Related Experiment Video
Updated: Jul 10, 2026

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties
F Sgarrella1, A Del Corso, M G Tozzi
1Istituto di Chimica Biologica, Facoltà di Farmacia, Università di Sassari, Italy.
Abstract:
Deoxyribose 5-phosphate aldolase was purified 41 times from Bacillus cereus induced by growth on deoxyribonucleosides. The purification procedure includes ammonium sulphate fractionation, gel filtration on Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel and preparative electrophoresis on 10% polyacrylamide gel. The enzyme is stable above pH 6.5, but is rapidly inactivated by sulfhydryl reagents. Being insensitive to EDTA, it may be considered as a Class I aldolase. Among a number of compounds tested (including some carboxylic acids, free and phosphorylated pentoses, nucleotides and nucleosides), none has been found to affect the enzyme activity. The enzyme appears to be dimeric, with a subunit Mr of 23,600. A Km of 4.4 x 10(-4) M was calculated for dRib 5-P.
Related Concept Videos
Glycolysis: Preparatory Phase
Base-Catalyzed Aldol Addition Reaction
Dehydration of Aldols to Enals: Base-Catalyzed Aldol Condensation
C–C Bond Formation: Aldol Condensation Overview
Acid-Catalyzed Aldol Addition Reaction
Production of Alcohol

