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 hide
2.2.1.2
-
RECOMMENDED NAME
GeneOntology No.
transaldolase
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldehyde group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Bifidobacterium shunt
-
-
Biosynthesis of antibiotics
-
-
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
-
-
pentose phosphate pathway (non-oxidative branch)
-
-
Rubisco shunt
-
-
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9014-46-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
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
strain LS3, gene ATAL
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Chromatium sp.
-
-
-
Manually annotated by BRENDA team
var. neoformans, strain JEC21
-
-
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
Euglena sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
transaldolase/glucose-6-phosphate isomerase bifunctional enzyme
Swissprot
Manually annotated by BRENDA team
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
brewer's yeast
-
-
Manually annotated by BRENDA team
2 isoforms
-
-
Manually annotated by BRENDA team
Tetranychus telarius
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
dysfunction could lead to liver cirrhosis and neonatal multi-organ diseases
physiological function
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 + D-fructose 6-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-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
glyceraldehyde 3-phosphate + ?
show the reaction diagram
-
assay at 25C, pH 7.5
-
-
?
D-fructose 6-phosphate + D-erythrose 4-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
preferred substrates
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
?
show the reaction diagram
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 + D-erythrose-4-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
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
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 SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-fructose 6-phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no metal requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
diphosphate
L-Glyceraldehyde
-
-
phosphate
sedoheptulose 7-phosphate
-
-
Sodium borohydride
-
-
sulfate
Tetranitromethane
-
isoenzyme III, only in presence of the substrates D-fructose 6-phosphate and sedoheptulose 7-phosphate
Tris-HCl
-
-
additional information
-
phosphate starvation leads to the downregulation of the enzyme expression
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
increased expression in media containing 5% NaCl
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 0.555
D-erythrose 4-phosphate
0.013 - 0.49
D-erythrose-4-phosphate
0.056 - 27
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 - 340
dihydroxyacetone
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 - 2.4
glyceraldehyde 3-phosphate
0.18 - 0.46
sedoheptulose 7-phosphate
additional information
additional information
-
positive cooperativity in binding of substrates
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.9
D-erythrose 4-phosphate
Thermotoga maritima
Q9WYD1
pH 9.0, 80C
6.44
D-erythrose-4-phosphate
Blastobotrys adeninivorans
Q0E4W0
-
0.21 - 22.3
D-fructose 6-phosphate
0.53
D-glyceraldehyde
Escherichia coli
-
mutant F178, pH 8.5, 30C
4.3 - 8.9
dihydroxyacetone
0.54
DL-glyceraldehyde
Escherichia coli
-
mutant F178, pH 8.5, 30C
12 - 13
glyceraldehyde 3-phosphate
additional information
D-erythrose 4-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
139.9
D-erythrose-4-phosphate
Fusarium oxysporum
-
-
9651
10.38
D-fructose-6-phosphate
Fusarium oxysporum
-
-
4331
9
D-glyceraldehyde
Escherichia coli
-
mutant F178, pH 8.5, 30C
639
4.3
DL-glyceraldehyde
Escherichia coli
-
mutant F178, pH 8.5, 30C
487
5000 - 6600
glyceraldehyde 3-phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0049
arabinose-5-phosphate
-
isoform ToTal1, 25C, pH 8.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
3.84
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
recombinant enzyme; recombinant enzyme
7.3 - 8.1
7.5
-
imidazole buffer
8.2
-
-
8.5 - 9.5
-
-
9
in glycine-NaOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
; native enzyme; native enzyme, 80% of maximal activity within this range
5.4 - 6.3
recombinant enzyme; recombinant enzyme, 80% of maximal activity within this range
6.3 - 9.5
-
about 50% of activity maximum at pH 6.3 and 9.5, isoenzyme I, II, III
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 40
-
-
20
; native and recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18 - 25
; native and recombinant enzyme, 80% of maximal activity within this range
40
28% of maximum activity
60
73% of maximum activity
90
96% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
isoelectric focusing-PAGE
5.14
-
isoelectric focusing
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
-
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
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoform ToTal1 and ToTal2
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
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 (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)
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
denatured enzyme, SDS-PAGE
36000
-
SDS-PAGE, denatured
36200
-
computer analysis of a 2-D PAGE
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
gel filtration
76100 - 77400
-
ultracentrifugation and gel filtration, isoenzyme I, sedimentation equilibrium ultracentrifugation
77000
-
gel filtration
140000
gel filtration; gel filtration; native enzyme (tetramer), gel filtration
271000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
-
10 * 24000, SDS-PAGE, 10 * 23960, calculated
monomer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
cleavage of 6 kDa plastid targeting sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
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
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
-
stable
486035
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
706567
7
-
room temperature, stable for a few hours
486032
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
55
-
total inactivation of enzyme
60
half life 198 h
90
-
15 min, 20% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
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
LITERATURE
-16C, 10-20% loss of activity after 1 week
-
-20C, stable for at least 2 months
-
-20C, stable for several months
-
2C, for at least 8 weeks
-
30C, 1 h, 20% activity lost
-
40C, 1 h, 40% activity lost
-
isoenzymes I and III are stable in the cold in the crystalline form for over 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
anion exchange and gel filtration chromatographies, after last step 50fold purification
-
II; III; isoenzymes: I
-
Ni2+ affinity column
recombinant enzyme
-
using Ni-NTA chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
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
amplification and expression in Escherichia coli strain HB523 harboring the phbCAB operon to shift the metabolic flux to production of poly-beta-hydroxybutyrate
-
expression as a fusion protein with glutathione S-transferase
-
expression in Escherichia coli
expression in Escherichia coli BL21
isoform ToTal1 and ToTal2, expression in Escherichia coli
-
mutant and wild-type protein are expressed in Escherichia coli as a GST-fusion protein
-
mutant and wild-type protein are expressed in Escherichia coli as a His-tagged fusion protein
overexpression in Clostridium acetobutylicum ATCC 824
-
overexpression in Escherichia coli
partial DNA and amino acid sequence determination and analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of is up-regulated in the presence of xylose
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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
T156A
-
lower specific activity than wild-type
D17A
-
lower specific activity than wild-type
-
E96A
-
lower specific activity than wild-type
-
N35A
-
lower specific activity than wild-type
-
S176A
-
lower specific activity than wild-type
-
T156A
-
lower specific activity than wild-type
-
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
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
medicine
molecular biology
-
TAL deficiency is shown as a modulator of mitochondrial homoeostasis, Ca2+ fluxing and apoptosis
synthesis
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