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 (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 (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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli | |
Mg2+ | required | Deinococcus radiodurans |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Deinococcus radiodurans | - |
- |
- |
Escherichia coli | - |
- |
- |
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 | 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 | 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 | 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 | Comment | Organism |
---|---|---|
DXS | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
thiamine diphosphate | binding structure, overview | Escherichia coli | |
thiamine diphosphate | binding structure, overview | Deinococcus radiodurans |