Literature summary for 2.2.1.7 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 .

Search for more literature for 2.2.1.7

Protein Variants

Protein Variants	Comment	Organism
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
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
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
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Deinococcus radiodurans	Q9RUB5	-	-
Deinococcus radiodurans DSM 20539	Q9RUB5	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
DXS	-	Deinococcus radiodurans

Turnover Number [1/s]

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

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	-	Deinococcus radiodurans

kcat/KM [mM/s]

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

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Release 2023.1 (January 2023)