Information on EC 2.2.1.2 - transaldolase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
2.2.1.2
-
RECOMMENDED NAME
GeneOntology No.
transaldolase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
mechanism
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
mechanism
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
mechanism
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
ping-pong kinetics with sedoheptulose 7-phosphate adding first
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldehyde group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Bifidobacterium shunt
-
Biosynthesis of secondary metabolites
-
formaldehyde assimilation II (RuMP Cycle)
-
formaldehyde assimilation III (dihydroxyacetone cycle)
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Pentose phosphate pathway
-
pentose phosphate pathway (non-oxidative branch)
-
Rubisco shunt
-
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Atalp
Blastobotrys adeninivorans LS3
Q0E4W0
-
-
dihydroxyacetone synthase
-
-
-
-
dihydroxyacetonetransferase
-
-
-
-
formaldehyde transketolase
-
-
-
-
hTAL
-
-
NQM1/YGR043C
P53228
-
TAL
Q2TUQ1
-
Tal1
P15019
gene name
TALase
-
-
TALDO
-
-
transaldolase
-
-
transaldolase
-
-
transaldolase
-
-
transaldolase
P53228
-
transaldolase
Trichosporonoides megachiliensis
-
-
transaldolase 1
-
-
transaldolase STY3758
-
-
transaldolase1
-
-
CAS REGISTRY NUMBER
COMMENTARY
9014-46-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; decrease in enzyme expression under phosphate starvation
-
-
Manually annotated by BRENDA team
P1, 2 isoenzymes: C1-inducible enzyme, C2-constitutive enzyme
-
-
Manually annotated by BRENDA team
Bifidobacterium bifidum A8
-
-
-
Manually annotated by BRENDA team
; increased expression in media containing 5% NaCl
-
-
Manually annotated by BRENDA team
strain LS3, gene ATAL
SwissProt
Manually annotated by BRENDA team
Blastobotrys adeninivorans LS3
strain LS3, gene ATAL
SwissProt
Manually annotated by BRENDA team
Chromatium sp.
-
-
-
Manually annotated by BRENDA team
var. neoformans, strain JEC21
-
-
Manually annotated by BRENDA team
3 isoenzymes: I, II, III
-
-
Manually annotated by BRENDA team
gene talA; recombinant enzyme
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
Euglena sp.
-
-
-
Manually annotated by BRENDA team
transaldolase/glucose-6-phosphate isomerase bifunctional enzyme
Swissprot
Manually annotated by BRENDA team
; pregnant and nonpregnant women
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
male, homo- or heterozygously lacking transaldolase
-
-
Manually annotated by BRENDA team
2 isoforms
-
-
Manually annotated by BRENDA team
Tetranychus telarius
-
-
-
Manually annotated by BRENDA team
Trichosporonoides megachiliensis
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
Trichosporonoides megachiliensis SN-G42
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
P53228
dysfunction could lead to liver cirrhosis and neonatal multi-organ diseases
physiological function
Trichosporonoides megachiliensis
-
part of pentose phosphate pathway
physiological function
P53228
key enzyme in pentose phosphate pathway
physiological function
-
transaldolase is a rate-limiting enzyme in the pentose phosphate pathway
physiological function
-
transaldolase shows a high mucin binding capacity. When exposed on the cell surface of Bifidobacterium bifidum, enzyme may act as an important colonization factor favoring its establishment in the gut. A recombinant Lactococcus lactis strain, engineered to secrete transaldolase, displays a mucin-binding level more than three times higher than the strain not producing the transaldolase
physiological function
P15019
gene disruption mutant displays a significant decrease in both growth on xylose and xylose-fermenting ability
physiological function
Bifidobacterium bifidum A8
-
transaldolase shows a high mucin binding capacity. When exposed on the cell surface of Bifidobacterium bifidum, enzyme may act as an important colonization factor favoring its establishment in the gut. A recombinant Lactococcus lactis strain, engineered to secrete transaldolase, displays a mucin-binding level more than three times higher than the strain not producing the transaldolase
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,5-D-threo-diketohexose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
2,5-D-threo-diketohexose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
2,5-D-threo-diketohexose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
2,5-D-threo-diketohexose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
2,5-D-threo-diketohexose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
D-erythrose + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-, Q0E4W0
-
-
-
?
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q9WYD1, -
-
-
-
?
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-, Q0E4W0
the preferred substrates for the enzyme include D-erythrose-4-phosphate and D-fructose-6-phosphate, whereas D-glyceraldehyde is not converted
-
-
?
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Blastobotrys adeninivorans LS3
Q0E4W0
-, the preferred substrates for the enzyme include D-erythrose-4-phosphate and D-fructose-6-phosphate, whereas D-glyceraldehyde is not converted
-
-
?
D-erythrose 4-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose 4-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose 4-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-erythrose 4-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + D-erythrose 4-phosphate
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + D-erythrose 4-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-, Q0E4W0
preferred substrates
-
-
?
D-fructose 6-phosphate + D-erythrose 4-phosphate
glyceraldehyde 3-phosphate + ?
show the reaction diagram
-
assay at 25C, pH 7.5
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
D-fructose 6-phosphate + D-ribose 5-phosphate
?
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + erythrose 4-phosphate
sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
D-fructose 6-phosphate + erythrose 4-phosphate
sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
D-fructose 6-phosphate + erythrose 4-phosphate
sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
D-fructose 6-phosphate + erythrose 4-phosphate
sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
D-fructose 6-phosphate + erythrose 4-phosphate
sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate
show the reaction diagram
P53228
assay at pH 7.6
-
-
?
D-fructose-6-phosphate + D-erythrose-4-phosphate
?
show the reaction diagram
Q76EM7
-
-
-
?
D-fructose-6-phosphate + D-erythrose-4-phosphate
?
show the reaction diagram
-
isoform ToTal1, highly specific for this pair of substrates
-
-
?
D-glyceraldehyde + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde + sedoheptulose 7-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
-
-
-
-
?
D-ribose 5-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
Chromatium sp., Euglena sp., Chlorella sp., Musca domestica, Chlorobium vibrioforme f. thiosulfatophilum, Tetranychus telarius
-
-
-
-
?
dihydroxyacetone + D-glyceraldehyde 3-phosphate
D-fructose 6-phosphate
show the reaction diagram
P0A870
-
-
-
?
dihydroxyacetone + D-glyceraldehyde 3-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
dihydroxypropanone + D-glyceraldehyde
D-fructose
show the reaction diagram
-
-
-
-
?
dihydroxypropanone + DL-glyceraldehyde
D-fructose
show the reaction diagram
-
-
-
-
?
dihydroxypropanone + glyceraldehyde 3-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
hydroxypyruvic aldehyde + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
hydroxypyruvic aldehyde + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
hydroxypyruvic aldehyde + sedoheptulose 7-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-glyceraldehyde 3-phosphate + sedoheptulose 7-phosphate
?
show the reaction diagram
-
-
-
-
?
L-glyceraldehyde 3-phosphate + 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
-
-
-
-
?
L-sorbose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
L-sorbose 6-phosphate + D-glyceraldehyde 3-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
-
-
-
-
?
octulose 8-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
Chromatium sp., Euglena sp., Chlorella sp., Musca domestica, Chlorobium vibrioforme f. thiosulfatophilum, Tetranychus telarius
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-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 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
P0A870
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-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 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-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 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
Chromatium sp., Euglena sp.
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-, Q0E4W0
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
not: glycoaldehyde, glycoaldehyde phosphate
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
not: glycoaldehyde, glycoaldehyde phosphate
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
not: glycoaldehyde, glycoaldehyde phosphate
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
maximal forward rate is about one third of the maximal reverse rate
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
Escherichia coli K12
-
-
-
-
r
sedoheptulose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
sedoheptulose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
sedoheptulose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
sedoheptulose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
-
-
-
?
sedoheptulose phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
L-sorbose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
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
?
-
-
alterations in the proteome response of Acidithiobacillus ferrooxidans to phosphate starvation, peptide mass fingerprinting, overview
-
-
-
additional information
?
-
-, Q2TUQ1
essential role of transaldolase in sperm-cell mitochondrial function
-
-
-
additional information
?
-
-
key enzyme in the nonoxidative pentose phosphate pathway, overview
-
-
-
additional information
?
-
-, Q2TUQ1
the enzyme is essential for maintenance of the mitochondrial transmembrane potential and fertility of spermatozoa, overview
-
-
-
additional information
?
-
-
the enzyme is part of a supramolecular complex containing glucose-6-phosphate dehydrogenase, responsible for substrate channeling, in female neutrophils that undergoes retrograde trafficking during pregnancy, trafficking occurs in nonpregnant women, the key regulatory enzyme in the nonoxidative branch of the hexose monophosphate shunt, is not in close physical proximity with lactate dehydrogenase, TALases retrograde motion contributes to uncoupling the shunt from its source of glucose-6-phosphate at the plasma membrane, thereby blunting NADPH2 production and downstream oxidant production by neutrophils, overview
-
-
-
additional information
?
-
-
the enzyme is upregulated as part in the posttranslational, translational, and transcriptional regulation system of the organism in response to nitrosative stress, microarrays, overview
-
-
-
additional information
?
-
-, Q0E4W0
no substrate: D-glyceraldehyde
-
-
-
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 SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-, Q0E4W0
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-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 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-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 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
Chromatium sp., Euglena sp., Chlorella sp., Musca domestica, Chlorobium vibrioforme f. thiosulfatophilum, Tetranychus telarius
-
-
-
-
r
D-erythrose 4-phosphate + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Blastobotrys adeninivorans LS3
Q0E4W0
-
-
-
?
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
?
-
-
alterations in the proteome response of Acidithiobacillus ferrooxidans to phosphate starvation, peptide mass fingerprinting, overview
-
-
-
additional information
?
-
-, Q2TUQ1
essential role of transaldolase in sperm-cell mitochondrial function
-
-
-
additional information
?
-
-
key enzyme in the nonoxidative pentose phosphate pathway, overview
-
-
-
additional information
?
-
-, Q2TUQ1
the enzyme is essential for maintenance of the mitochondrial transmembrane potential and fertility of spermatozoa, overview
-
-
-
additional information
?
-
-
the enzyme is part of a supramolecular complex containing glucose-6-phosphate dehydrogenase, responsible for substrate channeling, in female neutrophils that undergoes retrograde trafficking during pregnancy, trafficking occurs in nonpregnant women, the key regulatory enzyme in the nonoxidative branch of the hexose monophosphate shunt, is not in close physical proximity with lactate dehydrogenase, TALases retrograde motion contributes to uncoupling the shunt from its source of glucose-6-phosphate at the plasma membrane, thereby blunting NADPH2 production and downstream oxidant production by neutrophils, overview
-
-
-
additional information
?
-
-
the enzyme is upregulated as part in the posttranslational, translational, and transcriptional regulation system of the organism in response to nitrosative stress, microarrays, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
additional information
-
no cofactor requirement
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
no metal requirement
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
arabinose-5-phosphate
-
ToTal1, partial inhibition
D-arabinose-5-phosphate
-
-
D-erythrose 4-phosphate
-
-
D-Lactaldehyde
-
-
D-ribose-5-phosphate
-
above 15 mM
sedoheptulose 7-phosphate
-
-
Sodium borohydride
-
-
Tetranitromethane
-
isoenzyme III, only in presence of the substrates D-fructose 6-phosphate and sedoheptulose 7-phosphate
L-Glyceraldehyde
-
-
additional information
-
phosphate starvation leads to the downregulation of the enzyme expression
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NaCl
-, Q0E4W0
increased expression in media containing 5% NaCl
additional information
-
both isoforms: not activating: dithiothreitol, reduced form of glutathione
-
additional information
-
nitric oxide induces the enzyme expression
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.007
-
D-erythrose 4-phosphate
-
-
0.013
-
D-erythrose 4-phosphate
-, Q0E4W0
pH 6.0, 20C; pH 6.0, 20C
0.0156
-
D-erythrose 4-phosphate
-
pH 7.5, 25C
0.018
-
D-erythrose 4-phosphate
-
-
0.02
-
D-erythrose 4-phosphate
-
-
0.0278
-
D-erythrose 4-phosphate
-
pH 7.5, 50C
0.078
-
D-erythrose 4-phosphate
-
T156A
0.09
-
D-erythrose 4-phosphate
-
-
0.1
-
D-erythrose 4-phosphate
-
-
0.1
-
D-erythrose 4-phosphate
-
wild-type, N35A
0.11
-
D-erythrose 4-phosphate
-
D17N
0.111
-
D-erythrose 4-phosphate
-
S176A
0.117
-
D-erythrose 4-phosphate
-
E96Q
0.122
-
D-erythrose 4-phosphate
-
E96A
0.265
-
D-erythrose 4-phosphate
-
R300A
0.27
-
D-erythrose 4-phosphate
Q9WYD1, -
pH 9.0, 80C
0.295
-
D-erythrose 4-phosphate
-
wild-type
0.35
-
D-erythrose 4-phosphate
-
R300E
0.555
-
D-erythrose 4-phosphate
-
D17A
0.013
-
D-erythrose-4-phosphate
-, Q0E4W0
-
0.49
-
D-erythrose-4-phosphate
-
-
0.056
-
D-fructose 6-phosphate
-, Q0E4W0
; pH 6.0, 20C; pH 6.0, 20C
0.2
-
D-fructose 6-phosphate
-
-
0.32
-
D-fructose 6-phosphate
-
-
0.36
-
D-fructose 6-phosphate
Q9WYD1, -
pH 9.0, 80C
0.6
-
D-fructose 6-phosphate
-
E96A
0.64
-
D-fructose 6-phosphate
-
pH 7.5, 25C
0.65
-
D-fructose 6-phosphate
-
pH 7.5, 50C
0.7
-
D-fructose 6-phosphate
-
D17A
0.76
-
D-fructose 6-phosphate
-
mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate
0.8
-
D-fructose 6-phosphate
-
-
0.94
-
D-fructose 6-phosphate
-
wild-type
0.96
-
D-fructose 6-phosphate
-
D17N
1.02
-
D-fructose 6-phosphate
-
T156A
1.1
-
D-fructose 6-phosphate
-
N35A
1.14
-
D-fructose 6-phosphate
-
E96Q
1.2
-
D-fructose 6-phosphate
-
-
1.2
-
D-fructose 6-phosphate
-
R300E
1.2
-
D-fructose 6-phosphate
-
wild-type
1.35
-
D-fructose 6-phosphate
-
R300A
1.5
-
D-fructose 6-phosphate
P0A870
mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate
1.6
-
D-fructose 6-phosphate
-
-
4.9
-
D-fructose 6-phosphate
-
S176A
22
-
D-fructose 6-phosphate
P0A870
mutant F189Y, reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate
27
-
D-fructose 6-phosphate
-
mutant F189Y, reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate
6.66
-
D-fructose-6-phosphate
-
-
59
-
D-glyceraldehyde
-
mutant F178, pH 8.5, 30C
2.2
-
D-ribose 5-phosphate
-
pH 7.5, 50C, concentration of ribose-5-phosphate between 0.5 and 15 mM
30
-
Dihydroxyacetone
P0A870
mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate
340
-
Dihydroxyacetone
-
mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate
120
-
DL-glyceraldehyde
-
mutant F178, pH 8.5, 30C
0.132
-
erythrose 4-phosphate
-
isoform ToTal1, 25C, pH 8.5
0.343
-
fructose-6-phosphate
-
isoform ToTal1, 25C, pH 8.5
0.038
-
glyceraldehyde 3-phosphate
-
-
0.072
-
glyceraldehyde 3-phosphate
-
-
0.22
-
glyceraldehyde 3-phosphate
-
-
1.9
-
glyceraldehyde 3-phosphate
-
wild-type, pH 8.5, 30C
0.18
-
sedoheptulose 7-phosphate
-
-
0.285
-
sedoheptulose 7-phosphate
-
-
0.46
-
sedoheptulose 7-phosphate
-
-
2.4
-
glyceraldehyde 3-phosphate
-
mutant F178, pH 8.5, 30C
additional information
-
additional information
-
positive cooperativity in binding of substrates
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
22.9
-
D-erythrose 4-phosphate
Q9WYD1, -
pH 9.0, 80C
6.44
-
D-erythrose-4-phosphate
-, Q0E4W0
-
0.21
-
D-fructose 6-phosphate
-
mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate
0.22
-
D-fructose 6-phosphate
P0A870
mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate
4.9
-
D-fructose 6-phosphate
-, Q0E4W0
; pH 6.0, 20C
7.4
-
D-fructose 6-phosphate
-
mutant F189Y, reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate
8.8
-
D-fructose 6-phosphate
P0A870
mutant F189Y, reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate
22.3
-
D-fructose 6-phosphate
Q9WYD1, -
pH 9.0, 80C
0.53
-
D-glyceraldehyde
-
mutant F178, pH 8.5, 30C
4.3
-
Dihydroxyacetone
P0A870
mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate
8.9
-
Dihydroxyacetone
-
mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate
0.54
-
DL-glyceraldehyde
-
mutant F178, pH 8.5, 30C
12
-
glyceraldehyde 3-phosphate
-
mutant F178, pH 8.5, 30C
13
-
glyceraldehyde 3-phosphate
-
wild-type, pH 8.5, 30C
additional information
-
D-erythrose 4-phosphate
-, Q0E4W0
pH 6.0, 20C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
139.9
-
D-erythrose-4-phosphate
-
-
195567
10.38
-
D-fructose-6-phosphate
-
-
80918
9
-
D-glyceraldehyde
-
mutant F178, pH 8.5, 30C
9225
4.3
-
DL-glyceraldehyde
-
mutant F178, pH 8.5, 30C
10100
5000
-
glyceraldehyde 3-phosphate
-
mutant F178, pH 8.5, 30C
11067
6600
-
glyceraldehyde 3-phosphate
-
wild-type, pH 8.5, 30C
11067
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0049
-
arabinose-5-phosphate
-
isoform ToTal1, 25C, pH 8.5
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0035
-
-
glucose as sole carbon source, sampling after 24 h
0.0036
-
-
glucose as sole carbon source, sampling after 15 h; glucose as sole carbon source, sampling after 36 h
0.0306
-
-
glucose as sole carbon source, sampling after 24 h
0.0506
-
-
glucose as sole carbon source, sampling after 36 h
0.0611
-
-
glucose as sole carbon source, sampling after 15 h
0.125
-
-
xylose as sole carbon source, sampling after 36 h
0.18
-
-
xylose as sole carbon source, sampling after 60 h
0.185
-
-
xylose as sole carbon source, sampling after 84 h
0.3
-
-
crude enzyme
0.329
-
-
xylose as sole carbon source, sampling after 84 h
0.387
-
-
xylose as sole carbon source, sampling after 60 h
0.58
-
-
xylose as sole carbon source, sampling after 36 h
0.6
-
Trichosporonoides megachiliensis
-
-
3.84
-
-
-
8.9
-
Q9WYD1, -
30C, pH 9.0
10.1
-
Q76EM7
pH 7.0, 30C
15
-
-
-
15
-
-
enzyme after purification with anion exchange and gel filtration chromatography
42
-
Q9WYD1, -
80C, pH 9.0
additional information
-
-, Q0E4W0
-
additional information
-
-
quantification of transaldolase exchange activity from analysis of [U-2H7]glucuronide enrichment from [U-2H7]glucose
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-, Q0E4W0
native enzyme
5.5
-
-, Q0E4W0
; native enzyme
6
-
-, Q0E4W0
recombinant enzyme; recombinant enzyme
7.5
-
-
imidazole buffer
7.6
-
P53228
assay at
8
-
-
isoenzyme I, II, III
8.2
-
-
-
8.5
9.5
-
-
8.5
-
-
isoform ToTal1
8.5
-
P0A870
assay at
8.5
-
-
assay at
9
-
Q9WYD1, -
in glycine-NaOH buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
6
-, Q0E4W0
; native enzyme; native enzyme, 80% of maximal activity within this range
5.4
6.3
-, Q0E4W0
recombinant enzyme; recombinant enzyme, 80% of maximal activity within this range
6
9
Q9WYD1, -
-
6.3
9.5
-
about 50% of activity maximum at pH 6.3 and 9.5, isoenzyme I, II, III
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-, Q0E4W0
; native and recombinant enzyme
30
-
P0A870
assay at
30
-
-
assay at
80
-
Q9WYD1, -
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
18
25
-, Q0E4W0
; native and recombinant enzyme, 80% of maximal activity within this range
40
-
Q9WYD1, -
28% of maximum activity
60
-
Q9WYD1, -
73% of maximum activity
90
-
Q9WYD1, -
96% of maximum activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
isoelectric focusing-PAGE
5.14
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
human EBV-transformed human B-cells
Manually annotated by BRENDA team
-
in neutrophils from nonpregnant individuals, enzyme undergoes anterograde trafficking, whereas retrograde trafficking is found during pregnacy. Trafficking involves microtubules; the transaldolase is part of a supramolecular complex containing glucose-6-phosphate dehydrogenase in neutrophils that undergoes retrograde trafficking during pregnancy, enzyme trafficking, overview
Manually annotated by BRENDA team
additional information
-
isoform ToTal1, present in all tissues examined
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Bifidobacterium bifidum A8
-
-
-
Manually annotated by BRENDA team
-
isoform ToTal1 and ToTal2
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli O104:H4 (strain 2009EL-2071)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Prochlorococcus marinus (strain MIT 9312)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35000
-
-, Q0E4W0
denatured enzyme, SDS-PAGE
36000
-
-
SDS-PAGE, denatured
36200
-
-
computer analysis of a 2-D PAGE
38000
-
-
SDS-PAGE
38000
-
-
SDS-PAGE, purified
47500
-
-
gel filtration, C1-inducible enzyme
52000
-
-
gel filtration, constitutive enzyme
63600
65200
-
ultracentrifugation and gel filtration, isoenzyme III
65000
-
-
gel filtration
68100
-
-
ultracentrifugation and gel filtration, isoenzyme II
70000
-
-
gel filtration
75000
-
P0A870
gel filtration
76100
77400
-
ultracentrifugation and gel filtration, isoenzyme I, sedimentation equilibrium ultracentrifugation
77000
-
-
gel filtration
140000
-
-, Q0E4W0
gel filtration; gel filtration; native enzyme (tetramer), gel filtration
271000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q76EM7
x * 100000, SDS-PAGE
?
-
x * 42000, isoform ToTal1, x * 35000, isoform ToTal2, SDS-PAGE
?
-
x * 23609, MALDI-TOF MS; x * 23609, mass spectrometry
?
Q9WYD1, -
x * 24000, SDS-PAGE, x * 24213, calculated
decamer
-
10 * 24000, SDS-PAGE, 10 * 23960, calculated
dimer
-
alphabeta, 1 * 38000 + 1 * 35500, SDS-PAGE, isoenzyme II
dimer
-
alpha2, 2 * 38000, SDS-PAGE isoenzyme I; beta2, 2 * 35500, SDS-PAGE, isoenzyme III
dimer
-
alpha2, 2 * 35000, SDS-PAGE
dimer
-
the crystal forms a dimer
dimer
P0A870
gel filtration
dimer
-
gel filtration
dimer
Escherichia coli K12
-
alpha2, 2 * 35000, SDS-PAGE
-
monomer
-
1 * 50000, SDS-PAGE
tetramer
-, Q0E4W0
; 4 * 35000, SDS-PAGE; 4 * 35000, SDS-PAGE, 4 * 35095, calculated
tetramer
Blastobotrys adeninivorans LS3
-
4 * 35000, SDS-PAGE
-
additional information
Q76EM7
determinantion of N-terminal amino acid sequence
additional information
-
enzyme forms a complex with glucose-6-phosphate dehydrogenase
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
cleavage of 6 kDa plastid targeting sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; crystallization with a combination of micro- and macro-seeding techniques, space group: P212121
-
structure of the unliganded F178Y mutant is determined to 1.4 A resolution
P0A870
hanging drop method, mother liquid consits of: 27% w/v polyethylenglycol 4000, 0.08% NaN3, 0.3 M ammonium acetate, pH 4.4
-
hanging-drop vapor diffusion method
P53228
crystallization in polymorphic forms, to 3.0 and 2.7 A resolution. Crystal form 1 belong to the orthorhombic space group C2221 with five monomers per asymmetric unit and crystal form 2 belong to the monoclinic space group P21 with ten monomers per asymmetric unit
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
9
-
stable
6
9
-
80% loss of activity with Tris/HCl buffer at pH 7.5, 95% loss of activity with Tris/HCl buffer at pH 9.0, 62% loss of activity with glycine/NaOH buffer at pH 9.0, about half of enzyme activity lost with phosphate buffer at pH 6.0
7
-
-
room temperature, stable for a few hours
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
room temperature, at neutral pH stable for a few hours
25
-
-
3 weeks, no loss of activity
30
50
-
at 30C for 1 h only 80% residual activity, at 40C for 1 h only 60% residual activity, at 50C enzyme rapidly inactive, at 55C about 30% activity lost
50
-
-
heat-labile
50
-
-
2 min, C1-inducible enzyme loses 90% of activity, constitutive enzyme remains fully active
50
-
-
above 50C rapid loss in activity
55
-
-
total inactivation of enzyme
60
-
Q9WYD1, -
half life 198 h
80
-
-
4 h, no loss of activity, 24 h, 50% residual activity
80
-
Q9WYD1, -
half-life 13 h
90
-
-
15 min, 20% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
complete inactivation by treatment with sodium borohydride at pH 6.0 and 2C in absence of substrate D-fructose 6-phosphate
-
highly purified preparations can be dialyzed with little loss of activity
-
stable to lyophilization
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for at least 2 months
-
2C, for at least 8 weeks
-
isoenzymes I and III are stable in the cold in the crystalline form for over 1 year
-
30C, 1 h, 20% activity lost
-
40C, 1 h, 40% activity lost
-
-16C, 10-20% loss of activity after 1 week
-
-20C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
II; III; isoenzymes: I
-
using Ni-NTA chromatography
P0A870
anion exchange and gel filtration chromatographies, after last step 50fold purification
-
affinity chromatography
-
recombinant enzyme
-
Ni2+ affinity column
P53228
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; expressed in Escherichia coli; gene ATAL, DNA and amino acid sequence determination and analysis, including promoter and terminator sequences, single copy gene, genetic organization, expression in Escherichia coli
-, Q0E4W0
amplification and expression in Escherichia coli strain HB523 harboring the phbCAB operon to shift the metabolic flux to production of poly-beta-hydroxybutyrate
-
mutant and wild-type protein are expressed in Escherichia coli as a His-tagged fusion protein
P0A870
overexpression in Escherichia coli
-
overexpression in Clostridium acetobutylicum ATCC 824
-
expression in Escherichia coli
Q76EM7
expression as a fusion protein with glutathione S-transferase
-
expression in Escherichia coli
-
mutant and wild-type protein are expressed in Escherichia coli as a GST-fusion protein
-
overexpression in Escherichia coli
-
partial DNA and amino acid sequence determination and analysis
-, Q2TUQ1
expression in Escherichia coli BL21
P53228
isoform ToTal1 and ToTal2, expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
Q9WYD1, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of is up-regulated in the presence of xylose
P15019
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D17A
-
lower specific activity than wild-type
E96A
-
lower specific activity than wild-type
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
P0A870
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; 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
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
N35A
-
lower specific activity than wild-type
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
S176A
-
lower specific activity than wild-type
D17A
Escherichia coli K12
-
lower specific activity than wild-type
-
E96A
Escherichia coli K12
-
lower specific activity than wild-type
-
N35A
Escherichia coli K12
-
lower specific activity than wild-type
-
S176A
Escherichia coli K12
-
lower specific activity than wild-type
-
T156A
Escherichia coli K12
-
lower specific activity than wild-type
-
Q263R
-
5fold increase in activity. Mutation increases xylose-to-ethanol conversion by 36% and 100% as measured by volumetric production rate and specific production rate, respectively
additional information
-
wild-type Clostridium acetobutylicum ATCC 824 transaldolase lower enzyme activity than overexpressed transaldolase from Escherichia coli K12
T156A
-
lower specific activity than wild-type
additional information
-
overexpressed transaldolase gene higher enzyme activity than wild-type Clostridium acetobutylicum ATCC 824 transaldolase
F189Y
-
homologous human mutant F189 shows the same altered activity as mutant F179Y from Escherichia coli: mutant F189Y is 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; reaction fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate: Km (mM): 340 (dihydroxyacetone), kcat (1/sec): 8.9 (dihydroxyacetone). Reaction fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate: Km (mM) 0.76 (fructose 6-phosphate), kcat (1/sec): 0.21 (fructose 6-phosphate). Reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate: Km (mM): 27 (fructose 6-phosphate), kcat (1/sec): 7.4
additional information
-
sequencing analysis to identify common genetic variations in TALDO1 and their association with squamous cell carcinoma of the head and neck (SCCHN) using samples from a population-based case/control study with both European American and African American former and current smokers is performed. Three polymorphisms in TALDO1 are identified that are associated with SCCHN risk in our EA study population: specifically the 5 upstream variant -490 C to G or T (SNP name: rs10794338), identified as tri-allelic, shows a reduced risk compared with any presence of the common allele. Two intronic high frequency polymorphisms demonstrate a positive association with disease, with the presence of the variant IVS1 + 1874 T to A (SNP name: rs3901233) and IVS4 + 2187A to C (SNP name: rs4963163)
additional information
-
following ingestion of [1,2,3-13C3]glycerol, human glucuronide 13C-isotopomer distributions are quantified by 13C-NMR and the extent of transaldolase exchange for the hepatic glucose 6-phosphate pool is estimated. Results indicate that a substantial fraction of hepatic glucose 6-phosphate undergoes transaldolase exchange in healthy, fed humans. Failure to account for this activity results in a significant overestimation of the indirect pathway contribution to hepatic glycogen synthesis with some commonly used tracers such as (5-3H)glucose and D2O of human hepatic carbohydrate metabolism
TALDELTAS171
-
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
-, Q2TUQ1
TAL gene inactivation by homologous recombination, partial inactivation leads to partial male infertility, complete knockout leads to complete male infertility, TAL deficiency influences the structure and function of mitochondria without compromising the nucleus and DNA integrity and leads to accumulation of sedoheptulose 7-phosphate and depletion of pyridine nucleotides in TAL-deficient tissues, genotypes and phenotypes, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
transaldolase shows a high mucin binding capacity. When exposed on the cell surface of Bifidobacterium bifidum, enzyme may act as an important colonization factor favoring its establishment in the gut. A recombinant Lactococcus lactis strain, engineered to secrete transaldolase, displays a mucin-binding level more than three times higher than the strain not producing the transaldolase
medicine
Bifidobacterium bifidum A8
-
transaldolase shows a high mucin binding capacity. When exposed on the cell surface of Bifidobacterium bifidum, enzyme may act as an important colonization factor favoring its establishment in the gut. A recombinant Lactococcus lactis strain, engineered to secrete transaldolase, displays a mucin-binding level more than three times higher than the strain not producing the transaldolase
-
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
medicine
-
the results provide preliminary evidence that genetic polymorphisms in TALDO1 are associated with squamous cell carcinoma of the head and neck
medicine
-
transaldolase-deficient patients have significantly increased urinary sedoheptulose and sedoheptulose 7-phosphate, associated with subtle elevations of mannoheptulose, sedoheptitol and perseitol. The development of a liquid chromatography-tandem mass spectrometry method for quantitation of the seven-carbon carbohydrates biomarkers in urine is shown
medicine
-
clinical presentation and laboratory findings of a new patient with TALDO deficiency: a two-year-old Arabic boy presented with neonatal onset of anemia and thrombocytopenia, tubulopathy, and rickets and is subsequently found to have cirrhosis and deafness
molecular biology
-
TAL deficiency is shown as a modulator of mitochondrial homoeostasis, Ca2+ fluxing and apoptosis
medicine
-, Q2TUQ1
male mice lacking transaldolase are sterile because of defective forward motility of spermatozoa. Transaldolase -/- spermatozoa show loss of transmembrane potential and mitochondrial membrane integrity. Lack of enzyme influencies structure and function of mitochondria without compromising the nucleus and DNA integrity. Stimulation of de novo glutathione synthesis by oral N-acetyl-cysteine normalizes the low fertility rates of transaldolase +/- males without affecting the sterility of transaldolase -/- mice
synthesis
-
improvement of xylose-to-ethanol bioconversion by mutation Q263R, mutantion leads to 5fold increase in activity and increases ethanol production by 36% and 100% as measured by volumetric production rate and specific production rate, respectively
industry
Trichosporonoides megachiliensis
-
production of abundant intermediates for industrially erythritol production
industry
Trichosporonoides megachiliensis SN-G42
-
production of abundant intermediates for industrially erythritol production
-