Deoxyribose-phosphate aldolase from Escherichia coli

Enzyme Description

Extremophile
No
EC Number

Sequence

Length: 259 amino acids
MTDLKASSLRALKLMDLTTLNDDDTDEKVIALCHQAKTPVGNTAAICIYPRFIPIARKTLKEQGTPEIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIKAGADFIKTSTGKVAVNATPESARIMMEVIRDMGVEKTVGFKPAGGVRTAEDAQKYLAIADELFGADWADARHYRFGASSLLASLLKALGHGDGKSASSY
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
8 measurements
Database ID
UniProt: P0A6L0 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 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 Methanol 20% 100 39 % 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 4 % 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 84 % 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 66 % 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 13 % 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 46 % 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 43 % 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.

Structure

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