Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.2.1.7 extracted from

  • Xiang, S.; Usunow, G.; Lange, G.; Busch, M.; Tong, L.
    Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis (2007), J. Biol. Chem., 282, 2676-2682.
    View publication on PubMed

Application

Application Comment Organism
drug development DXS is an attractive target for the development of antibiotics, antimalarials, and herbicides Escherichia coli
drug development DXS is an attractive target for the development of antibiotics, antimalarials, and herbicides Deinococcus radiodurans

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of the His-tagged enzyme in Escherichia coli, production of the selenomethionine enzyme form in Escherichia coli strain B834 Escherichia coli
overexpression of the His-tagged enzyme in Escherichia coli, production of the selenomethionine enzyme form in Escherichia coli strain B834 Deinococcus radiodurans

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type and selenomethionine-labeled enzyme in complex with cofactor thiamine diphosphate, mixing of protein solution with reservoir solution containing 150 mM NaCl, and 20% w/v PEG 6000 or PEG 8000, cryoprotection by 25% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.9 A resolution Deinococcus radiodurans
purified recombinant wild-type and selenomethionine-labeled enzyme in complex with cofactor thiamine diphosphate, protein solution is mixed with the reservoir solution containing 30% w/v PEG 3350 and 200 mM Na,K-tartrate and infected by a fungus, the enzyme crystallized only after in situ proteolysis by a fungal protease, cryoprotection by 25% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.4 A resolution Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Mg2+ required Deinococcus radiodurans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate + D-glyceraldehyde 3-phosphate Escherichia coli the enzyme is crucial in the isoprenoid pathway, catalyzing the first step of the 2C-methyl-D-erythritol-4-phosphate, MEP, DXS is also a crucial enzyme for the biosynthesis of isopentenyl diphosphate, thiamine, and pyridoxol 1-deoxy-D-xylulose 5-phosphate + CO2
-
?
pyruvate + D-glyceraldehyde 3-phosphate Deinococcus radiodurans the enzyme is crucial in the isoprenoid pathway, catalyzing the first step of the 2C-methyl-D-erythritol-4-phosphate, MEP, DXS is also a crucial enzyme for the biosynthesis of isopentenyl diphosphate, thiamine, and pyridoxol 1-deoxy-D-xylulose 5-phosphate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans
-
-
-
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzymes from Escherichia coli by nickel affinity and anion exchange chromatography, and gel filtration Escherichia coli
recombinant His-tagged enzymes from Escherichia coli by nickel affinity and anion exchange chromatography, and gel filtration Deinococcus radiodurans

Reaction

Reaction Comment Organism Reaction ID
pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2 active site structure Escherichia coli
pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2 active site structure Deinococcus radiodurans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + D-glyceraldehyde 3-phosphate
-
Escherichia coli 1-deoxy-D-xylulose 5-phosphate + CO2
-
?
pyruvate + D-glyceraldehyde 3-phosphate
-
Deinococcus radiodurans 1-deoxy-D-xylulose 5-phosphate + CO2
-
?
pyruvate + D-glyceraldehyde 3-phosphate the enzyme is crucial in the isoprenoid pathway, catalyzing the first step of the 2C-methyl-D-erythritol-4-phosphate, MEP, DXS is also a crucial enzyme for the biosynthesis of isopentenyl diphosphate, thiamine, and pyridoxol Escherichia coli 1-deoxy-D-xylulose 5-phosphate + CO2
-
?
pyruvate + D-glyceraldehyde 3-phosphate the enzyme is crucial in the isoprenoid pathway, catalyzing the first step of the 2C-methyl-D-erythritol-4-phosphate, MEP, DXS is also a crucial enzyme for the biosynthesis of isopentenyl diphosphate, thiamine, and pyridoxol Deinococcus radiodurans 1-deoxy-D-xylulose 5-phosphate + CO2
-
?

Subunits

Subunits Comment Organism
More secondary structure analysis, the enzyme possesses a three domain structure, the active site of DXS is located at the interface of domains I and II in the same monomer Escherichia coli
More secondary structure analysis, the enzyme possesses a three domain structure, the active site of DXS is located at the interface of domains I and II in the same monomer Deinococcus radiodurans

Synonyms

Synonyms Comment Organism
DXS
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate binding structure, overview Escherichia coli
thiamine diphosphate binding structure, overview Deinococcus radiodurans