title: Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties.
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.
authors.affiliation: Istituto di Chimica Biologica, Facoltà di Farmacia, Università di Sassari, Italy.
authors.forename: F
authors.initials: F
authors.lastname: Sgarrella
authors.forename: A
authors.initials: A
authors.lastname: Del Corso
authors.forename: M G
authors.initials: MG
authors.lastname: Tozzi
authors.forename: M
authors.initials: M
authors.lastname: Camici
mesh_terms: D000446:Aldehyde-Lyases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D001409:Bacillus cereus / Q000201:enzymology*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D013438:Sulfhydryl Compounds / Q000494:pharmacology
chemical_list: D013438:Sulfhydryl Compounds; D000446:Aldehyde-Lyases; C020019:deoxyribose-phosphate aldolase