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2 D-xylulose 5-phosphate
glyceraldehyde 3-phosphate + glycolaldehyde
-
reversible single substrate reaction, about 6% of the double-substrate reaction rate
-
-
?
2 hydroxypyruvate
2 glyoxylic acid + erythrulose
-
-
-
-
ir
2 propanal + 2 lithium beta-hydroxypyruvate
(3S)-1,3-dihydroxypentan-2-one + (3R)-1,3-dihydroxypentan-2-one + 2 CO2 + 2 Li+
2 pyruvate
erythrulose
-
-
-
?
2-deoxy-D-erythrose 4-phosphate + ?
?
-
-
-
-
?
2-deoxy-D-ribose 5-phosphate + ?
?
-
-
-
-
?
2-methoxyethanal + glycolaldehyde
(3S)-1,3-dihydroxy-4-methoxybutan-2-one
-
-
-
?
2-phenylethanal + hydroxypyruvate
(S)-1,3-dihydroxy-4-phenylbutan-2-one + CO2
-
-
-
-
ir
3-formylbenzoic acid + hydroxypyruvate
3-(1,3-dihydroxy-2-oxopropyl)benzoic acid + CO2
-
-
-
-
?
3-formylbenzoic acid + pyruvate
3-(2-oxopropanoyl)benzoate + CO2
-
-
-
?
3-formylbenzoic acid + pyruvate
3-(2-oxopropanoyl)benzoic acid + CO2
-
-
-
ir
3-hydroxybenzaldehyde + hydroxypyruvate
1,3-dihydroxy-1-(3-hydroxyphenyl)propan-2-one + CO2
-
-
-
-
?
3-hydroxypyruvate + n-pentanal
1,3-dihydroxy-2-heptanone + CO2
3% yield after 1 h (92% (S)), 12% yield after 3 h (87% (S))
-
-
ir
3-hydroxypyruvate + propanal
1,3-dihydroxy-2-pentanone + CO2
12% yield after 1 h (57% (S)), 32% yield after 3 h (53% (S))
-
-
ir
3-phenylpropanal + hydroxypyruvate
(S)-1,3-dihydroxy-5-phenylpentan-2-one + CO2
-
-
-
-
ir
4-formylbenzoic acid + hydroxypyruvate
4-(1,3-dihydroxy-2-oxopropyl)benzoic acid + CO2
-
-
-
-
?
benzaldehyde + hydroxypyruvate
(R)-1,3-dihydroxy-1-phenylpropan-2-one + CO2
-
the wild type enzyme shows very little activity against benzaldehyde
-
-
ir
beta-hydroxypyruvate + ?
?
-
-
-
-
?
beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + CO2
butanal + glycolaldehyde
(3S)-1,3-dihydroxyhexan-2-one
-
-
-
?
butanal + hydroxypyruvate
1,3-dihydroxyhexan-2-one + CO2
-
-
-
?
butyraldehyde + hydroxypyruvate
? + CO2
-
-
-
?
D-arabinose 5-phosphate + ?
?
-
-
-
-
?
D-erythrose + ?
?
-
-
-
-
?
D-erythrose 4-phosphate + ?
?
D-erythrose 4-phosphate + D-xylulose 5-phosphate
?
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-ribose 5-phosphate
?
D-fructose 6-phosphate + D-ribose 5-phosphate
D-erythrose 4-phosphate + sedoheptulose 7-phosphate
-
-
-
?
D-fructose 6-phosphate + Fe(CN)3-
glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+
D-glucose 6-phosphate + D-fructose-6-phosphate
octulose 8-phosphate + ?
-
reaction catalyzed by transketolase 7 and 10, but not transketolase 3
-
-
?
D-glucose 6-phosphate + hydroxypyruvate
2-D-glycero-D-ido-octulose phosphate + ?
-
reaction is catalyzed by either isoform Tkt7 or isoform Tkt10 or both
-
-
?
D-glyceraldehyde + hydroxypyruvate
D-ribulose + ?
-
-
-
?
D-glyceraldehyde + hydroxypyruvate
D-xylulose + CO2
-
-
-
?
D-glyceraldehyde 3-phosphate + D-fructose 6-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
?
D-lactaldehyde + hydroxypyruvate
5-deoxy-D-ribulose + ?
-
-
-
?
D-ribose + hydroxypyruvate
? + CO2
-
-
-
?
D-ribose 5-phosphate + 2,3-dihydroxy-4-O-(2'-oxo-benzopyran-7'-yl)-D-threose
?
-
fluorogenic substrate as probe for measuring wild-type or altered transketolase activity from variants with improved or new properties acquired by random mutagenesis
-
-
?
D-ribose 5-phosphate + 7'-(2,3,5-trihydroxy-4-oxo-pentyl)oxycoumarin
?
-
fluorogenic substrate as probe for measuring wild-type or altered transketolase activity from variants with improved or new properties acquired by random mutagenesis
-
-
?
D-ribose 5-phosphate + 7-(2',3',5'-trihydroxy-4'-oxo-pentyl)oxycoumarine
?
-
fluorogenic substrate as probe for measuring wild-type or altered transketolase activity from variants with improved or new properties acquired by random mutagenesis
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose-5-phosphate + L-erythrulose
D-sedoheptulose 7-phosphate + glycolaldehyde
-
-
-
?
D-threose 4-phosphate + ?
?
-
-
-
-
?
D-xylulose 5-phosphate + D-erythrose 4-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + D-ribose 5-phosphate
?
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-xylulose-5-phosphate + D-ribose-5-phosphate
?
-
-
-
?
DL-glyceraldehyde + ?
?
-
-
-
-
?
DL-glyceraldehyde + hydroxypyruvate
? + CO2
-
-
-
?
DL-glyceraldehyde 3-phosphate + ?
?
formaldehyde + ?
?
-
-
-
-
?
fructose 6-phosphate + ?
?
fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
-
r
fructose-6-phosphate + hydroxypyruvate
?
-
-
-
-
?
glyceraldehyde 3-phosphate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
glycolaldehyde + ?
?
-
-
-
-
?
glycolaldehyde + hydroxypyruvate
L-erythrulose + CO2
-
-
-
?
glycolaldehyde + pyruvate
3,4-dihydroxy-2-butanone + CO2
-
-
-
?
hexanal + 2-oxoheptanoic acid
7-hydroxydodecan-6-one + CO2
-
-
-
?
hexanal + pyruvate
2-hydroxyheptanal + CO2
-
-
-
?
hydroxypyruvate + ?
?
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
hydroxypyruvate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + ?
-
-
-
-
?
hydroxypyruvate + D-ribose-5-phosphate
D-sedoheptulose 7-phosphate
-
-
-
ir
hydroxypyruvate + ferricyanide + H2O
glycolic acid + ferrocyanide + ?
-
-
-
-
?
hydroxypyruvate + glycolaldehyde
erythrulose + ?
-
-
-
-
?
hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
hydroxypyruvate + ribose 5-phosphate
sedoheptulose 7-phosphate + ?
L-arabinose + ?
?
-
-
-
-
?
L-arabinose + lithium beta-hydroxypyruvate
L-gluco-heptulose + CO2 + Li+
48% conversion after 24 h
-
-
?
L-erythrulose + D-ribose-5-phosphate
D-sedoheptulose 7-phosphate + glycolaldehyde
-
-
-
?
L-erythrulose + ribose 5-phosphate
?
-
-
-
-
?
L-glyceraldehyde + hydroxypyruvate
L-ribulose + ?
minor reactivity
-
-
?
L-lactaldehyde + hydroxypyruvate
5-deoxy-L-ribulose + ?
minor reactivity
-
-
?
Li-hydroxypyruvate + propionaldehyde
1,3-dihydroxypentan-2-one + ?
-
-
-
-
?
lithium beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
-
-
-
-
?
N-acetyl-O'-(2R,3S,5-trihydroxy-4-oxopentyl)-L-tyrosine ethyl ester + D-ribose 5-phosphate
N-acetyl-O-[(2R)-2-hydroxy-3-oxopropyl]-L-tyrosine + D-sedoheptulose 7-phosphate
-
transketolase catalyzes the hydroxyacetyl group transfer from the donor substrate N-acetyl-O'-(2R,3S,5-trihydroxy-4-oxopentyl)-L-tyrosine ethyl ester to D-ribose-5-phosphate, the natural acceptor substrate of transketolase. Transketolase catalyzes C2-C3 bond cleavage from N-acetyl-O'-(2R,3S,5-trihydroxy-4-oxopentyl)-L-tyrosine ethyl ester
-
-
?
pentanal + 2-oxohexanoic acid
6-hydroxydecan-5-one + CO2
-
-
-
?
pentanal + pyruvate
2-hydroxyhexanal + CO2
-
-
-
?
propanal + glycolaldehyde
(3S)-1,3-dihydroxypentan-2-one
propionaldehyde + 2-oxobutanoic acid
4-hydroxyhexan-3-one + CO2
-
-
-
?
propionaldehyde + pyruvate
2-hydroxybutanal + CO2
-
-
-
?
ribulose 5-phosphate + ribose 5-phosphate
a heptulose phosphate + glyceraldehyde 3-phosphate
-
ribulose is cleaved and ribose acts as acceptor
-
-
?
sedoheptulose 7-phosphate + ?
?
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
additional information
?
-
2 propanal + 2 lithium beta-hydroxypyruvate
(3S)-1,3-dihydroxypentan-2-one + (3R)-1,3-dihydroxypentan-2-one + 2 CO2 + 2 Li+
-
use of lithium beta-hydroxypyruvate as a donor renders the reaction irreversible
wild-type, 58% enantiomeric excess for 3S-product
-
r
2 propanal + 2 lithium beta-hydroxypyruvate
(3S)-1,3-dihydroxypentan-2-one + (3R)-1,3-dihydroxypentan-2-one + 2 CO2 + 2 Li+
-
-
-
-
ir
beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + CO2
-
-
-
-
?
beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + CO2
-
-
-
?
beta-hydroxypyruvate + glycolaldehyde
L-erythrulose + CO2
-
-
-
-
?
D-erythrose 4-phosphate + ?
?
-
-
-
-
?
D-erythrose 4-phosphate + ?
?
-
-
-
-
?
D-erythrose 4-phosphate + ?
?
-
-
-
-
?
D-erythrose 4-phosphate + D-xylulose 5-phosphate
?
-
-
-
r
D-erythrose 4-phosphate + D-xylulose 5-phosphate
?
-
-
-
r
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
D-fructose 6-phosphate + D-ribose 5-phosphate
?
-
40% as effective as D-xylulose 5-phosphate
-
-
?
D-fructose 6-phosphate + D-ribose 5-phosphate
?
-
-
-
-
?
D-fructose 6-phosphate + D-ribose 5-phosphate
?
-
-
-
-
?
D-fructose 6-phosphate + D-ribose 5-phosphate
?
-
-
-
-
?
D-fructose 6-phosphate + Fe(CN)3-
glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+
-
-
-
-
?
D-fructose 6-phosphate + Fe(CN)3-
glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+
-
-
-
?
D-fructose 6-phosphate + Fe(CN)3-
glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+
-
-
-
?
D-fructose 6-phosphate + Fe(CN)3-
glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-xylulose 5-phosphate + D-erythrose 4-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
best acceptor with D-xylulose 5-phosphate as donor
-
-
r
D-xylulose 5-phosphate + D-erythrose 4-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-erythrose 4-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-erythrose 4-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
L-erythrulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-arabinose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-deoxyribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
glycolaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
DL-glyceraldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
octulose 8-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
allose 6-phosphate, glucose 6-phosphate, formaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-ribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
sedoheptulose 7-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-xylulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ping pong bi bi mechanism
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
best donor with D-ribose 5-phosphate as acceptor
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-ribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
catalyzes reversible transfer of a keto group between several donor and acceptor substrates
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
L-erythrulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-arabinose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-deoxyribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
glycolaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
DL-glyceraldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
octulose 8-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
allose 6-phosphate, glucose 6-phosphate, formaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-ribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
sedoheptulose 7-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-xylulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
L-erythrulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-arabinose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-deoxyribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
glycolaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
DL-glyceraldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
octulose 8-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
allose 6-phosphate, glucose 6-phosphate, formaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-ribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
sedoheptulose 7-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-xylulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
L-erythrulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
glycolaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-ribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
sedoheptulose 7-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
L-erythrulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-arabinose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-deoxyribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
glycolaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
DL-glyceraldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
octulose 8-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
allose 6-phosphate, glucose 6-phosphate, formaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-ribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
sedoheptulose 7-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-xylulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
pathway in non-oxidative sequence of pentose cycle
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
two optical methods for transketolase activity assay using only one substrate, xylulose 5-phosphate or glycol aldehyde. For transketolase activity assay in the first method, it is necessary to add auxiliary enzyme, glyceraldehyde phosphate dehydrogenase. It is not needed in the second method. The range of transketolase concentration in the activity assay is 0.036-0.144 U/ml for the first method and 1.8-6.8 U/ml for the second one
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
in presence of Ca2+, the active centers of the enzyme are nonequivalent with respect to both ribose 5-phosphate and xylulose 5-phosphate binding
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
the active centers of the enzyme are nonequivalent with respect to ribose 5-phosphate binding. Under the conditions where only one out of the two active centers of transketolase is functional, their affinities for ribose 5-phosphate are identical. Nonequivalence becomes apparent when the substrate interacts with one of the two active centers. As a consequence, the affinity of the second active center for ribose 5-phosphate decreases
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
L-erythrulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-arabinose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-deoxyribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
glycolaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
DL-glyceraldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
octulose 8-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
allose 6-phosphate, glucose 6-phosphate, formaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-ribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
sedoheptulose 7-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-xylulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
L-erythrulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-arabinose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-deoxyribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
glycolaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
DL-glyceraldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
octulose 8-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
allose 6-phosphate, glucose 6-phosphate, formaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-ribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
sedoheptulose 7-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-xylulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
pathway in non-oxidative sequence of pentose cycle
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
L-erythrulose
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
glycolaldehyde
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
and acceptor substrates may be: D-glyceraldehyde 3-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-ribose 5-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
sedoheptulose 7-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
D-erythrose 4-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
sedoheptulose 7-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
wide specificity for both reactants: donor substrates may be: fructose 6-phosphate
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
DL-glyceraldehyde 3-phosphate + ?
?
-
-
-
-
?
DL-glyceraldehyde 3-phosphate + ?
?
-
-
-
?
fructose 6-phosphate + ?
?
-
-
-
-
?
fructose 6-phosphate + ?
?
-
-
-
-
?
fructose 6-phosphate + ?
?
-
-
-
?
fructose 6-phosphate + ?
?
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
ir
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
ir
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
enantioselective
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
enantioselective
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
CO2 + ribulose 5-phosphate
-
-
-
-
ir
hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
-
-
-
-
?
hydroxypyruvate + glycolaldehyde
L-erythrulose + ?
-
-
-
?
hydroxypyruvate + ribose 5-phosphate
sedoheptulose 7-phosphate + ?
-
-
-
-
?
hydroxypyruvate + ribose 5-phosphate
sedoheptulose 7-phosphate + ?
-
-
-
-
?
hydroxypyruvate + ribose 5-phosphate
sedoheptulose 7-phosphate + ?
-
-
-
?
propanal + glycolaldehyde
(3S)-1,3-dihydroxypentan-2-one
-
-
-
-
?
propanal + glycolaldehyde
(3S)-1,3-dihydroxypentan-2-one
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
additional information
?
-
-
low cost, rapid colorimetric transketolase assay, able to detect value above 8% bioconversion using non-alpha-hydroxylated aldehydes as acceptor substrates. The assay is significantly faster and more convenient to use than HPLC and can be used with a range of aliphatic and aromatic aldehydes. In addition, analysis of the alpha,alpha'-dihydroxyketone produced in the bioconversion can be quantified using this assay system with high-throughput. Furthermore, this method has the potential to be used to screen other chemical reactions or bioconversions leading to the formation of products possessing a 2-hydroxyketone motif
-
-
?
additional information
?
-
the wild type enzyme shows no activity with 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde
-
-
-
additional information
?
-
-
the wild type enzyme shows no activity with 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde
-
-
-
additional information
?
-
-
no acceptors with D-xylulose 5-phosphate as donor substrate: glucose 6-phosphate
-
-
?
additional information
?
-
-
the enzyme interacts with the Atg1 kinase complex
-
-
-
additional information
?
-
-
D-arabinose 5-phosphate
-
-
?
additional information
?
-
-
no acceptors with D-xylulose 5-phosphate as donor substrate: glucose 6-phosphate
-
-
?
additional information
?
-
-
no acceptors are D-ribose, formaldehyde, acetaldehyde, glucose 6-phosphate
-
-
?
additional information
?
-
-
transketolase reaction is irreversible when hydroxypyruvate is used as a donor substrate
-
-
?
additional information
?
-
the enzyme shows a broad substrate specificity with D-xylulose 5-phosphate, D-fructose 6-phosphate, erythrulose 4-phosphate, and sedoheptulose 7-phosphate as typical donor substrates as well as D-ribose 5-phosphate, glyceraldehyde 3-phosphate, and D-erythrose 4-phosphate as typical acceptor substrates
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate specificity with D-xylulose 5-phosphate, D-fructose 6-phosphate, erythrulose 4-phosphate, and sedoheptulose 7-phosphate as typical donor substrates as well as D-ribose 5-phosphate, glyceraldehyde 3-phosphate, and D-erythrose 4-phosphate as typical acceptor substrates
-
-
?
additional information
?
-
A0A0F6B484; A0A0F6B483
isoform TktA is responsible for more than 88% of the transketolase activity in wild type cells
-
-
-
additional information
?
-
isoform TktA is responsible for more than 88% of the transketolase activity in wild type cells
-
-
-
additional information
?
-
isoform TktA is responsible for more than 88% of the transketolase activity in wild type cells
-
-
-
additional information
?
-
-
isoform TktA is responsible for more than 88% of the transketolase activity in wild type cells
-
-
-
additional information
?
-
A0A0F6B484; A0A0F6B483
isoform TktA is responsible for more than 88% of the transketolase activity in wild type cells
-
-
-
additional information
?
-
isoform TktA is responsible for more than 88% of the transketolase activity in wild type cells
-
-
-
additional information
?
-
isoform TktA is responsible for more than 88% of the transketolase activity in wild type cells
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-erythrose 4-phosphate + D-xylulose 5-phosphate
?
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
erythrose 4-phosphate + D-xylulose 5-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + D-ribose 5-phosphate
?
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-xylulose-5-phosphate + D-ribose-5-phosphate
?
-
-
-
?
fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
-
r
glyceraldehyde 3-phosphate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
additional information
?
-
D-erythrose 4-phosphate + D-xylulose 5-phosphate
?
-
-
-
r
D-erythrose 4-phosphate + D-xylulose 5-phosphate
?
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
erythrose 4-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-ribose 5-phosphate + D-xylulose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ping pong bi bi mechanism
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
pathway in non-oxidative sequence of pentose cycle
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
ubiquitous enzyme, involved in carbohydrate and nucleic acid metabolism, bacterial pentose biosynthesis, microbial shikimic acid biosynthesis, formaldehyde metabolism
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
pathway in non-oxidative sequence of pentose cycle
-
-
?
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-xylulose 5-phosphate + D-ribose 5-phosphate
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
-
-
r
additional information
?
-
the enzyme shows a broad substrate specificity with D-xylulose 5-phosphate, D-fructose 6-phosphate, erythrulose 4-phosphate, and sedoheptulose 7-phosphate as typical donor substrates as well as D-ribose 5-phosphate, glyceraldehyde 3-phosphate, and D-erythrose 4-phosphate as typical acceptor substrates
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate specificity with D-xylulose 5-phosphate, D-fructose 6-phosphate, erythrulose 4-phosphate, and sedoheptulose 7-phosphate as typical donor substrates as well as D-ribose 5-phosphate, glyceraldehyde 3-phosphate, and D-erythrose 4-phosphate as typical acceptor substrates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.3 - 56
3-formylbenzoic acid
180 - 390
3-Hydroxybenzaldehyde
2 - 251
4-formylbenzoic acid
10
D,L-glyceraldehyde
-
-
2.1
D,L-glyceraldehyde 3-phosphate
-
-
0.023 - 0.36
D-erythrose 4-phosphate
0.029 - 0.72
D-fructose 6-phosphate
6
D-glyceraldehyde
at pH 7.2 and 50°C
0.67 - 0.92
D-glyceraldehyde 3-phosphate
8.4
D-Lactaldehyde
at pH 7.2 and 50°C
0.007 - 7
D-ribose 5-phosphate
0.13 - 2.75
D-ribose-5-phosphate
0.0056 - 4.08
D-xylulose 5-phosphate
0.61 - 11
fructose 6-phosphate
2.25
fructose-6-phosphate
-
-
4.9
glyceraldehyde 3-phosphate
-
4.78 - 33
Hydroxypyruvate
300
L-glyceraldehyde
Km above 300 mM, at pH 7.2 and 50°C
300
L-lactaldehyde
Km above 300 mM, at pH 7.2 and 50°C
26
lithium beta-hydroxypyruvate
-
pH 7.0, 25°C
0.031 - 4
sedoheptulose 7-phosphate
0.0003 - 0.007
thiamine diphosphate
0.0365 - 0.16
Xylulose 5-phosphate
additional information
additional information
-
1.3
3-formylbenzoic acid
-
mutant enzyme S385Y/D469T/R520Q, at pH 7.0 and 22°C
1.7
3-formylbenzoic acid
-
mutant enzyme S385T/D469T/R520Q, at pH 7.0 and 22°C
13
3-formylbenzoic acid
-
mutant enzyme D469T/R520Q, at pH 7.0 and 22°C
18
3-formylbenzoic acid
-
mutant enzyme S385E/D469T/R520Q, at pH 7.0 and 22°C
56
3-formylbenzoic acid
-
mutant enzyme D469T, at pH 7.0 and 22°C
180
3-Hydroxybenzaldehyde
-
mutant enzyme S385T/D469T/R520Q, at pH 7.0 and 22°C
245
3-Hydroxybenzaldehyde
-
mutant enzyme S385E/D469T/R520Q, at pH 7.0 and 22°C
390
3-Hydroxybenzaldehyde
-
mutant enzyme S385Y/D469T/R520Q, at pH 7.0 and 22°C
2 - 3
4-formylbenzoic acid
-
mutant enzyme S385T/D469T/R520Q, at pH 7.0 and 22°C
13
4-formylbenzoic acid
-
mutant enzyme S385Y/D469T/R520Q, at pH 7.0 and 22°C
25
4-formylbenzoic acid
-
mutant enzyme D469T/R520Q, at pH 7.0 and 22°C
72
4-formylbenzoic acid
-
mutant enzyme S385E/D469T/R520Q, at pH 7.0 and 22°C
251
4-formylbenzoic acid
-
mutant enzyme D469T, at pH 7.0 and 22°C
0.023
D-erythrose 4-phosphate
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.082
D-erythrose 4-phosphate
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.09
D-erythrose 4-phosphate
-
-
0.099
D-erythrose 4-phosphate
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.36
D-erythrose 4-phosphate
-
-
0.029
D-fructose 6-phosphate
wild type enzyme, at pH 8.0 and 25°C
0.25
D-fructose 6-phosphate
-
isoform TKTp, at pH 7.7 and 55°C
0.34
D-fructose 6-phosphate
-
pH 7.6, temperature not specified in the publication
0.6
D-fructose 6-phosphate
pH 7.6, 37°C
0.72
D-fructose 6-phosphate
-
isoform TKTc, at pH 7.5 and 55°C
0.67
D-glyceraldehyde 3-phosphate
-
isoform TKTp, at pH 7.7 and 55°C
0.92
D-glyceraldehyde 3-phosphate
-
isoform TKTc, at pH 7.5 and 55°C
0.007
D-ribose 5-phosphate
-
and second value 0.698 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication
0.014
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Ca2+
0.0362
D-ribose 5-phosphate
-
wild-type
0.058
D-ribose 5-phosphate
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.06
D-ribose 5-phosphate
-
first active center of transketolase
0.06
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied
0.063
D-ribose 5-phosphate
-
pH 7.6, 22°C
0.08
D-ribose 5-phosphate
-
hemiholotransketolase 2, i.e., transketolase, in which the functional active center has a lower affinity for thiamine diphosphate than hemiholotransketolase 1
0.09
D-ribose 5-phosphate
-
hemiholotransketolase 1, i. e. transketolase, in which the functional active center has a higher affinity for the coenzyme than the other active center
0.093
D-ribose 5-phosphate
-
H263A
0.095
D-ribose 5-phosphate
-
-
0.12
D-ribose 5-phosphate
-
isoform TKTc, at pH 7.5 and 55°C
0.146
D-ribose 5-phosphate
-
wild-type
0.146
D-ribose 5-phosphate
wild-type
0.15
D-ribose 5-phosphate
-
H481A
0.159
D-ribose 5-phosphate
-
pH 7.6, temperature not specified in the publication
0.193
D-ribose 5-phosphate
-
H69A
0.25
D-ribose 5-phosphate
-
second active center of transketolase
0.25
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied
0.25
D-ribose 5-phosphate
-
isoform TKTp, at pH 7.7 and 55°C
0.29
D-ribose 5-phosphate
-
H30A
0.3
D-ribose 5-phosphate
-
cosubstrate D-xylulose 5-phosphate
0.33
D-ribose 5-phosphate
-
-
0.33
D-ribose 5-phosphate
-
cosubstrate D-xylulose 5-phosphate
0.356
D-ribose 5-phosphate
-
wild-type, pH 6.7, 25°C
0.4
D-ribose 5-phosphate
-
-
0.4
D-ribose 5-phosphate
-
-
0.4
D-ribose 5-phosphate
-
0.4
D-ribose 5-phosphate
-
cosubstrate D-xylulose 5-phosphate
0.4
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Mg2+
0.4
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Mg2+
0.436
D-ribose 5-phosphate
-
mutant C160S, pH 7.9, 25°C
0.48
D-ribose 5-phosphate
recombinant enzyme, pH 7.6, 30°C
0.53
D-ribose 5-phosphate
-
-
0.6
D-ribose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Ca2+
0.61
D-ribose 5-phosphate
His-tagged recombinant enzyme, pH 7.6, 30°C
0.63
D-ribose 5-phosphate
-
cosubstrate D-xylulose 5-phosphate
0.66
D-ribose 5-phosphate
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.698
D-ribose 5-phosphate
-
and first value 0.007 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication
0.72
D-ribose 5-phosphate
-
cosubstrate D-xylulose 5-phosphate
0.73
D-ribose 5-phosphate
with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.739
D-ribose 5-phosphate
-
mutant C160E, pH 7.6, 25°C
0.8
D-ribose 5-phosphate
pH 7.6, 37°C
0.8
D-ribose 5-phosphate
-
pH 7.5, 22°C
0.837
D-ribose 5-phosphate
-
mutant C160D, pH 8.5, 25°C
0.879
D-ribose 5-phosphate
-
R433A
0.882
D-ribose 5-phosphate
-
mutant C160A, pH 7.8, 25°C
0.949
D-ribose 5-phosphate
-
wild-type, pH 7.8, 25°C
1.4
D-ribose 5-phosphate
-
-
1.75
D-ribose 5-phosphate
D477A
2.316
D-ribose 5-phosphate
-
wild-type, pH 8.5, 25°C
5.65
D-ribose 5-phosphate
R359A
5.97
D-ribose 5-phosphate
H469A
7
D-ribose 5-phosphate
R528A
0.13
D-ribose-5-phosphate
at pH 7.5 and 50°C
0.2
D-ribose-5-phosphate
at pH 7.5 and 25°C
2.75
D-ribose-5-phosphate
pH 7.5
0.0056
D-xylulose 5-phosphate
-
wild-type, pH 6.7, 25°C
0.011
D-xylulose 5-phosphate
-
pH 7.6, 22°C
0.011
D-xylulose 5-phosphate
-
wild-type, pH 7.8, 25°C
0.015
D-xylulose 5-phosphate
-
mutant C160A, pH 7.8, 25°C
0.02
D-xylulose 5-phosphate
-
mutant C160D, pH 8.5, 25°C
0.021
D-xylulose 5-phosphate
-
pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Ca2+
0.023
D-xylulose 5-phosphate
-
H263A
0.025
D-xylulose 5-phosphate
-
-
0.025
D-xylulose 5-phosphate
-
and second value 0.773 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication
0.033
D-xylulose 5-phosphate
-
mutant C160S, pH 7.9, 25°C
0.034
D-xylulose 5-phosphate
-
wild-type, pH 8.5, 25°C
0.038
D-xylulose 5-phosphate
-
-
0.0399
D-xylulose 5-phosphate
-
wild-type
0.04
D-xylulose 5-phosphate
-
presence of 1 mM D-ribose 5-phosphate, pH 7.6, temperature not specified in the publication
0.065
D-xylulose 5-phosphate
-
mutant C160E, pH 7.6, 25°C
0.067
D-xylulose 5-phosphate
-
-
0.07
D-xylulose 5-phosphate
-
wild-type
0.073
D-xylulose 5-phosphate
wild-type
0.075
D-xylulose 5-phosphate
-
pH 7.6, temperature not specified in the publication
0.1
D-xylulose 5-phosphate
-
presence of 2 mM D-ribose 5-phosphate, pH 7.6, temperature not specified in the publication
0.115
D-xylulose 5-phosphate
-
pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Mg2+
0.115
D-xylulose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Mg2+
0.12
D-xylulose 5-phosphate
-
(+ D-ribose 5-phosphate)
0.12
D-xylulose 5-phosphate
with excess D-erythrose 4-phosphate as cosubstrate, at pH 7.5 and 37°C
0.145
D-xylulose 5-phosphate
wild type enzyme, with D-erythrose 4-phosphate as cosubstrate, at pH 8.0 and 25°C
0.15
D-xylulose 5-phosphate
-
(+ D-ribose 5-phosphate)
0.15
D-xylulose 5-phosphate
-
isoform TKTc, at pH 7.5 and 55°C
0.16
D-xylulose 5-phosphate
-
-
0.163
D-xylulose 5-phosphate
R359A
0.17
D-xylulose 5-phosphate
with excess D-erythrose 4-phosphate as cosubstrate, at pH 7.5 and 37°C
0.18
D-xylulose 5-phosphate
-
(+ D-ribose 5-phosphate)
0.18
D-xylulose 5-phosphate
with excess D-erythrose 4-phosphate as cosubstrate, at pH 7.5 and 37°C
0.183
D-xylulose 5-phosphate
wild type enzyme, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C
0.2
D-xylulose 5-phosphate
-
pH 7.5, 22°C
0.2
D-xylulose 5-phosphate
-
presence of 5 mM D-ribose 5-phosphate, pH 7.6, temperature not specified in the publication
0.21
D-xylulose 5-phosphate
-
-
0.21
D-xylulose 5-phosphate
-
0.21
D-xylulose 5-phosphate
-
(+ D-ribose 5-phosphate)
0.23
D-xylulose 5-phosphate
-
isoform TKTp, at pH 7.7 and 55°C
0.232
D-xylulose 5-phosphate
mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C
0.255
D-xylulose 5-phosphate
recombinant enzyme, pH 7.6, 30°C
0.27
D-xylulose 5-phosphate
with excess D-ribose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.29
D-xylulose 5-phosphate
with excess D-ribose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.303
D-xylulose 5-phosphate
His-tagged recombinant enzyme, pH 7.6, 30°C
0.318
D-xylulose 5-phosphate
R528A
0.4
D-xylulose 5-phosphate
-
H69A
0.4
D-xylulose 5-phosphate
pH 7.6, 37°C
0.41
D-xylulose 5-phosphate
-
presence of 10 mM D-ribose 5-phosphate, pH 7.6, temperature not specified in the publication
0.44
D-xylulose 5-phosphate
-
(+ D-ribose 5-phosphate)
0.4579
D-xylulose 5-phosphate
-
R433A
0.49
D-xylulose 5-phosphate
-
-
0.5
D-xylulose 5-phosphate
-
pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Ca2+
0.517
D-xylulose 5-phosphate
mutant enzyme R356L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C
0.595
D-xylulose 5-phosphate
D477A
0.68
D-xylulose 5-phosphate
mutant enzyme R525L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C
0.75
D-xylulose 5-phosphate
with excess D-ribose 5-phosphate as cosubstrate, at pH 7.5 and 37°C
0.773
D-xylulose 5-phosphate
-
and first value 0.025 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication
0.829
D-xylulose 5-phosphate
H469A
1.01
D-xylulose 5-phosphate
-
H30A
1.24
D-xylulose 5-phosphate
-
H481A
3.35
D-xylulose 5-phosphate
-
H481S
4.08
D-xylulose 5-phosphate
-
H481Q
0.61
fructose 6-phosphate
-
1.1
fructose 6-phosphate
-
-
1.8
fructose 6-phosphate
-
-
1.8
fructose 6-phosphate
-
1.8
fructose 6-phosphate
-
(+ ribose 5-phosphate)
3.2
fructose 6-phosphate
-
-
7
fructose 6-phosphate
-
-
11
fructose 6-phosphate
-
-
14
glycolaldehyde
-
-
35
glycolaldehyde
-
wild-type, in the presence of 50 mM hydroxypyruvate
200
glycolaldehyde
-
mutant A29E, in the presence of 50 mM hydroxypyruvate
4.78
Hydroxypyruvate
-
-
5.3
Hydroxypyruvate
-
wild-type, in the presence of 50 mM glycolaldehyde
6.6
Hydroxypyruvate
-
mutant A29E, in the presence of 50 mM glycolaldehyde
4.9
L-erythrulose
-
cosubstrate glyceraldehyde 3-phosphate
5.2
L-erythrulose
at pH 7.5 and 25°C
8
L-erythrulose
at pH 7.5 and 50°C
55
propionaldehyde
-
mutant D469T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
140
propionaldehyde
-
wild-type, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.031
sedoheptulose 7-phosphate
wild type enzyme, at pH 8.0 and 25°C
0.294
sedoheptulose 7-phosphate
mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C
4
sedoheptulose 7-phosphate
-
-
0.0003
thiamine diphosphate
-
H481A
0.0004
thiamine diphosphate
-
in the presence of Mg2+
0.0005
thiamine diphosphate
H469A
0.0005
thiamine diphosphate
-
H30N, H418S
0.0006
thiamine diphosphate
-
wild-type
0.0006
thiamine diphosphate
wild-type
0.0007
thiamine diphosphate
-
H481Q
0.0008
thiamine diphosphate
-
H30A
0.0012
thiamine diphosphate
D477A
0.0012
thiamine diphosphate
-
H263A
0.0018
thiamine diphosphate
-
H69A
0.0019
thiamine diphosphate
R359A
0.0024
thiamine diphosphate
R528A
0.0054
thiamine diphosphate
-
-
0.007
thiamine diphosphate
-
-
0.0365
Xylulose 5-phosphate
-
KM for the first active center of transketolase in the presence of Ca2+
0.16
Xylulose 5-phosphate
-
KM for the second active center of transketolase in the presence of Ca2+
additional information
additional information
-
kinetic data concerning the lag phase of transketolase reaction
-
additional information
additional information
-
modeling and simulation of the reaction. Among six kinetic parameters that govern the performance of the reaction, the modification of the MichaelisMenten constant for glycolaldehyde, inhibition constant for beta-hydroxypyruvate and the rate of reaction result in a positive effect on the performance of the reaction. An increase of inhibition constant for beta-hydroxypyruvate by 10fold yields a 35% increase in the level of achieved conversion. A 10fold decrease in Michaelis-Menten constant for glycolaldehyde has similar results, 36%. A 10fold increase of the rate of reaction results in almost 150% increase in the achievable product concentration
-
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0.0012
-
mutant R520I, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.0014
-
mutant S188T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.0018
-
mutant S188R, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.002
-
mutant D259Stop, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.007
-
mutant H461Y, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.008
-
mutant H100A and mutant H100V, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.0086
-
mutant R520G, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.009
-
mutant R520P, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.013
-
mutant H461Q, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.02
-
mutant D469S, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.022
-
mutant S188Q, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.025
-
mutant H26V, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.027
-
mutant A29D, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.028
-
mutant H100I and mutant H26V, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.029
-
wild-type, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.036
-
mutant H26K, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.04
-
mutant H461S, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0. Mutant D469Y, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehydee, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.043
-
mutant R358P, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.05
-
mutant D259G, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.055
-
mutant R358I, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.063
-
mutant H26T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.066
-
mutant D259A and mutant H26A, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.09
-
mutant H100V, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.1
-
mutant A29E, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.11
-
mutant S188R, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.12
-
mutant D259Stop, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.125
-
mutant D469A, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.127
-
mutant D469Y, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.13
-
mutant H100A and mutant S188T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.16
-
mutant H26T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.26
-
mutant H26A, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.31
-
mutant H26K, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.42
-
mutant R520I, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.43
-
mutant D469S, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.48
-
mutant H461Y, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.52
-
mutant H461Q, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.61
-
mutant D469A, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehydee, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.65
-
wild-type, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.77
-
crude extract with 4 mg/l added thiamine
1
-
mutant R358P, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.3
-
mutant D259G, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.37
-
mutant R358I, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.4
-
mutant R520G, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.95
-
mutant A29E, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
21.8
-
mutant C160S, pH 7.9, 25°C
3.14
-
mutant H461S, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
30.1
-
mutant C160D, pH 8.5, 25°C
5.5
recombinant enzyme, pH 7.6, 30°C
9.5
-
mutant C160E, pH 7.6, 25°C
0.14
-
mutant D469T, mutant R520V and mutant R520Stop, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.14
-
mutant R520Stop, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.37
-
mutant D469T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
0.37
-
crude extract without thiamine addition
0.88
-
mutant H100I, in the presence of 50 mM Li-hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.5
-
mutant D259A, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.5
-
mutant R520P, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.5
-
mutant S188Q, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.8
-
mutant A29D, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
1.8
using 10 mM D-glyceraldehyde 3-phosphate
2.3
-
mutant R520Stop, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
2.3
-
mutant R520V, in the presence of 50 mM hydroxypyruvate, 50 mM glycolaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0
2.7
-
mutant C160A, pH 7.8, 25°C
2.7
His-tagged recombinant enzyme, pH 7.6, 30°C
37
-
wild-type, pH 7.8, 25°C
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C160A
-
81% of wild-type activity
C160D
-
26% of wild-type activity
C160E
-
7% of wild-type activity
C160S
-
59% of wild-type activity
D259Stop
-
specific activity with propionaldehyde as substrate is lower than for wild-type
D381A
-
56fold less active than the wild-type enzyme. Shows significant destabilization of native and intermediate states of transketolase that can be monitored by changes in the urea denaturation transition mid-points (C1/2) measured by fluorescence
D469A
-
specific activity with propionaldehyde as substrate is 4.3fold greater than for wild-type
D469S
-
specific activity with propionaldehyde as substrate is lower than for wild-type
F434A
the mutation leads to 53% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal)
F434L
the mutation leads to 74% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H100A
-
specific activity with propionaldehyde as substrate is lower than for wild-type
H100F
the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H100I
-
has the same specific activity with propionaldehyde as substrate as the wild-type. Does not improve specific activity towards propionaldehyde
H100L
the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H100V
-
specific activity with propionaldehyde as substrate is lower than for wild-type
H100Y
the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A
the mutant shows about wild type activity with propionaldehyde and pyruvate
H192P/A282P/I365L/G506A/D469E
the mutant shows about 6.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/D469E/H473S
the mutant shows about 2fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L
the mutant shows about 2fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L/D469E
the mutant shows about 8fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L/D469E/R520Q
the mutant shows about 9fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L/D469T
the mutant shows about 1.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L/H473N
the mutant shows about 4fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H100L/H473S
the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H473N
the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H192P/A282P/I365L/G506A/H473S
the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H261A
the mutation leads to 75% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H261F
the mutation leads to 33% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H261G
the mutation leads to 59% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H261L
the mutation leads to 55% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H261V
the mutation leads to 65% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
H26K
-
specific activity with propionaldehyde as substrate is 1.2fold greater than for wild-type
H26T
-
specific activity with propionaldehyde as substrate is 2.2fold greater than for wild-type. 8.5fold improvement in specificity towards propionaldehyde relative to glycolaldehyde
H26V
-
has the same specific activity with propionaldehyde as substrate as the wild-type
H26W
the mutant shows an 8fold decreased formation of (R)-1,3-dihydroxy-2-heptanone and an ee-value of 30% (S) after 1 h reaction time
H461Q
-
specific activity with propionaldehyde as substrate is lower than for wild-type
H473N
the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
H473S
the mutant shows about 1.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
L116I
the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
L382A
the mutation leads to 97% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
L382A/F434A
the mutation leads to 66% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
L382A/F434L
the mutation leads to 10% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal
R358S
the mutant shows about 1.4fold increased activity with L-arabinose compared to the wild type enzyme
R520I
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520Y
the mutant shows about 2fold increased activity with L-arabinose compared to the wild type enzyme
S188R
-
specific activity with propionaldehyde as substrate is lower than for wild-type
S188T
-
specific activity with propionaldehyde as substrate is lower than for wild-type
S385E
-
the mutation completely removes the substrate inhibition for 3-formylbenzoic acid
S385E/D469T/R520Q
-
the mutant shows 350% activity with 3-formylbenzoic acid, 20% activity with 4-formylbenzoic acid and 600% activity activity with 3-hydroxybenzaldehyde compared to mutant enzyme D469T
S385T/D469T/R520Q
-
the mutant shows 50% activity with 3-formylbenzoic acid, 210% activity with 4-formylbenzoic acid and 1270% activity activity with 3-hydroxybenzaldehyde compared to mutant enzyme D469T
Y440A
-
700fold less active than the wild-type enzyme. Shows significant destabilization of native and intermediate states of transketolase that can be monitored by changes in the urea denaturation transition mid-points (C1/2) measured by fluorescence
D470T
-
the mutant shows slightly increased activity with benzaldehyde compared to the wild type enzyme
D477A
the mutant shows a kcat/KM value decrease for (2R)-hydroxylated aldehydes decrease by three orders of magnitude compared to the wild type enzyme
L191I/D470L
-
the mutant has an activity improvement of roughly 7.4fold compared to the wild type enzyme
L191V/D470
-
the mutant exhibits high 3R stereoselectivity as compared to the wild type enzyme
L191V/D470I
-
the mutant exhibits 74% 3R stereoselectivity and 5.8fold activity improvement as compared to the wild type enzyme
L191V/D470R
-
the mutant exhibits 84% 3R stereoselectivity as compared to the wild type enzyme
L382E/D470T
-
the mutant shows increased activity with benzaldehyde compared to the wild type enzyme
L382F/D470
-
the mutant has specific activity towards propanal 11 times higher than that of the wild type enzyme, with high yield of the 3S product
L382I/D470L
-
the mutant shows inversed stereoselectivity with low yield of the 3R product
L382N/D470S
-
the mutant shows strongly increased activity with benzaldehyde compared to the wild type enzyme
L382N/D470T
-
the mutant shows increased activity with benzaldehyde compared to the wild type enzyme
R102A
-
similar catalytyc activity like wild-type enzyme
R350A
-
lower activity than wild-type enzyme
R433A
-
lower activity than wild-type enzyme, less stable at 55°C than wild-type
R506A
-
lower activity than wild-type enzyme
E418A
-
about 0.12% of wild-type activity
H103A
-
mutantion does not affect affinity of the coenzyme to apoenzyme in presence of Ca2+, but affects all the kinetic parameters for coenzyme-apoenzyme interaction in presence of Mg2+. Acceleration of one-substrate reaction with slow-down of two-substrate reaction, kinetics
H30A
-
lower activity than wild-type enzyme
H30N
-
lower activity than wild-type enzyme
H469A
lower activity than wild-type enzyme
H481A
-
lower activity than wild-type enzyme
H481Q
-
lower activity than wild-type enzyme
H481S
-
lower activity than wild-type enzyme
H69A
-
lower activity than wild-type enzyme
R359A
lower activity than wild-type enzyme
R528A
lower activity than wild-type enzyme
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
A29D
-
specific activity is 2.7fold greater than for the wild-type
A29D
-
specific activity with propionaldehyde as substrate is lower than for wild-type
A29E
-
specific activity is 3fold greater than for the wild-type
A29E
-
specific activity with propionaldehyde as substrate is 3.4fold greater than for wild-type
D259A
-
specific activity is 2.3fold greater than for the wild-type
D259A
-
specific activity with propionaldehyde as substrate is 2.3fold greater than for wild-type
D259G
-
specific activity is 2fold greater than for the wild-type
D259G
-
specific activity with propionaldehyde as substrate is 1.7fold greater than for wild-type
D469E
-
formation of (3S)-1,3-dihydroxypentan-2-one in 90% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate
D469E
the mutant shows about 4.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme
D469T
-
specific activity with propionaldehyde as substrate is 4.9fold greater than for wild-type. 8.5fold improvement in specificity towards propionaldehyde relative to glycolaldehyde
D469T
-
formation of (3S)-1,3-dihydroxypentan-2-one in 64% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate
D469T
the mutant shows activities towards the three benzaldehyde analogues, 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde compared to the wild type enzyme
D469T
-
the mutant shows higher activity with 3-formylbenzoic acid and 4-formylbenzoic acid compared to the wild type enzyme
D469T/R520Q
-
the mutant shows 80% activity with 3-formylbenzoic acid, 50% activity with 4-formylbenzoic acid and no activity with 3-hydroxybenzaldehyde compared to mutant enzyme D469T
D469T/R520Q
the mutant shows improved activities towards the three benzaldehyde analogues, 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde compared to mutant enzyme D469T
D469Y
-
specific activity with propionaldehyde as substrate is 4.4fold greater than for wild-type. 64fold improvement in specificity towards propionaldehyde relative to glycolaldehyde
D469Y
-
formation of (3R)-1,3-dihydroxypentan-2-one in 53% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate
H26A
-
specific activity with propionaldehyde as substrate is 2.3fold greater than for wild-type
H26A
the mutation results in stereoinversion for the formation of 1,3-dihydroxy-2-heptanone, with a lower ee-value of 18% (R) as compared to the wild type enzyme
H26A/H261A
three hydrogen-bonding interactions between the active site and the 3-hydroxyl and 4-hydroxyl groups of the intermediate cannot be formed when compared to the wild-type
H26A/H261A
the mutation leads to 54% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal)
H26Y
-
formation of (3R)-1,3-dihydroxypentan-2-one in 88% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate
H26Y
the mutant catalyzes the formation of (R)-1,3-dihydroxy-2-heptanone with an ee-value of 98% and a yield of 8% after 1 h
H461S
-
specific activity is 4.8fold greater than for the wild-type
H461S
-
specific activity with propionaldehyde as substrate is 1.4fold greater than for wild-type
H461Y
-
specific activity with propionaldehyde as substrate is lower than for wild-type
H461Y
the mutant shows about 1.2fold increased activity with L-arabinose compared to the wild type enzyme
R358I
-
specific activity is 2.1fold greater than for the wild-type
R358I
-
specific activity with propionaldehyde as substrate is 1.9fold greater than for wild-type
R358I
the mutant shows about 1.2fold increased activity with L-arabinose compared to the wild type enzyme
R358P
-
specific activity is 1.5fold greater than for the wild-type
R358P
-
specific activity with propionaldehyde as substrate is 1.5fold greater than for wild-type
R358P
the mutant shows about 1.4fold increased activity with L-arabinose compared to the wild type enzyme
R520G
-
specific activity is 2.1fold greater than for the wild-type
R520G
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520P
-
specific activity is 2.3fold greater than for the wild-type
R520P
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520P
the mutant shows about 1.5fold increased activity with L-arabinose compared to the wild type enzyme
R520Stop
-
specific activity is 3.6fold greater than for the wild-type
R520Stop
-
specific activity with propionaldehyde as substrate is lower than for wild-type
R520V
-
specific activity is 3.6fold greater than for the wild-type
R520V
-
specific activity with propionaldehyde as substrate is 4.7fold greater than for wild-type
S188Q
-
specific activity is 2.3fold greater than for the wild-type
S188Q
-
specific activity with propionaldehyde as substrate is lower than for wild-type
S385Y/D469T/R520Q
-
the mutant shows 50% activity with 3-formylbenzoic acid, 340% activity with 4-formylbenzoic acid and 1240% activity activity with 3-hydroxybenzaldehyde compared to mutant enzyme D469T
S385Y/D469T/R520Q
the mutant shows improved activities towards the three benzaldehyde analogues, 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde compared to mutant enzyme D469T/R520Q
F435L/D470E
-
the mutant shows a large activity improvement (4.9fold) compared to the wild type enzyme
F435L/D470E
-
the mutant shows a roughly 4.9fold activity improvement compared to the wild type enzyme
L382D/D470S
the mutant leads up to 4 and 5fold higher activities towards L-lactaldehyde and L-glyceraldehyde, respectively, compared to the wild type enzyme
L382D/D470S
-
the mutant shows strongly increased activity with benzaldehyde compared to the wild type enzyme
D477A
-
lower activity than wild-type enzyme
D477A
lower activity than wild-type enzyme
H263A
-
-
H263A
-
lower activity than wild-type enzyme
additional information
-
deletion of tktA increases antibiotic and oxidative stress susceptibilities
additional information
on LB medium, tktB mutants show no growth defect. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
on LB medium, tktB mutants show no growth defect. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
-
on LB medium, tktB mutants show no growth defect. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
tktA mutants are slightly slower growing on LB medium. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
tktA mutants are slightly slower growing on LB medium. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
-
tktA mutants are slightly slower growing on LB medium. TktA tktB double mutant shows growth inhibition in LB medium comparable to that observed in tktA ppGpp null strains. DELTAtktB::kan mutation confers synthetic growth defects in the tktA mutant similar to that observed from ppGpp deficiency. PpGpp regulates transketolase B activity in the tktA relA256 mutant
additional information
-
in vitro induction of the expression by arabinose decreases the amount of recombinant enzyme isolated and lowers its specific activity
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