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Information on EC 2.2.1.1 - transketolase and Organism(s) Scheffersomyces stipitis and UniProt Accession P34736

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EC Tree
     2 Transferases
         2.2 Transferring aldehyde or ketonic groups
             2.2.1 Transketolases and transaldolases
                2.2.1.1 transketolase
IUBMB Comments
A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
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Scheffersomyces stipitis
UNIPROT: P34736
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Word Map
The taxonomic range for the selected organisms is: Scheffersomyces stipitis
The enzyme appears in selected viruses and cellular organisms
Synonyms
transketolase, tktl1, transketolase a, transketolase-like 1, tktl-1, transketolase-like-1, tktl2, transketolase-like enzyme 1, transketolase-like-2, tkt10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycolaldehydetransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
keto group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glycolaldehydetransferase
A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-48-6
-
SUBSTRATE
PRODUCT                       
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-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
show the reaction diagram
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
show the reaction diagram
-
-
-
r
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
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029
D-fructose 6-phosphate
wild type enzyme, at pH 8.0 and 25°C
0.145 - 0.68
D-xylulose 5-phosphate
0.031 - 0.294
sedoheptulose 7-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26.87
D-fructose 6-phosphate
wild type enzyme, at pH 8.0 and 25°C
0.35 - 25.31
D-xylulose 5-phosphate
20.58 - 28.642
sedoheptulose 7-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
920
D-fructose 6-phosphate
wild type enzyme, at pH 8.0 and 25°C
0.66 - 140
D-xylulose 5-phosphate
70 - 910
sedoheptulose 7-phosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 74969, calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild type and mutants H261F, H66C/261C, R356L and R525L enzymes in complex with various physiological ligands, hanging drop vapor diffusion method, using 0.1 M MES at pH 6.5, 0.1M NaCl, 30% (w/V) PEG 400
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H27A
in the reaction with sedoheptulose 7-phosphate (backward) the mutant exhibits weaker activity relative to the wild type enzyme
R356L
in the reaction with D-xylulose 5-phosphate (forward) the mutant exhibits weaker activity relative to the wild type enzyme
R525L
in the reaction with D-xylulose 5-phosphate (forward) the mutant exhibits weaker activity relative to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-NTA agarose resin column chromatography and Superdex S-200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hsu, L.J.; Hsu, N.S.; Wang, Y.L.; Wu, C.J.; Li, T.L.
Structural and biochemical interrogation on transketolase from Pichia stipitis for new functionality
Protein Eng. Des. Sel.
29
513-522
2016
Scheffersomyces stipitis (P34736), Scheffersomyces stipitis
Manually annotated by BRENDA team