Preliminary characterization of adenosine deaminase from Bacillus cereus.
Adenosine deaminase from Bacillus cereus is quite unstable, similarly to other bacterial deaminases, but it shows a peculiar stabilizing effect by some monovalent cations. These include K+, Li+, NH4+ and to a lesser extent Cs+. Maximal stabilization of the deaminase is exerted by K+ at concentrations higher than 20 mM. The enzyme can be rapidly inactivated by sulphydryl reagents such as p-hydroxymercuribenzoate. Since adenosine deaminase from B. cereus, in addition to monovalent cations, is stabilized also by dithiothreitol, a possible influence of monovalent cations on the reactivity of some sulphydryl groups on the enzyme has been suggested.
D000243:Adenosine Deaminase / Q000378:metabolism*; D000818:Animals; D001409:Bacillus cereus / Q000201:enzymology*; D002122:Calcium Chloride / Q000494:pharmacology; D002417:Cattle; D006902:Hydroxymercuribenzoates / Q000494:pharmacology; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D015636:Magnesium Chloride; D009700:Nucleoside Deaminases / Q000378:metabolism*; D011189:Potassium Chloride / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013997:Time Factors
D006902:Hydroxymercuribenzoates; D015636:Magnesium Chloride; D012965:Sodium Chloride; D011189:Potassium Chloride; D009700:Nucleoside Deaminases; D000243:Adenosine Deaminase; D008274:Magnesium; D002122:Calcium Chloride