2.2.1.1: transketolase
This is an abbreviated version!
For detailed information about transketolase, go to the full flat file.
Word Map on EC 2.2.1.1
-
2.2.1.1
-
thiamin
-
pentose
-
erythrocyte
-
pyrophosphate
-
transaldolase
-
glucose-6-phosphate
-
tpp
-
ribose
-
5-phosphate
-
aldolase
-
non-oxidative
-
glycation
-
encephalopathy
-
pyridoxine
-
apoenzyme
-
phosphoglycerate
-
wernicke
-
baker
-
oxythiamine
-
neuropathy
-
ribose-5-phosphate
-
thiamine-deficient
-
xylulose
-
thiamine-dependent
-
6-phosphogluconate
-
riboflavin
-
calvin
-
pharmacology
-
drug development
-
biotechnology
-
pentose-phosphate
-
xylulokinase
-
industry
-
alpha-ketoglutarate
-
dihydroxyacetone
-
warburg
-
phosphoketolase
-
3-epimerase
-
hemolysates
-
pyrophosphokinase
-
xylitol
-
phosphoribulokinase
-
thiaminase
-
hydroxypyruvate
-
aminopyrimidine
-
fructose-6-phosphate
-
medicine
-
fructose-1,6-bisphosphate
-
antivitaminous
-
erythrose
-
egypt
-
thdp-dependent
-
diphosphate-dependent
-
synthesis
-
isotopomer
-
analysis
- 2.2.1.1
- thiamin
- pentose
- erythrocyte
- pyrophosphate
- transaldolase
- glucose-6-phosphate
- tpp
- ribose
- 5-phosphate
- aldolase
-
non-oxidative
-
glycation
- encephalopathy
- pyridoxine
-
apoenzyme
- phosphoglycerate
- wernicke
-
baker
- oxythiamine
- neuropathy
- ribose-5-phosphate
-
thiamine-deficient
- xylulose
-
thiamine-dependent
- 6-phosphogluconate
- riboflavin
-
calvin
- pharmacology
- drug development
- biotechnology
-
pentose-phosphate
- xylulokinase
- industry
- alpha-ketoglutarate
- dihydroxyacetone
-
warburg
- phosphoketolase
-
3-epimerase
- hemolysates
-
pyrophosphokinase
- xylitol
- phosphoribulokinase
- thiaminase
- hydroxypyruvate
- aminopyrimidine
- fructose-6-phosphate
- medicine
- fructose-1,6-bisphosphate
-
antivitaminous
- erythrose
-
egypt
-
thdp-dependent
-
diphosphate-dependent
- synthesis
-
isotopomer
- analysis
Reaction
Synonyms
glycolaldehydetransferase, STM14_2885, STM14_2886, TK16, TKA, TKL, TKL1, Tkl2, TKT, TKT10, TKT3, TKT7, TktA, TktB, TKTc, TKTL-1, TKTL1, TKTL2, TKTp, transketolase, transketolase 10, transketolase 3, transketolase 7, transketolase A, transketolase B, transketolase like 1, transketolase-1, transketolase-like 1, transketolase-like enzyme 1, transketolase-like-1, transketolase-like-1-gene, transketolase-like-2
ECTree
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Metals Ions
Metals Ions on EC 2.2.1.1 - transketolase
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Ca2+
Mg2+
additional information
Ca2+
-
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+. Influence of Mg2+ is less pronounced than of Ca2+
Ca2+
-
holoenzyme reconstituted in the presence of Ca2+ is more stable than its Mg2+ counterpart
Ca2+
-
thiamine diphosphate affinity to the enzymes active sites is higher in the presence of Ca2+ than in the presence of Mg2+
Ca2+
-
when Ca2+ is substituted for Mg2+, the two active centers of transketolase are nonequivalent in the ability to bind xylulose 5-phosphate
Ca2+
-
in the presence of Ca2+, the enzyme exhibits strong negative active site cooperativity in both xylulose 5-phosphate binding and ribose 5-phosphate binding and positive cooperativity in the catalytic activity
Ca2+
-
in the presence of free Ca2+, the equivalence of the two active centers of the enzyme is lost. Negative cooperativity is induced on binding of either xylulose 5-phosphate or ribose 5-phosphate, whereupon the catalytic conversion of the bound substrates causes the interaction between the centers to become positively cooperative. Enzyme total activity increases in presence of Ca2+
Mg2+
the enzyme attains its full activation at Mg2+ concentration of equal or more than 1 mM. 15 mM used in assay conditions. Mg2+ is fundamental to allow gradual conformational arrangements suited for optimal catalysis. Moreover, Mg2+ is involved in the control of redox sensitivity of the enzyme
Mg2+
is necessary for the catalytic activation of thiamine diphosphate-associated apo-transketolase
Mg2+
-
biochemical correction of abnormal erythrocyte transketolase activity and/or the thiamin pyrophosphate effect invariably depends on the provision of non-caloric nutrients, especially magnesium
Mg2+
The Mg2+ ion is octahedrally coordinated to residues Asp177, Asn207 and Ile209, along with two oxygen atoms of the diphosphate moiety of the cofactor thiamine diphosphate and a water molecule
Mg2+
-
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+. Influence of Mg2+ is less pronounced than of Ca2+
Mg2+
-
holoenzyme reconstituted in the presence of Ca2+ is more stable than its Mg2+ counterpart
Mg2+
-
in the presence of Mg2+, the two active centers of transketolase are equivalent in the ability to bind xylulose 5-phosphate
Mg2+
-
thiamine diphosphate affinity to the enzymes active sites is higher in the presence of Ca2+ than in the presence of Mg2+
Mg2+
-
nonequivalence of the active sites is not observed in presence of Mg2+
-
presence of magnesium ions, alone or in combination with thiamine diphosphate, does not affect the activity