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Information on EC 2.2.1.2 - transaldolase and Organism(s) Homo sapiens

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EC Tree
     2 Transferases
         2.2 Transferring aldehyde or ketonic groups
             2.2.1 Transketolases and transaldolases
                2.2.1.2 transaldolase
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
transaldolase, taldo1, dihydroxyacetone synthase, taldo, transaldolase 1, transaldolase b, fotal, transaldolase a, talase, peroxisomal transaldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydroxyacetone synthase
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-
-
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dihydroxyacetonetransferase
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-
-
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formaldehyde transketolase
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-
-
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hTAL
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TALase
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-
TALDO
-
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transaldolase 1
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transaldolase1
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldehyde group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9014-46-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,5-D-threo-diketohexose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose 4-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
dihydroxyacetone + D-glyceraldehyde 3-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
hydroxypyruvic aldehyde + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
L-glyceraldehyde 3-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
L-sorbose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
octulose 8-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
sedoheptulose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
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phosphate
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sulfate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.76 - 27
D-fructose 6-phosphate
340
dihydroxyacetone
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mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 7.4
D-fructose 6-phosphate
8.9
dihydroxyacetone
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mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
quantification of transaldolase exchange activity from analysis of [U-2H7]glucuronide enrichment from [U-2H7]glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
wall
Manually annotated by BRENDA team
-
human EBV-transformed human B-cells
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TALDO_HUMAN
337
0
37540
Swiss-Prot
other Location (Reliability: 5)
A0A140VK56_HUMAN
337
0
37540
TrEMBL
other Location (Reliability: 5)
F2Z393_HUMAN
318
0
35329
TrEMBL
other Location (Reliability: 5)
B4DID5_HUMAN
154
0
17074
TrEMBL
other Location (Reliability: 5)
E9PKI8_HUMAN
93
0
10249
TrEMBL
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
SDS-PAGE
77000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
-
enzyme forms a complex with glucose-6-phosphate dehydrogenase
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, mother liquid consits of: 27% w/v polyethylenglycol 4000, 0.08% NaN3, 0.3 M ammonium acetate, pH 4.4
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F189Y
TALDELTAS171
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TAL-deficient lymphoblasts (caused by deletion of Ser 171) reveal co-ordinated changes in expression of genes involved in the pentose phosphate pathway, mitochondrial biogenesis, oxidative stress, and Ca2+ fluxing. Sedoheptulose 7-phosphate and ADP-ribose are accumulated, glucose 6-phosphate, NADPH and NAD+ are depleted. TAL-deficient cells have diminished mitochondrial transmembrane potential and increased mitochondrial mass associated with increased production of nitric oxide and ATP. TAL deficiency results in enhanced spontaneous and H2O2-induced apoptosis. Normalization of TAL activity by adeno-associated-virus-mediated gene transfer reverses the TAL-deficient phenotype
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as a fusion protein with glutathione S-transferase
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expression in Escherichia coli
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mutant and wild-type protein are expressed in Escherichia coli as a GST-fusion protein
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
molecular biology
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TAL deficiency is shown as a modulator of mitochondrial homoeostasis, Ca2+ fluxing and apoptosis
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
-
Manually annotated by BRENDA team
Banki, K.; Perl, A.
Inhibition of the catalytic activity of human transaldolase by antibodies and site-directed mutagenesis
FEBS Lett.
378
161-165
1996
Homo sapiens
Manually annotated by BRENDA team
Thorell, S.; Gergely, P.Jr.; Banki, K.; Perl, A.; Schneider, G.
The three-dimensional structure of human transaldolase
FEBS Lett.
475
205-208
2000
Homo sapiens
Manually annotated by BRENDA team
Huang, J.B.; Espinoza, J.; Romero, R.; Petty, H.R.
Transaldolase is part of a supramolecular complex containing glucose-6-phosphate dehydrogenase in human neutrophils that undergoes retrograde trafficking during pregnancy
Metab. Clin. Exp.
54
1027-1033
2005
Homo sapiens
Manually annotated by BRENDA team
Qian, Y.; Banerjee, S.; Grossman, C.E.; Amidon, W.; Nagy, G.; Barcza, M.; Niland, B.; Karp, D.R.; Middleton, F.A.; Banki, K.; Perl, A.
Transaldolase deficiency influences the pentose phosphate pathway, mitochondrial homoeostasis and apoptosis signal processing
Biochem. J.
415
123-134
2008
Homo sapiens
Manually annotated by BRENDA team
Basta, P.V.; Bensen, J.T.; Tse, C.K.; Perou, C.M.; Sullivan, P.F.; Olshan, A.F.
Genetic variation in Transaldolase 1 and risk of squamous cell carcinoma of the head and neck
Cancer Detect. Prev.
32
200-208
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Wamelink, M.M.; Smith, D.E.; Jansen, E.E.; Verhoeven, N.M.; Struys, E.A.; Jakobs, C.
Detection of transaldolase deficiency by quantification of novel seven-carbon chain carbohydrate biomarkers in urine
J. Inherit. Metab. Dis.
30
735-742
2007
Homo sapiens
Manually annotated by BRENDA team
Jones, J.G.; Garcia, P.; Barosa, C.; Delgado, T.C.; Caldeira, M.M.; Diogo, L.
Quantification of hepatic transaldolase exchange activity and its effects on tracer measurements of indirect pathway flux in humans
Magn. Reson. Med.
59
423-429
2008
Homo sapiens
Manually annotated by BRENDA team
Wamelink, M.M.; Struys, E.A.; Salomons, G.S.; Fowler, D.; Jakobs, C.; Clayton, P.T.
Transaldolase deficiency in a two-year-old boy with cirrhosis
Mol. Genet. Metab.
94
255-258
2008
Homo sapiens
Manually annotated by BRENDA team
Basu, R.; Chandramouli, V.; Schumann, W.; Basu, A.; Landau, B.R.; Rizza, R.A.
Additional evidence that transaldolase exchange, isotope discrimination during the triose-isomerase reaction, or both occur in humans: effects of type 2 diabetes
Diabetes
58
1539-1543
2009
Homo sapiens
Manually annotated by BRENDA team
Delgado, T.C.; Silva, C.; Fernandes, I.; Caldeira, M.; Bastos, M.; Baptista, C.; Carvalheiro, M.; Geraldes, C.F.; Jones, J.G.
Sources of hepatic glycogen synthesis during an oral glucose tolerance test: Effect of transaldolase exchange on flux estimates
Magn. Reson. Med.
62
1120-1128
2009
Homo sapiens
Manually annotated by BRENDA team