22
D-fructose 6-phosphate
mutant F189Y, reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.3
dihydroxyacetone
mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate
0.22
D-fructose 6-phosphate
mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate
8.8
D-fructose 6-phosphate
mutant F189Y, reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.85
D-fructose 1,6-bisphosphate
-
transaldolase B, competitive inhibition with respect to D-fructose 6-phosphate, at pH 7.2 and 37°C
3.2
D-fructose 1,6-bisphosphate
-
transaldolase A, competitive inhibition with respect to D-fructose 6-phosphate, at pH 7.2 and 37°C
6.5
D-fructose 1,6-bisphosphate
-
transaldolase A, uncompetitive inhibition with respect to D-erythrose 4-phosphate, at pH 7.2 and 37°C
9.4
D-fructose 1,6-bisphosphate
-
transaldolase B, competitive inhibition with respect to D-erythrose 4-phosphate, at pH 7.2 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme F178Y with bound D-tagatose 6-phosphate , hanging drop vapor diffusion method, using 0.15 M Li2SO4, 18% (w/v) PEG 3350. Mutant enzyme E96Q with bound D-fructose 6-phosphate, hanging drop vapor diffusion method, using 0.2 M DL-malic acid pH 7.0, 18% (w/v) PEG3350
structure of the unliganded F178Y mutant is determined to 1.4 A resolution
crystallization with a combination of micro- and macro-seeding techniques, space group: P212121
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E96Q
the mutant enzyme with reduced transaldolase activity is irreversibly inhibited by D-tagatose 6-phosphate
E96Q/F178Y
the mutant enzyme is irreversibly inhibited by D-tagatose 6-phosphate
F178Y
F178E
-
mutant is able to catalyze aldol reactions and readily accepts hihydroxypropanone and hydroxypropanone
F178E/S176A
-
improved acceptance of substrate hydroxypropanone compared with mutant F178E
F178Y/R181E
-
mutation based on mutant F178Y, which is able to use dihydroxyacetone as donor in aldol reactions. Mutant F178Y/R181E exhibits an at least fivefold increase in affinity towards glyceraldehyde and can use D- and L-glyceraldehyde as acceptor substrates, resulting in preparative synthesis of D-fructose, D-xylulose and L-sorbose when dihydroxyacetone is used as donor. Mutant enzyme does not show transaldolase activity
R300A
-
little lower activity than the wild type, but same stability against urea and thermal inactivation
R300E
-
little lower activity than the wild type, but same stability against urea and thermal inactivation
F178Y
by screening of library of proteins bearing a mutation in the active site mutant protein F178Y is found to be able to synthesize fructose 6-phosphate from dihydroxyacetone and glyceraldehyde 3-phosphate. Mutant is not only able to transfer a dihydroxyacetone moiety from a ketose donor, fructose 6-phosphate, onto an aldehyde acceptor, erythrose 4-phosphate, but to use it as a substrate directly in an aldolase reaction. Mutant fructose 6-phosphate aldolase activity is increased considerably above 70fold compared to wild-type. Structural studies of the wild-type and mutant protein suggest that this is due to a different H-bond pattern in the active site leading to a destabilization of the Schiff base intermediate
F178Y
reaction fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate: Km (mM): 30 (dihydroxyacetone), kcat (1/sec): 4.3 (dihydroxyacetone). Reaction fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate: Km (mM) 1.5 (fructose 6-phosphate), kcat (1/sec): 0.22 (fructose 6-phosphate). Reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate: Km (mM): 22 (fructose 6-phosphate), kcat (1/sec): 8.8
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant and wild-type protein are expressed in Escherichia coli as a His-tagged fusion protein
amplification and expression in Escherichia coli strain HB523 harboring the phbCAB operon to shift the metabolic flux to production of poly-beta-hydroxybutyrate
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
overexpression of enzyme in Escherichia coli harboring poly-beta-hydroxybutyrate operon phbCAB leads to increase in poly-beta-hydroxybutyrate from 28.2% to 52.3%
synthesis
-
mutation F178Y/R181E is based on mutant F178Y, which is able to use dihydroxyacetone as donor in aldol reactions. Mutant F178Y/R181E exhibits an at least fivefold increase in affinity towards glyceraldehyde and can use D- and L-glyceraldehyde as acceptor substrates, resulting in preparative synthesis of D-fructose, D-xylulose and L-sorbose when dihydroxyacetone is used as donor. Mutant enzyme does not show transaldolase activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsolas, O.; Horecker, B.L.
Transaldolase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
259-280
1972
Bos taurus, Saccharomyces cerevisiae, Cyberlindnera jadinii, Chlorella sp., Prosthecochloris vibrioformis f. thiosulfatophilum, Chromatium sp., Oryctolagus cuniculus, Escherichia coli, Euglena sp., Homo sapiens, Musca domestica, Rattus norvegicus, Saccharomyces pastorianus, Spinacia oleracea, Tetranychus telarius
-
Horecker, B.L.; Smyrniotis, P.Z.
Purification and properties of yeast transaldolase
J. Biol. Chem.
212
811-825
1955
Escherichia coli, Rattus norvegicus, Saccharomyces pastorianus, Spinacia oleracea
Sprenger, G.A.; Schoerken, U.; Sprenger, G.; Sahm, H.
Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains
J. Bacteriol.
177
5930-5936
1995
Escherichia coli
Jia, J.; Schorken, U.; Lindqvist, Y.; Sprenger, G.A.; Schneider, G.
Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases
Protein Sci.
6
119-124
1997
Escherichia coli
Schorken, U.; Jia, J.; Sahm, H.; Sprenger, G.A.; Schneider, G.
Disruption of Escherichia coli transaldolase into catalytically active monomers: evidence against half-of-the-sites mechanism
FEBS Lett.
441
247-250
1998
Escherichia coli
Schorken, U.; Thorell, S.; Schurmann, M.; Jia, J.; Sprenger, G.A.; Schneider, G.
Identification of catalytically important residues in the active site of Escherichia coli transaldolase
Eur. J. Biochem.
268
2408-2415
2001
Escherichia coli
Song, B.G.; Kim, T.K.; Jung, Y.M.; Lee, Y.H.
Modulation of talA gene in pentose phosphate pathway for overproduction of poly-beta-hydroxybutyrate in transformant Escherichia coli harboring phbCAB operon
J. Biosci. Bioeng.
102
237-240
2006
Escherichia coli
Schneider, S.; Sandalova, T.; Schneider, G.; Sprenger, G.A.; Samland, A.K.
Replacement of a phenylalanine by a tyrosine in the active site confers fructose 6-phosphate aldolase activity to the transaldolase of Escherichia coli and human origin
J. Biol. Chem.
283
30064-30072
2008
Homo sapiens, Escherichia coli (P0A870), Escherichia coli
Schneider, S.; Gutierrez, M.; Sandalova, T.; Schneider, G.; Clapes, P.; Sprenger, G.A.; Samland, A.K.
Redesigning the active site of transaldolase TalB from Escherichia coli: new variants with improved affinity towards nonphosphorylated substrates
ChemBioChem
11
681-690
2010
Escherichia coli
Rale, M.; Schneider, S.; Sprenger, G.A.; Samland, A.K.; Fessner, W.D.
Broadening deoxysugar glycodiversity: natural and engineered transaldolases unlock a complementary substrate space
Chemistry
17
2623-2632
2011
Escherichia coli
Stellmacher, L.; Sandalova, T.; Schneider, S.; Schneider, G.; Sprenger, G.A.; Samland, A.K.
Novel mode of inhibition by D-tagatose 6-phosphate through a Heyns rearrangement in the active site of transaldolase B variants
Acta Crystallogr. Sect. D
72
467-476
2016
Escherichia coli (P0A870), Escherichia coli
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