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Literature summary for 2.2.1.7 extracted from

  • Brammer, L.A.; Smith, J.M.; Wade, H.; Meyers, C.F.
    1-Deoxy-D-xylulose 5-phosphate synthase catalyzes a novel random sequential mechanism (2011), J. Biol. Chem., 286, 36522-36531.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.2.1.7

Inhibitors

Inhibitors Comment Organism Structure
D-glyceraldehyde competitive inhibition with respect to pyruvate Escherichia coli
D-glyceraldehyde 3-phosphate substrate inhibition Escherichia coli
pyruvate substrate inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.023
-
 D-glyceraldehyde 3-phosphate pH 8.0, 37°C Escherichia coli
0.049
-
 pyruvate pH 8.0, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2 reaction follows a random sequential mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + D-glyceraldehyde 3-phosphate D-glyceraldehyde and pyruvate bind reversibly and independently Escherichia coli 1-deoxy-D-xylulose 5-phosphate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
DXP synthase
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information the most efficient turnover of substrates is observed in HEPES buffer, pH 8.0 Escherichia coli
2.6
-
 pyruvate pH 8.0, 37°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 the most efficient turnover of substrates is observed in HEPES buffer, pH 8.0 Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2
-
 D-glyceraldehyde pH 8.0, 37°C Escherichia coli