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Literature summary for 2.2.1.1 extracted from

  • 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 (2016), Protein Eng. Des. Sel., 29, 513-522 .
    View publication on PubMed
Search for more literature for 2.2.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Scheffersomyces stipitis

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Scheffersomyces stipitis

Protein Variants

Protein Variants Comment Organism
H261F inactive Scheffersomyces stipitis
H27A in the reaction with sedoheptulose 7-phosphate (backward) the mutant exhibits weaker activity relative to the wild type enzyme Scheffersomyces stipitis
R356L in the reaction with D-xylulose 5-phosphate (forward) the mutant exhibits weaker activity relative to the wild type enzyme Scheffersomyces stipitis
R525L in the reaction with D-xylulose 5-phosphate (forward) the mutant exhibits weaker activity relative to the wild type enzyme Scheffersomyces stipitis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.029
-
 D-fructose 6-phosphate wild type enzyme, at pH 8.0 and 25°C Scheffersomyces stipitis
0.031
-
 sedoheptulose 7-phosphate wild type enzyme, at pH 8.0 and 25°C Scheffersomyces stipitis
0.145
-
 D-xylulose 5-phosphate wild type enzyme, with D-erythrose 4-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
0.183
-
 D-xylulose 5-phosphate wild type enzyme, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
0.232
-
 D-xylulose 5-phosphate mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
0.294
-
 sedoheptulose 7-phosphate mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
0.517
-
 D-xylulose 5-phosphate mutant enzyme R356L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
0.68
-
 D-xylulose 5-phosphate mutant enzyme R525L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-ribose 5-phosphate + D-xylulose 5-phosphate Scheffersomyces stipitis
-
 sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
 r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate Scheffersomyces stipitis
-
 D-ribose 5-phosphate + D-xylulose 5-phosphate
-
 r

Organism

Organism UniProt Comment Textmining
Scheffersomyces stipitis P34736
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-NTA agarose resin column chromatography and Superdex S-200 gel filtration Scheffersomyces stipitis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
 Scheffersomyces stipitis D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
 r
D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
 Scheffersomyces stipitis D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
 r
D-ribose 5-phosphate + D-xylulose 5-phosphate
-
 Scheffersomyces stipitis sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
 r
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
 Scheffersomyces stipitis D-ribose 5-phosphate + D-xylulose 5-phosphate
-
 r

Subunits

Subunits Comment Organism
homodimer 2 * 74969, calculated from amino acid sequence Scheffersomyces stipitis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.35
-
 D-xylulose 5-phosphate mutant enzyme R356L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
0.53
-
 D-xylulose 5-phosphate mutant enzyme R525L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
18.02
-
 D-xylulose 5-phosphate wild type enzyme, with D-erythrose 4-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
18.56
-
 D-xylulose 5-phosphate mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
20.58
-
 sedoheptulose 7-phosphate mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
25.31
-
 D-xylulose 5-phosphate wild type enzyme, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
26.87
-
 D-fructose 6-phosphate wild type enzyme, at pH 8.0 and 25°C Scheffersomyces stipitis
28.642
-
 sedoheptulose 7-phosphate wild type enzyme, at pH 8.0 and 25°C Scheffersomyces stipitis

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
 Scheffersomyces stipitis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.66
-
 D-xylulose 5-phosphate mutant enzyme R356L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
0.78
-
 D-xylulose 5-phosphate mutant enzyme R525L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
70
-
 sedoheptulose 7-phosphate mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
80
-
 D-xylulose 5-phosphate mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
120
-
 D-xylulose 5-phosphate wild type enzyme, with D-erythrose 4-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
140
-
 D-xylulose 5-phosphate wild type enzyme, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C Scheffersomyces stipitis
910
-
 sedoheptulose 7-phosphate wild type enzyme, at pH 8.0 and 25°C Scheffersomyces stipitis
920
-
 D-fructose 6-phosphate wild type enzyme, at pH 8.0 and 25°C Scheffersomyces stipitis