Deoxyribose-phosphate aldolase from Rhodococcus erythropolis DSM 311
Enzyme Description
Sequence
MSEAALTRSQVAAMVDHTLLKPEATAADVTALIDEARSLGVLAVCVSPSMLPIRADGLVTAAVVGFPSGKHHSLVKGAEARLAVDQGATEIDMVIDVGAAVAGDYSAVLADILTVREAMGESAILKVILETAALSDEAIVECCRAAVRAGANFVKTSTGFHPAGGATVEAVELMARTVGPGVGVKASGGIRTTQAALDMIAAGATRLGLSGTRAVLDGLTD
Irene Kullartz et al. (2012)
β Cloning and characterisation of a new 2-deoxy-d-ribose-5-phosphate aldolase from Rhodococcus erythropolis
Journal of Biotechnology
Β· doi:10.1016/j.jbiotec.2011.12.018 β
Β· Activity - Classical
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Database ID
UniProt: C0ZUQ6 β
Sequence Annotation
Explicit - Provided GenBank Accession Number
Protein Source
Recombinant, host bacterium Escherichia coli BL21 (DE3)
Experimental Data (8 measurements)
8 measurements
| Property | Assay | Solvent | Solvent Volume | Aqueous Reference | Measured Value | Units | Solution | pH | Temperature | Substrate(s) | Product(s) | Cofactor(s) | Shaking | Comments |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Activity - Classical | Activity measured by absorbance spectrophotometry (NADH absorbance measurement, from glycerol-3-phosphate dehydrogenase-catalyzed reaction usign dihydroxyacetone phosphate as substrate, itself obtained the product of the triose-phosphate isomerase-catalyzed reaction with glyceraldehyde 3-phosphate, 340 nm) in the presence of organic solvent | Tetrahydrofuran (THF) | 20% | 100 | 2 | % | 100 mM potassium phosphate buffer, 4 U GDH, 11 U TPI, 0.1 mM NADH | 7 | 25Β°C | 0.4 mM 2-Deoxy-D-ribose 5-phosphate | Acetaldehyde , Glyceraldehyde 3-phosphate | β | β | Classical aqueous control (in %) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (NADH absorbance measurement, from glycerol-3-phosphate dehydrogenase-catalyzed reaction usign dihydroxyacetone phosphate as substrate, itself obtained the product of the triose-phosphate isomerase-catalyzed reaction with glyceraldehyde 3-phosphate, 340 nm) in the presence of organic solvent | Methanol | 20% | 100 | 60 | % | 100 mM potassium phosphate buffer, 4 U GDH, 11 U TPI, 0.1 mM NADH | 7 | 25Β°C | 0.4 mM 2-Deoxy-D-ribose 5-phosphate | Acetaldehyde , Glyceraldehyde 3-phosphate | β | β | Classical aqueous control (in %) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (NADH absorbance measurement, from glycerol-3-phosphate dehydrogenase-catalyzed reaction usign dihydroxyacetone phosphate as substrate, itself obtained the product of the triose-phosphate isomerase-catalyzed reaction with glyceraldehyde 3-phosphate, 340 nm) in the presence of organic solvent | Acetonitrile | 20% | 100 | 0 | % | 100 mM potassium phosphate buffer, 4 U GDH, 11 U TPI, 0.1 mM NADH | 7 | 25Β°C | 0.4 mM 2-Deoxy-D-ribose 5-phosphate | Acetaldehyde , Glyceraldehyde 3-phosphate | β | β | Classical aqueous control (in %) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (NADH absorbance measurement, from glycerol-3-phosphate dehydrogenase-catalyzed reaction usign dihydroxyacetone phosphate as substrate, itself obtained the product of the triose-phosphate isomerase-catalyzed reaction with glyceraldehyde 3-phosphate, 340 nm) in the presence of organic solvent | Dimethyl Sulfoxide (DMSO) | 20% | 100 | 92 | % | 100 mM potassium phosphate buffer, 4 U GDH, 11 U TPI, 0.1 mM NADH | 7 | 25Β°C | 0.4 mM 2-Deoxy-D-ribose 5-phosphate | Acetaldehyde , Glyceraldehyde 3-phosphate | β | β | Classical aqueous control (in %) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (NADH absorbance measurement, from glycerol-3-phosphate dehydrogenase-catalyzed reaction usign dihydroxyacetone phosphate as substrate, itself obtained the product of the triose-phosphate isomerase-catalyzed reaction with glyceraldehyde 3-phosphate, 340 nm) in the presence of organic solvent | tert-Butyl Methyl Ether (MTBE) | 20% | 100 | 68 | % | 100 mM potassium phosphate buffer, 4 U GDH, 11 U TPI, 0.1 mM NADH | 7 | 25Β°C | 0.4 mM 2-Deoxy-D-ribose 5-phosphate | Acetaldehyde , Glyceraldehyde 3-phosphate | β | β | Classical aqueous control (in %) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (NADH absorbance measurement, from glycerol-3-phosphate dehydrogenase-catalyzed reaction usign dihydroxyacetone phosphate as substrate, itself obtained the product of the triose-phosphate isomerase-catalyzed reaction with glyceraldehyde 3-phosphate, 340 nm) in the presence of organic solvent | Isopropanol | 20% | 100 | 19 | % | 100 mM potassium phosphate buffer, 4 U GDH, 11 U TPI, 0.1 mM NADH | 7 | 25Β°C | 0.4 mM 2-Deoxy-D-ribose 5-phosphate | Acetaldehyde , Glyceraldehyde 3-phosphate | β | β | Classical aqueous control (in %) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (NADH absorbance measurement, from glycerol-3-phosphate dehydrogenase-catalyzed reaction usign dihydroxyacetone phosphate as substrate, itself obtained the product of the triose-phosphate isomerase-catalyzed reaction with glyceraldehyde 3-phosphate, 340 nm) in the presence of organic solvent | Ethyl Acetate | 20% | 100 | 55 | % | 100 mM potassium phosphate buffer, 4 U GDH, 11 U TPI, 0.1 mM NADH | 7 | 25Β°C | 0.4 mM 2-Deoxy-D-ribose 5-phosphate | Acetaldehyde , Glyceraldehyde 3-phosphate | β | β | Classical aqueous control (in %) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (NADH absorbance measurement, from glycerol-3-phosphate dehydrogenase-catalyzed reaction usign dihydroxyacetone phosphate as substrate, itself obtained the product of the triose-phosphate isomerase-catalyzed reaction with glyceraldehyde 3-phosphate, 340 nm) in the presence of organic solvent | Ethanol | 20% | 100 | 62 | % | 100 mM potassium phosphate buffer, 4 U GDH, 11 U TPI, 0.1 mM NADH | 7 | 25Β°C | 0.4 mM 2-Deoxy-D-ribose 5-phosphate | Acetaldehyde , Glyceraldehyde 3-phosphate | β | β | Classical aqueous control (in %) |
Visualization : Activity β Classical
One bar per measurement. Colour = solvent, shade = solvent volume.