2.2.1.2: transaldolase
This is an abbreviated version!
For detailed information about transaldolase, go to the full flat file.
Word Map on EC 2.2.1.2
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2.2.1.2
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pentose
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transketolase
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glucose-6-phosphate
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5-phosphate
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non-oxidative
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methylotrophic
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hexose
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6-phosphogluconate
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fructose-6-phosphate
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hansenula
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xylulose
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egypt
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boidinii
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triose
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polymorpha
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xylitol
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xylulokinase
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hepatosplenomegaly
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phosphoketolase
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erythrose
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isotopomer
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methanol-induced
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ribitol
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erythritol
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stipitis
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molecular biology
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medicine
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industry
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synthesis
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3-epimerase
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ribulose-5-phosphate
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co-circulation
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hpaiv
- 2.2.1.2
- pentose
- transketolase
- glucose-6-phosphate
- 5-phosphate
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non-oxidative
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methylotrophic
- hexose
- 6-phosphogluconate
- fructose-6-phosphate
- hansenula
- xylulose
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egypt
- boidinii
- triose
- polymorpha
- xylitol
- xylulokinase
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hepatosplenomegaly
- phosphoketolase
- erythrose
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isotopomer
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methanol-induced
- ribitol
- erythritol
- stipitis
- molecular biology
- medicine
- industry
- synthesis
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3-epimerase
- ribulose-5-phosphate
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co-circulation
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hpaiv
Reaction
Synonyms
824-TAL, 824-WT, ATAL, Atalp, dihydroxyacetone synthase, dihydroxyacetonetransferase, formaldehyde transketolase, FoTal, hTAL, NQM1/YGR043C, peroxisomal transaldolase, TAL, Tal1, TAL2, TALase, TALB, TALDO, TALDO1, transaldolase, transaldolase 1, transaldolase A, transaldolase B, transaldolase STY3758, transaldolase1, transladolase B, XIF1
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2.2.1.2 transaldolaseAdvanced search results
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Engineering on EC 2.2.1.2 - transaldolase
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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
F178E
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mutant is able to catalyze aldol reactions and readily accepts hihydroxypropanone and hydroxypropanone
F178E/S176A
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improved acceptance of substrate hydroxypropanone compared with mutant F178E
F178Y
F178Y/R181E
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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
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little lower activity than the wild type, but same stability against urea and thermal inactivation
R300E
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little lower activity than the wild type, but same stability against urea and thermal inactivation
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
Q263R
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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
E60Q/F132Y
the mutant enzyme has no transaldolase activity and shows D-fructose 6-phosphate aldolase activity
F132Y
the mutant enzyme has no transaldolase activity and shows D-fructose 6-phosphate aldolase activity
additional information
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
F189Y
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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
F189Y
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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
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wild-type Clostridium acetobutylicum ATCC 824 transaldolase lower enzyme activity than overexpressed transaldolase from Escherichia coli K12
additional information
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overexpressed transaldolase gene higher enzyme activity than wild-type Clostridium acetobutylicum ATCC 824 transaldolase
additional information
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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
additional information
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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
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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
additional information
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
