Literature summary for 2.2.1.7 extracted from

Brammer Basta, L.A.; Patel, H.; Kakalis, L.; Jordan, F.; Freel Meyers, C.L.
Defining critical residues for substrate binding to 1-deoxy-D-xylulose 5-phosphate synthase: active site substitutions stabilize the predecarboxylation intermediate C2alpha-lactylthiamin diphosphate (2014), FEBS J., 281, 2820-2837.

Search for more literature for 2.2.1.7

Cloned(Commentary)

Cloned (Comment)	Organism
mutant enzymes are expressed in Escherichia coli BL21(DE3) cells	Deinococcus radiodurans

Protein Variants

Protein Variants	Comment	Organism
R420A	thiamine diphosphate is significantly stabilized on the variant compared to the wild type enzyme in the absence of acceptor substrate. The substitution reduces affinity for D-glyceraldehyde 3-phosphate	Deinococcus radiodurans
R478A	thiamine diphosphate is significantly stabilized on the variant compared to the wild type enzyme in the absence of acceptor substrate. The substitution reduces affinity for D-glyceraldehyde 3-phosphate	Deinococcus radiodurans
Y392F	thiamine diphosphate is significantly stabilized on the variant compared to the wild type enzyme in the absence of acceptor substrate. The substitution reduces affinity for D-glyceraldehyde 3-phosphate	Deinococcus radiodurans

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0016	-	D-glyceraldehyde 3-phosphate	mutant enzyme R478A, at pH 8.0 and 37°C	Deinococcus radiodurans
0.0235	-	D-glyceraldehyde 3-phosphate	wild type enzyme, at pH 8.0 and 37°C	Deinococcus radiodurans
0.049	-	pyruvate	wild type enzyme, at pH 8.0 and 37°C	Deinococcus radiodurans
0.054	-	pyruvate	mutant enzyme R478A, at pH 8.0 and 37°C	Deinococcus radiodurans
0.073	-	pyruvate	mutant enzyme Y392F, at pH 8.0 and 37°C	Deinococcus radiodurans
0.21	-	D-glyceraldehyde 3-phosphate	mutant enzyme Y392F, 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	-	?

Organism

Organism	UniProt	Comment	Textmining
Deinococcus radiodurans	-	-	-

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	-	?

Synonyms

Synonyms	Comment	Organism
1-deoxy-D-xylulose 5-phosphate synthase	-	Deinococcus radiodurans
DXP synthase	-	Deinococcus radiodurans

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2.57	-	pyruvate	wild type enzyme, at pH 8.0 and 37°C	Deinococcus radiodurans
2.57	-	D-glyceraldehyde 3-phosphate	wild type enzyme, 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
0.03	-	D-glyceraldehyde 3-phosphate	mutant enzyme R420A, at pH 8.0 and 37°C	Deinococcus radiodurans
2.3	-	D-glyceraldehyde 3-phosphate	mutant enzyme R478A, at pH 8.0 and 37°C	Deinococcus radiodurans
15.1	-	D-glyceraldehyde 3-phosphate	mutant enzyme Y392F, at pH 8.0 and 37°C	Deinococcus radiodurans
53.3	-	pyruvate	wild type enzyme, at pH 8.0 and 37°C	Deinococcus radiodurans
113.3	-	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)