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Literature summary extracted from

  • White, J.K.; Handa, S.; Vankayala, S.L.; Merkler, D.J.; Woodcock, H.L.
    Thiamin diphosphate activation in 1-deoxy-D-xylulose 5-phosphate synthase insights into the mechanism and underlying intermolecular interactions (2016), J. Phys. Chem. B, 120, 9922-9934 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.7 D430A while the kcat for D430A mutant remains relatively unchanged, the KM for pyruvate and D-glyceraldehyde 3-phosphate increases 1.9 and 2.4times, respectively. The mutant shows 97.3% and 97.5% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively Deinococcus radiodurans
2.2.1.7 H304A the mutant produces a catalytically defective enzyme. The mutant shows 12.1% and 11.4% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively Deinococcus radiodurans
2.2.1.7 H434A the electrostatic effects that accompany the H434A mutation have a clear destabilizing effect on substrate binding while enhancing turnover. The mutant shows 133.8% and 121.5% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively Deinococcus radiodurans
2.2.1.7 H82A the mutant produces a catalytically defective enzyme. The mutant shows 5.1% and 4.7% catalytic efficiency for pyruvate and D-glyceraldehyde 3-phosphate, respectively Deinococcus radiodurans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.7 0.03
-
 D-glyceraldehyde 3-phosphate mutant enzyme H82A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 0.05
-
 D-glyceraldehyde 3-phosphate wild type enzyme, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 0.08
-
 D-glyceraldehyde 3-phosphate mutant enzyme H304A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 0.12
-
 D-glyceraldehyde 3-phosphate mutant enzyme D430A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 0.23
-
 D-glyceraldehyde 3-phosphate mutant enzyme H434A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 0.23
-
 pyruvate mutant enzyme H82A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 0.28
-
 pyruvate wild type enzyme, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 0.52
-
 pyruvate mutant enzyme D430A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 1.7
-
 pyruvate mutant enzyme H304A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 1.7
-
 pyruvate mutant enzyme H434A, at pH 8.0 and 37°C Deinococcus radiodurans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.2.1.7 pyruvate + D-glyceraldehyde 3-phosphate Deinococcus radiodurans
-
 1-deoxy-D-xylulose 5-phosphate + CO2
-
 ?
2.2.1.7 pyruvate + D-glyceraldehyde 3-phosphate Deinococcus radiodurans DSM 20539
-
 1-deoxy-D-xylulose 5-phosphate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.7 Deinococcus radiodurans Q9RUB5
-
-
2.2.1.7 Deinococcus radiodurans DSM 20539 Q9RUB5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.7 pyruvate + D-glyceraldehyde 3-phosphate
-
 Deinococcus radiodurans 1-deoxy-D-xylulose 5-phosphate + CO2
-
 ?
2.2.1.7 pyruvate + D-glyceraldehyde 3-phosphate
-
 Deinococcus radiodurans DSM 20539 1-deoxy-D-xylulose 5-phosphate + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.2.1.7 DXS
-
 Deinococcus radiodurans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.2.1.7 0.37
-
 D-glyceraldehyde 3-phosphate mutant enzyme H82A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 0.38
-
 pyruvate mutant enzyme H82A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 0.9
-
 pyruvate mutant enzyme H304A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 0.9
-
 D-glyceraldehyde 3-phosphate mutant enzyme H304A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 7.2
-
 pyruvate mutant enzyme D430A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 7.4
-
 pyruvate wild type enzyme, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 7.7
-
 D-glyceraldehyde 3-phosphate mutant enzyme D430A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 7.9
-
 D-glyceraldehyde 3-phosphate wild type enzyme, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 9.6
-
 D-glyceraldehyde 3-phosphate mutant enzyme H434A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 9.9
-
 pyruvate mutant enzyme H434A, at pH 8.0 and 37°C Deinococcus radiodurans

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.7 thiamine diphosphate
-
 Deinococcus radiodurans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.2.1.7 0.58
-
 pyruvate mutant enzyme H304A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 1.7
-
 pyruvate mutant enzyme H82A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 4.2
-
 D-glyceraldehyde 3-phosphate mutant enzyme H434A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 5.9
-
 pyruvate mutant enzyme H434A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 6.6
-
 D-glyceraldehyde 3-phosphate mutant enzyme D430A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 11
-
 D-glyceraldehyde 3-phosphate mutant enzyme H304A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 13
-
 D-glyceraldehyde 3-phosphate mutant enzyme H82A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 14
-
 pyruvate mutant enzyme D430A, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 26
-
 pyruvate wild type enzyme, at pH 8.0 and 37°C Deinococcus radiodurans
2.2.1.7 150
-
 D-glyceraldehyde 3-phosphate wild type enzyme, at pH 8.0 and 37°C Deinococcus radiodurans